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1
Jovanovic, Jelena, Andrea Stefanovic, Milena Zuza, Sonja Jakovetic, Natasa Sekuljica, Branko Bugarski, and Zorica Knezevic-Jugovic. "Improvement of antioxidant properties of egg white protein enzymatic hydrolysates by membrane ultrafiltration." Chemical Industry 70, no. 4 (2016): 419–28. http://dx.doi.org/10.2298/hemind150506047j.
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The production of bioactive peptides from egg white proteins (EWPs) and their separation are emerging areas with many new applications. The objective of this study was to compare antioxidant activity of three distinct EWP hydrolysates and their peptide fractions prepared by membrane ultrafiltration using membranes with 30, 10 and 1 kDa molecular weight cut-off. The hydrolysates were obtained by thermal and ultrasound pretreated EWPs hydrolyzed with a bacterial protease, Alcalase. It appeared that the pretreatment significantly affected peptide profiles and antioxidant activity of the hydrolysates measured by ABTS, DPPH and FRAP methods. The hydrolysate prepared using Alcalase and ultrasound pretreatment at 40 kHz - 15 min has shown to be the most effective in scavenging both DPPH and ABTS radicals (28.10?1.38 and 79.44?2.31%, respectively). It has been noticed that this hydrolysate had a nutritionally more adequate peptide profile than the other hydrolysates with a much lower amount of peptides <1 kDa (11.19?0.53 %) and the greatest content of the peptide fraction in the molecular weight (MW) range of 1-10 kDa (28.80?0.07 %). This peptide fraction has been exactly showed the highest DPPH and ABTS antioxidant activity compared to all other fractions having a potential to be used as a functional food ingredient.
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Atef, Maryam, Yasmina Ait Chait, Seyed Mahdi Ojagh, Ali Mohammad Latifi, Mina Esmaeili, Riadh Hammami, and Chibuike C. Udenigwe. "Anti-Salmonella Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen (Huso huso) Using Commercial Enzymes." Nutrients 13, no. 8 (July 30, 2021): 2657. http://dx.doi.org/10.3390/nu13082657.
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This study investigated peptide fractions from fish skin collagen for antibacterial activity against Escherichia coli and Salmonella strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight <10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against E. coli, and Neutrase and papain hydrolysates showing the best activity against S. abony; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four Salmonella strains, including S. abony (NCTC 6017), S. typhimurium (ATCC 13311), S. typhimurium (ATCC 14028) and S. chol (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6–22 and 6–24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure–activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.
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Cournoyer, Aurore, Jacinthe Thibodeau, Laila Ben Said, Zain Sanchez-Reinoso, Sergey Mikhaylin, Ismail Fliss, and Laurent Bazinet. "How Discoloration of Porcine Cruor Hydrolysate Allowed the Identification of New Antifungal Peptides." Foods 11, no. 24 (December 14, 2022): 4035. http://dx.doi.org/10.3390/foods11244035.
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Porcine blood is an important by-product from slaughterhouses and an abundant source of proteins. Indeed, cruor, the solid part of blood, is mainly composed of hemoglobin. Its enzymatic hydrolysis with pepsin generates a diversity of peptides, particularly antimicrobials. One of the downsides of using these hydrolysates as food bio-preservatives is the color brought by the heme, which can be removed by discoloration. Nonetheless, the effects of this procedure on the antimicrobial peptide population have not been completely investigated. In this study, its impacts were evaluated on the final antibacterial and antifungal activities of a cruor hydrolysate. The results demonstrated that 38 identified and characterized peptides showed a partial or total decrease in the hydrolysate, after discoloration. Antifungal activities were observed for the raw and discolored hydrolysates: MICs vary between 0.1 and 30.0 mg/mL of proteins, and significant differences were detected between both hydrolysates for the strains S. boulardii, C. guilliermondii, K. marxianus, M. racemosus and P. chrysogenum. The raw hydrolysate showed up to 12 times higher antifungal activities. Hence, peptides with the highest relative abundance decrease after discoloration were synthesized and tested individually. In total, eight new antifungal peptides were characterized as active and promising. To our knowledge, this is the first time that effective antifungal peptide sequences have been reported from porcine cruor hydrolysates.
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Guo, Honghui, Zhuan Hong, and Guangyu Yan. "Collagen peptide chelated zinc nanoparticles from tilapia scales for zinc supplementation." International Food Research Journal 30, no. 2 (April 28, 2023): 386–97. http://dx.doi.org/10.47836/ifrj.30.2.10.
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Collagen peptide chelated zinc (CPCZ) nanoparticles were prepared using collagen peptide hydrolysate from tilapia scales. The nano-chelating ability of collagen peptide hydrolysates treated with ten enzymes was evaluated. Among these collagen peptide hydrolysates, trypsin hydrolysate exhibited the best nano-chelating ability. The molecular weight distribution of trypsin hydrolysate that produced CPCZ nanoparticles indicated that most of the peptides were less than 1,000 Da. These small molecular peptides with excellent nanozinc-chelating ability were chelated with zinc ions to form CPCZ nanoparticles. CPCZ nanoparticles were nearly spherical with an average diameter of approximately 100 nm, and a zinc content of 13.2%. Transmission electron microscopy coupled with energy dispersive spectroscopy and Fourier transform infrared spectrometry was used to measure the physicochemical properties of the CPCZ nanoparticles. Their cytotoxicity was also estimated by BHK21 cells. Result indicated that the CPCZ nanoparticles were non-toxic to BHK-21, and such nanoparticles significantly enhanced the survival of cells. The present work suggested that CPCZ nanoparticles could be used as zinc supplementation in the food and pharmaceutical industries.
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Phetchthumrongchai, Thithi, Viroj Tachapuripunya, Sutasinee Chintong, Sittiruk Roytrakul, Teerasak E-kobon, and Wanwimol Klaypradit. "Properties of Protein Hydrolysates and Bioinformatics Prediction of Peptides Derived from Thermal and Enzymatic Process of Skipjack Tuna (Katsuwonus pelamis) Roe." Fishes 7, no. 5 (September 24, 2022): 255. http://dx.doi.org/10.3390/fishes7050255.
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Currently, the use of skipjack tuna (Katsuwonus pelamis) roe to produce hydrolysate is limited, although it is a potentially valuable resource. This study aimed to investigate the physical and chemical characteristics of protein hydrolysates from tuna roe using autoclave and enzymes (alcalase and trypsin at 0.5 and 1.0% w/v). Bioinformatics was also applied to analyze the identified peptides. The hydrolysates were determined for amino acid composition, peptide profile patterns, antioxidant activity, solubility and foaming properties. The proteins were separated by SDS-PAGE before tryptic digestion and peptide identification by nano LC-ESI-MS/MS. The putative bioactivities of the identified peptides were predicted using bioinformatics prediction tools. The main amino acids found in all hydrolysates were cysteine, glycine and arginine (16.26–20.65, 10.67–13.61 and 10.87–12.08 g/100 g protein, respectively). The hydrolysates obtained from autoclaving showed lower molecular weights than those by the enzymatic method. The 0.1 g/mL concentration of hydrolysates provided higher antioxidant activities compared to the others. All hydrolysates had high solubility and exhibited foaming capacity and foam stability. Putative anti-hypertensive, anti-virus and anti-parasite activities were highly abundant within the obtained peptides. Moreover, predicted muti-bioactivity was indicated for seven novel peptides. In the future work, these peptides should be experimentally validated for further applications.
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Awosika, Temitola, and Rotimi E. Aluko. "Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors." Foods 8, no. 6 (June 10, 2019): 200. http://dx.doi.org/10.3390/foods8060200.
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In this work, we report the potency of enzymatic hydrolysates of pea proteins against trypsin and chymotrypsin. Pea protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the protein hydrolysates into peptide fractions (<1, 1–3, 3–5, and 5–10 kDa). Peptide size profiling with size-exclusion gel chromatography indicated the narrowest size range (0.85–4.98 kDa) for alcalase. Trypsin activity was strongly (p < 0.05) inhibited by the ultrafiltration fractions (mean IC50 = 2.2 mg/mL) obtained from the trypsin hydrolysate when compared to the unfractionated hydrolysate (IC50 = 6.8 mg/mL). Similarly, ultrafiltration also enhanced trypsin inhibition by the alcalase-digested peptides with an IC50 of 21.4 mg/mL for the unfractionated hydrolysate in comparison to 3.1–4.7 mg/mL for the fractions. However, ultrafiltration did not enhance trypsin inhibitory activity of chymotrypsin-digested peptides, while the peptide separation reduced efficacy of pepsin-digested peptides. In contrast, chymotrypsin inhibition by all the enzymatic digests was significantly (p < 0.05) enhanced by ultrafiltration, especially peptide sizes >3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage.
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Zhang, Jianan, Yang Liu, Liwen Jiang, Tiantian Zhao, Guowan Su, and Mouming Zhao. "Exploring the Release of Elastin Peptides Generated from Enzymatic Hydrolysis of Bovine Elastin via Peptide Mapping." Molecules 28, no. 22 (November 10, 2023): 7534. http://dx.doi.org/10.3390/molecules28227534.
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To enhance the understanding of enzymatic hydrolysis and to accelerate the discovery of key bioactive peptides within enzymatic products, this research focused on elastin as the substrate and investigated the variations in peptide profiles and the production of key bioactive peptides (those exceeding 5% of the total) and their impacts on the biological activity of the hydrolysates. Through the application of advanced analytical techniques, such as stop-flow two-dimensional liquid chromatography and ultra-high-performance liquid chromatography-tandem mass spectrometry, the research tracks the release and profiles of peptides within elastin hydrolysates (EHs). Despite uniform peptide compositions, significant disparities in peptide concentrations were detected across the hydrolysates, hinting at varying levels of bioactive efficacy. A comprehensive identification process pinpointed 403 peptides within the EHs, with 18 peptides surpassing 5% in theoretical maximum content, signaling their crucial role in the hydrolysate’s bioactivity. Of particular interest, certain peptides containing sequences of alanine, valine, and glycine were released in higher quantities, suggesting Alcalase® 2.4L’s preference for these residues. The analysis not only confirms the peptides’ dose-responsive elastase inhibitory potential but also underscores the nuanced interplay between peptide content, biological function, and their collective synergy. The study sets the stage for future research aimed at refining enzymatic treatments to fully exploit the bioactive properties of elastin.
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Rosida, Dedin Finatsiyatull, Teeradate Kongpichitchoke, Phattara-Orn Havanapan, Andre Yusuf Trisna Putra, and Anugerah Dany Priyanto. "Chemical and Sensory Evaluation of Umami Taste Derived from Proteolytic Hydrolysate of Pila ampullacea." Trends in Sciences 21, no. 1 (November 10, 2023): 6827. http://dx.doi.org/10.48048/tis.2024.6827.
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In this study, umami taste was produced and identified from bromelain and trypsin hydrolysate of Pila ampullacea (PA). The PA hydrolysates, obtained from individually bromelain and trypsin with various Enzyme-to-Substrate ratio (E/S) of 1/10, 1/20, and 1/100 (w/v) using divers proteolysis times (3, 6, 9, 12, 15 and 18 h), were evaluated their chemical properties by degree of hydrolysis (DH), total peptide content, and amino acid content. Two chosen proteolysis conditions of PA hydrolysates were concluded by sensory evaluation using hedonic test and principal component analysis (PCA). PA hydrolysate using bromelain with E/S of 1:10 (w/v) for 18 h was one of the 2 chosen proteolysis conditions, which had DH value of 56.56 ± 1.65 %, total peptide content of 10.89 ± 0.09 mg/mL, and amino acid content of 95.34 ± 0.12 ppm. On the other hand, the chosen from trypsin digestion used E/S of 1:10 (w/v) for 15 h, which had DH value of 49.71 ± 0.22 %, total peptide content of 6.44 ± 0.28 mg/mL, and amino acid content of 81.43 ± 1.29 ppm. PA hydrolysates were subjected to explain the released peptides using liquid chromatography-tandem mass spectrometry (LC-MS/MS) and database-assisted identification. There were many identified peptides contained in PA hydrolysates that contributed to umami taste. Their sequences from bromelain digestion were GPEGPQGPPGPRG, GIMLGAA, GLPGLPGLKGDPGEPGLP, GKDGEAG, GLVMDSCAGH, and EEKITEDDDAVGDDAENR. Several peptide fragments from trypsin digestion were GQTVIGL, GLPGLPGLSGPKG, DTGPAGPAGPAGPQGPR and QTLEKALSHVIQEFETEKQLITVNAR. HIGHLIGHTS Umami taste derived from proteolytic hydrolysate of Pila ampullacea was firstly reported The findings revealed that Pila ampullacea hydrolysates using bromelain with the Enzyme-to-Substrate ratio (E/S) 1:10 (w/v) for 18 h and trypsin with E/S of 1:10 (w/v) for 15 h had exhibited as the proficient treatment for hydrolysis conditions and selected based on sensory properties This new method will be of considerable advantage to the best practice of umami taste establishment as flavor enhancer in the food manufacture GRAPHICAL ABSTRACT
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Jafarpour, Ali, Simon Gregersen, Rocio Marciel Gomes, Paolo Marcatili, Tobias Hegelund Olsen, Charlotte Jacobsen, Michael Toft Overgaard, and Ann-Dorit Moltke Sørensen. "Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction." Marine Drugs 18, no. 12 (November 27, 2020): 599. http://dx.doi.org/10.3390/md18120599.
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Protein hydrolysates show great promise as bioactive food and feed ingredients and for valorization of side-streams from e.g., the fish processing industry. We present a novel approach for hydrolysate characterization that utilizes proteomics data for calculation of weighted mean peptide properties (length, molecular weight, and charge) and peptide-level abundance estimation. Using a novel bioinformatic approach for subsequent prediction of biofunctional properties of identified peptides, we are able to provide an unprecedented, in-depth characterization. The study further characterizes bulk emulsifying, foaming, and in vitro antioxidative properties of enzymatic hydrolysates derived from cod frame by application of Alcalase and Neutrase, individually and sequentially, as well as the influence of heat pre-treatment. All hydrolysates displayed comparable or higher emulsifying activity and stability than sodium caseinate. Heat-treatment significantly increased stability but showed a negative effect on the activity and degree of hydrolysis. Lower degrees of hydrolysis resulted in significantly higher chelating activity, while the opposite was observed for radical scavenging activity. Combining peptide abundance with bioinformatic prediction, we identified several peptides that are likely linked to the observed differences in bulk emulsifying properties. The study highlights the prospects of applying proteomics and bioinformatics for hydrolysate characterization and in food protein science.
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Bueno-Gavilá, Estefanía, Adela Abellán, Francisco Girón-Rodríguez, José María Cayuela, and Luis Tejada. "Bioactivity of Hydrolysates Obtained from Chicken Egg Ovalbumin Using Artichoke (Cynara scolymus L.) Proteases." Foods 10, no. 2 (January 26, 2021): 246. http://dx.doi.org/10.3390/foods10020246.
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The aim of this work was to obtain chicken egg ovalbumin hydrolysates using aspartic proteinases present in extracts from the artichoke flower (Cynara scolymus L.) and evaluate their antioxidant, antimicrobial, and angiotensin I-converting enzyme (ACE) inhibitory activity in vitro. Hydrolysis time and molecular weight (<3 kDa) had a significant influence on the hypertensive and antioxidant activity of the hydrolysates. The <3 kDa fraction of the 16 h hydrolysate had an ACE inhibitory activity with an IC50 of 64.06 µg peptides/mL. The fraction <3 kDa of ovalbumin hydrolysate at 2 h of hydrolysis showed a DPPH radical scavenging activity of 30.27 µM of Trolox equivalents/mg peptides. The fraction <3 kDa of the hydrolysate of 16 h had an ABTS+ caption activity of 4.30 mM of Trolox equivalents/mg peptides. The fraction <3 kDa of the hydrolysate of 2 h had an iron (II) chelating activity of 32.18 µg peptides/mL. From the peptide sequences identified in the hydrolysates, we detected four peptides (from the BIOPEP database) that were already in their bioactive form (IAAEVYEHTEGSTTSY, HLFGPPGKKDPV, PIAAEVYEHTEGSTTSY, and YAEERYPIL), and are reported to display antioxidant and ACE inhibitory activity.
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González-Osuna, María Fernanda, Wilfrido Torres-Arreola, Enrique Márquez-Ríos, Francisco Javier Wong-Corral, Eugenia Lugo-Cervantes, José Carlos Rodríguez-Figueroa, Guillermina García-Sánchez, et al. "Antioxidant Activity of Peptide Fractions from Chickpea Globulin Obtained by Pulsed Ultrasound Pretreatment." Horticulturae 9, no. 4 (March 23, 2023): 415. http://dx.doi.org/10.3390/horticulturae9040415.
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Protein hydrolysates and peptides can show biological activities, and pulsed ultrasound improves bioactivities. Among matrices from which protein hydrolysates can be obtain, chickpea is an excellent source. The objective of this research was to evaluate the effect of pulsed ultrasound on globulin concentrate to obtain chickpea hydrolysate (HGb) and peptide fractions and their bioactivity. Antioxidant activity by ABTS (2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt), FRAP (Ferric Reducing Antioxidant Power) and human erythrocyte assays was determined. The electrophoretic profile, amino acid profile, and antimicrobial activity of hydrolysates were also determined. Two hydrolysates had the highest antioxidant activity: HGb (91.44% ABTS inhibition, 73.04% hemolysis inhibition and 5185.57 µmol TE/g dried sample in FRAP assay) and HGb-20 (48.25% ABTS inhibition, 100% hemolysis inhibition and 2188.53 µmol TE/g dried sample in FRAP assay). Peptide fractions inhibited 100% of the hemolysis on human erythrocytes. The hydrolysates from chickpea proteins obtained with savinase have antioxidant activity through the SET and HAT mechanisms. The application of the obtained compounds for the development of functional foods or for food preservation should be considered.
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Fouchereau‐Peron, M., L. Duvail, C. Michel, A. Gildberg, I. Batista, and Y. Le Gal. "Isolation of an acid fraction from a fish protein hydrolysate with a calcitonin‐gene‐related‐peptide‐like biological activity." Biotechnology and Applied Biochemistry 29, no. 1 (February 1999): 87–92. http://dx.doi.org/10.1111/j.1470-8744.1999.tb01152.x.
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The possibility of obtaining calcitonin and/or calcitonin‐gene‐related peptide (CGRP) immunorelated molecules from partly digested proteins was investigated with fish and shrimp hydrolysates. These two peptides were quantified by both radioimmunoassay and radioreceptor assay; the positive extracts were partly purified. Different hydrolysates were analysed: cod head, stomach and viscera hydrolysates, a shrimp hydrolysate and two sardine hydrolysates. Although each cod extract interacted in the CGRP radioimmunoassay, none of these extracts was able to displace the CT binding to its antibody. In contrast, shrimp and sardine hydrolysates interacted with both radioimmunoassays. Radioreceptor assays performed on the same extracts demonstrated that only three extracts contained the structural determinants that allowed them to interact in the CGRP radioreceptor assay. No interaction with the calcitonin radioreceptor assay could be demonstrated. Molecular sieving of the two sardine extracts showed that the immunoreactivity was resolved into two main fractions. The higher‐molecular‐mass fraction interacted only in the CGRP radioreceptor assay. The results obtained suggest the presence of a biologically related CGRP molecule in peptone hydrolysates and requires further investigation into the role of these peptide fragments in the regulation of intestinal function by partly digested proteins.
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Bui, Phong T., Khoa T. Pham, and Tam D. L. Vo. "Earthworm (Perionyx excavatus) Protein Hydrolysate: Hypoglycemic Activity and Its Stability for the Hydrolysate and Its Peptide Fractions." Processes 11, no. 8 (August 19, 2023): 2490. http://dx.doi.org/10.3390/pr11082490.
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This study aims at exploring earthworm protein hydrolysate and its peptide fractions as a potential hypoglycemic agent by inhibiting α-amylase and α-glucosidase. Firstly, the best hydrolysis conditions to gain the hydrolysates with the highest α-amylase inhibitory activity (α-AIA) and α-glucosidase inhibitory activity (α-GIA) were figured out using a one-factor test. Next, the stability of the hypoglycemic activity of the hydrolysates and their 5 peptide fractions recovered using ultrafiltration membranes were assessed by employing the tests of in vitro digestion, thermal, and pH treatment. The results showed that at the best hydrolysis conditions, the hydrolysates exhibited α-AIA of 91.30 ± 2.51% and α-GIA of 44.69 ± 0.47%. Specifically, the <1 kDa peptide fraction from the hydrolysate expressed a greater α-AIA than that of acarbose, with nearly the same α-GIA as that of voglibose. The α-AIA and α-GIA of the hydrolysates and their fractions were enhanced after the in vitro digestion treatment, whereas they remained over 40% after the pH treatment in the range of 1 to 11 or heat treatment at 100 °C for 180 min. These data provide the preliminary evidence to develop the earthworm protein hydrolysate and its peptide fractions in functional food or nutraceutical products with hypoglycemic activity.
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Ovsyannikov, Yuriy S., and Maxim S. Dursenev. "Comparative evaluation of nutrient media based on protein hydrolysates." Veterinariya, Zootekhniya i Biotekhnologiya 9, no. 118 (2023): 52–58. http://dx.doi.org/10.36871/vet.zoo.bio.202309006.
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The problem of the choice of protein raw materials and the method of its hydrolysis for the creation of new protein hydrolysates has not yet lost its relevance. The purpose of the work: to study the peculiarities of obtaining enzymatic and acid hydrolysates of embryonic mass, vaccine production waste and to conduct a comparative assessment of the effect of the hydrolysis method on the physico-chemical characteristics, peptide and amino acid composition of the resulting hydrolysates. To obtain hydrolysates, 12-day-old chicken embryos were used as raw materials, after sucking off the virus-containing allantois fluid, are waste products of anti-influenza medication. As hydrolyzing agents, the pancreatic glands of cattle State Standart 11285-93 were used for enzymatic hydrolysis, and synthetic hydrochloric acid State Standart 857-95 was used for acid hydrolysis. It was found that the degree of cleavage in all hydrolysates is average. The content of total and amine nitrogen in the enzyme and initial acid hydrolysates is in the same range, and the values of the same indicators in the acid deionized hydrolysate are significantly less. This is due to the dilution of the hydrolysate during deionization and does not affect its quality. In the studied hydrolysates, the presence of peptides of different molecular weights was noted: in the enzyme hydrolysate, the content of peptides with a molecular weight of 1000 to 2000 Daltons is almost 2.5 times greater than in the acidic one, the level of free amino acids is also higher in the enzyme hydrolysate, and peptides with a molecular weight of 500 to 1000 Daltons in it is 6 times less. The data of the amino acid profile of hydrolysates indicates that the total amount of amino acids in both hydrolysates does not differ significantly. However, all the essential amino acids are present in the enzymatic hydrolysate, and there is no proline and tryptophan in the acid hydrolysate. Thus, the enzymatic and acidic hydrolysis method makes it possible to effectively break down the protein of the embryonic mass and obtain final products with an average degree of protein cleavage. However, the distribution of peptides by fractions and the amino acid composition of hydrolysates varies from the method of its preparation. This circumstance should be taken into account when designing nutrient media for a particular microorganism, taking into account its needs.
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Zhang, Xiaogang, Parinya Noisa, and Jirawat Yongsawatdigul. "Chemical and Cellular Antioxidant Activities of In Vitro Digesta of Tilapia Protein and Its Hydrolysates." Foods 9, no. 6 (June 25, 2020): 833. http://dx.doi.org/10.3390/foods9060833.
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Production of protein hydrolysate as nutraceuticals is typically based on the activity of the hydrolysate, which might not yield the optimal activity under physiological condition due to structural modification of peptides upon gastrointestinal (GI) digestion. This study systematically compared the chemical and cellular antioxidant activities of the in vitro digesta of tilapia protein and its hydrolysates prepared with various degree of hydrolysis (DH) by Alcalase. The enzymes used in the in vitro GI digestion analysis significantly contributed to the peptide content, Trolox equivalent antioxidant capacity (TEAC), and oxygen radical absorbance capacity (ORAC). Proteins and all hydrolysates were slightly digested by pepsin but hydrolyzed extensively by pancreatin. Both hydrolysate and digesta predominantly scavenged free radicals via hydrogen atom transfer (HAT). The antioxidant activities of the hydrolysates increased with the increasing DH up to 16 h of hydrolysis. However, the digesta of 10-h hydrolysate displayed the highest chemical and HepG2 cellular antioxidant activities, while the protein digesta displayed the lowest. Principal component analysis (PCA) showed that the TEAC of the digesta was positively correlated with the cellular antioxidant activity (CAA). Therefore, the production of protein hydrolysate should be optimized based on the activity of the hydrolysate digesta rather than that of hydrolysates.
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Hayes, Maria, and Leticia Mora. "Alternative Proteins as a Source of Bioactive Peptides: The Edible Snail and Generation of Hydrolysates Containing Peptides with Bioactive Potential for Use as Functional Foods." Foods 10, no. 2 (January 30, 2021): 276. http://dx.doi.org/10.3390/foods10020276.
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Members of the Phylum Mollusca include shellfish such as oysters and squid but also the edible garden snail known as Helix aspersa. This snail species is consumed as a delicacy in countries including France (where they are known as petit-gris), southern Spain (where they are known as Bobe), Nigeria, Greece, Portugal and Italy but is not a traditional food in many other countries. However, it is considered an excellent protein source with a balanced amino acid profile and an environmentally friendly, sustainable protein source. The aim of this work was to develop a different dietary form of snail protein by generating protein hydrolysate ingredients from the edible snail using enzyme technology. A second aim was to assess the bioactive peptide content and potential health benefits of these hydrolysates. H. aspersa hydrolysates were made using the enzyme Alcalase® and the nutritional profile of these hydrolysates was determined. In addition, the bioactive peptide content of developed hydrolysates was identified using mass spectrometry. The potential heart health benefits of developed snail hydrolysates were measured in vitro using the Angiotensin-I-converting Enzyme (ACE-1; EC 3.4.15.1) inhibition assay, and the ACE-1 inhibitory drug Captopril© was used as a positive control. The generated H. aspersa hydrolysates were found to inhibit ACE-1 by 95.60% (±0.011) when assayed at a concentration of 1 mg/mL (n = 9) compared to the positive control Captopril© which inhibited ACE-1 by 96.53% (±0.0156) when assayed at a concentration of 0.005 mg/mL (n = 3). A total of 113 unique peptide sequences were identified following MS analysis with peptides identified ranging from 628.35 Da (peptide GGGLVGGI—protein accession number sp|P54334|XKDO_BACSU) to 2343.14 Da (peptide GPAGVPGLPGAKGDHGFPGSSGRRGD—protein accession number sp|Q7SIB2|CO4A1_BOVIN) in size using the BIOPEP-UWM database.
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Ningrum, Andriati, Dian Wahyu Wardani, Nurul Vanidia, Manikharda, Achmat Sarifudin, Rima Kumalasari, Riyanti Ekafitri, Dita Kristanti, Woro Setiaboma, and Heli Siti Helimatul Munawaroh. "Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction." Molecules 28, no. 13 (June 24, 2023): 4974. http://dx.doi.org/10.3390/molecules28134974.
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Okara is a solid byproduct created during the processing of soy milk. The production of protein hydrolysates utilizing enzymatic tests such as papain can result in the production of bioactive peptides (BPs), which are amino acid sequences that can also be produced from the okara protein by hydrolysis. The objective of this study was to investigate the antioxidant activities of okara hydrolysates using papain, based on the in silico and in vitro assays using the papain enzyme. We found that using the in silico assessment, the antioxidant peptides can be found from the precursor (glycinin and conglycinin) in okara. When used as a protease, papain provides the maximum degree of hydrolysis for antioxidative peptides. The highest-peptide-rank peptide sequence was predicted using peptide ranks such as proline–histidine–phenylalanine (PHF), alanine–aspartic acid–phenylalanine (ADF), tyrosine–tyrosine–leucine (YYL), proline–histidine–histidine (PHH), isoleucine–arginine (IR), and serine–valine–leucine (SVL). Molecular docking studies revealed that all peptides generated from the parent protein impeded substrate access to the active site of xanthine oxidase (XO). They have antioxidative properties and are employed in the in silico approach to the XO enzyme. We also use papain to evaluate the antioxidant activity by using in vitro tests for protein hydrolysate following proteolysis. The antioxidant properties of okara protein hydrolysates have been shown in vitro, utilizing DPPH and FRAP experiments. This study suggests that okara hydrolysates generated by papain can be employed as natural antioxidants in food and for further applications, such as active ingredients for antioxidants in packaging.
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Silvestre, Marialice P. C., Wendel O. Afonso, Carlos O. Lopes Junior, Viviane D. M. Silva, Mariana W. S. Souza, and Mauro R. Silva. "Effect of Some Hydrolytic Parameters in the Action of Subtilisin and Pancreatin on Whey Protein Concentrate." International Journal of Food Engineering 9, no. 1 (June 8, 2013): 55–66. http://dx.doi.org/10.1515/ijfe-2012-0158.
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AbstractIn this work, the influence of some reactional parameters in the hydrolysis of whey protein concentrate (WPC) was evaluated, in terms of the nutritional quality of peptide profiles of the hydrolysates as well as the reduction of costs for scaling-up the process. Two enzymes (subtilisin and pancreatin) were used for preparing 18 hydrolysates, using different E:S ratios and reaction times, and the distribution of peptides according to chain length was analyzed by size-exclusion chromatography. The studied parameters affected the peptide profiles of WPC hydrolysates and the best result was similar for subtilisin and pancreatin, both using an E:S ratio of 4:100, after 5 h and 10 h, respectively. In these conditions, these enzymes gave rise to the smallest large peptide contents (12.28% and 12.34%, respectively) and one of the highest amount of di- and tripeptides (13.34% and 13.00%, respectively) as well as of free amino acids (45.56% and 47.26%, respectively). However, in terms of number of samples the action of pancreatin was more advantageous than subtilisin, since among the nine hydrolysates, four showed appropriate peptide profiles (P1, P2, P5, and P6), from the nutritional point of view, while the same happened only with one hydrolysate prepared by using subtilisin (S3). Also, the economical advantage of using smaller E:S ratio and reaction time was observed in several cases for both enzymes.
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Grimble, G. K., P. P. Keohane, B. E. Higgins, M. V. Kaminski, and D. B. A. Silk. "Effect of peptide chain length on amino acid and nitrogen absorption from two lactalbumin hydrolysates in the normal human jejunum." Clinical Science 71, no. 1 (July 1, 1986): 65–69. http://dx.doi.org/10.1042/cs0710065.
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1. A double lumen jejunal perfusion technique has been used in man to study the effect of peptide chain length on absorption of amino acid nitrogen from two partial enzymic hydrolysates of lactalbumin. 2. Copper-chelation chromatography showed that one lactalbumin hydrolysate (LH2) contained 98% peptides with a chain length > 4, whilst the other (LH1) contained a more even spread of chain lengths with 55% <4. 3. Absorption of total nitrogen and of 14 amino acid residues occurred to a significantly greater extent from the low molecular weight LH1 than from the higher molecular weight LH2. 4. The results suggest that the pattern of nitrogen and amino acid absorption from partial enzymic hydrolysates of whole protein is markedly influenced by peptide chain length and that brush border peptide hydrolysis has an important rate limiting effect on absorption rates.
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Arise, Rotimi, Samuel Tobi Farohunbi, and Halimat Olanike Ayilara. "Blood Pressure Regulating and Antioxidant Potentials of Theobroma Cacao Pod Husk Protein Hydrolysates." Avicenna Journal of Medical Biochemistry 9, no. 1 (June 29, 2021): 26–36. http://dx.doi.org/10.34172/ajmb.2021.05.
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Background: Agrowastes like Theobroma cacao (Cocoa) pod husk can be used to prepare bioactive peptides with various bio-functionalities. Objectives: This study aimed to investigate antioxidant and angiotensin converting enzyme I (ACE) inhibitory peptides contained in Theobroma cacao (cocoa) pod husks – an agro-waste. Methods: Protein isolated from cocoa pod husk was enzymatically digested with alcalase, pepsin, and trypsin. ACE inhibition, kinetics of ACE inhibition, and antioxidant properties of the cocoa pod husks hydrolysates were evaluated in vitro. Results: Trypsin and alcalase hydrolysates displayed higher peptide yields (63.1% and 61.2%) than pepsin hydrolysate (61.2%). However, no significant difference (P>0.05) was observed in the degree of hydrolysis (DH) of the three proteases on cocoa pod husk protein. Methionine, lysine, and cysteine were the amino acid residues presented in cocoa pod husk hydrolysates. A concentration-dependent ACE inhibition by cocoa pod husk hydrolysates was observed. The highest ACE inhibitions of 84.4%, 81.5%, and 73.5% were obtained at 2.0 mg/mL of pepsin, trypsin, and alcalase hydrolysates, respectively, with the minimum IC50 value of 0.36 mg/mL obtained for trypsin hydrolysate. An uncompetitive and mixed-type inhibition was obtained from double reciprocal plots of alcalase and pepsin as well as trypsin cocoa pod husk protein hydrolysates. The Ki values of ACE inhibition for pepsin, trypsin, and alcalase hydrolysates were 3.05, 2.19, and 3.57 mg/mL, respectively. A concentration-dependent increase in the scavenging of 2,2-diphenyl-1-picrylhydrazyl and superoxide radicals as well as ferric reducing antioxidant power were recorded for the cocoa pod husk hydrolysates. Conclusion: Trypsin and alcalase cocoa pod husk protein hydrolysates could be an effective source of a natural ACE inhibitor and antioxidant.
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Ngoc, Ngo Minh. "ANTIOXIDANT ACTIVITIES OF HYDROLYSATES ORIGINATED FROM SOYBEAN AND SOY MILK RESIDUE." Vietnam Journal of Science and Technology 55, no. 5A (March 24, 2018): 134. http://dx.doi.org/10.15625/2525-2518/55/5a/12188.
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Soybean (Glycine max) and soy milk residue (okara) are protein-rich materials. Soybean possesses the highest protein content among different types of beans (protein content of soybean varies from 40–42 %). Soy milk residue, a by-product of the soy milk manufacturing industry, contains approximately 27 % protein (by dry weight). A number of recent studies have investigated the improvement of functional properties of protein contained in soybean and okara by fermentation or by the use of proteolytic enzymes. The aim of this study was to evaluate the antioxidant activities of soybean and okara hydrolysates obtained by the fermentation with Aspergillus oryzae or by using proteolytic enzymes (neutrase and flavourzyme). DPPH radical scavenging assay was used to determine the antioxidant activities of hydrolysates. The concentration of peptides required to scavenge DPPH radical by 50 % (IC50 value) was used to evaluate the antioxidant activity of peptides produced obtained from hydrolysates. The results showed that when fermented with A. oryzae, the okara hydrolysate had higher antioxidant activity than the soybean hydrolysate, with IC50 values of 0.447 mg/ml and 3.95 mg/ml, respectively. The hydrolyzed okara obtained from hydrolysis using Neutrase had higher antioxidant activity than the one obtained from hydrolysis using Flavourzyme, with IC50 values of0.200 mg/ml and 0.407 mg/ml, respectively. Different peptide fractions obtained from the hydrolysates using cut-off membrane (10 kDa, 3 kDa and 1 kDa) possessed different antioxidant activities. The < 1 kDa peptide fraction exhibited the highest antioxidant activity with an IC50 value of 0.158 mg/ml.
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Ekun, Oluwafemi Emmanuel. "Peptide Fractions from Pepsin-digested Moringa oleifera Seed Proteins Inhibit Hemoglobin Glycation and Carbohydrate-hydrolyzing Enzymes." Biology, Medicine, & Natural Product Chemistry 12, no. 1 (August 4, 2023): 413–22. http://dx.doi.org/10.14421/biomedich.2023.121.413-422.
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The multidirectional abilities of peptide digests and fractions obtained from the hydrolysis of food-based proteins have been investigated in recent times. This study aims to evaluate the effects of pepsin-derived Moringa oleifera seed protein hydrolysates and fractions on hemoglobin glycation and the carbohydrases - ?-amylase and ?-glucosidase. Proteins were extracted from M. oleifera seeds and consequently digested using pepsin. The hydrolysates obtained were separated into fractions of <1 kD, 1-3 kD, and 3-5 kD ranges using size-exclusion chromatography and comparison with elution volumes of known standards. The activities of the hydrolysates and peptide fractions against both the non-enzymatic glycation of hemoglobin and the carbohydrases were determined in vitro. Results revealed that the hydrolysate and its peptide fractions demonstrated varying abilities against the glycation of hemoglobin, with the unfractionated hydrolysate showing better activities (78.230 ± 0.774 % at a maximum concentration of 1.0 mg/ml) than its peptide fractions. Also, the hydrolysates and fractions demonstrated higher inhibitory effects on a-amylase (with all fractions displaying above 50% inhibition at a final concentration of 1.0 mg/mL) than against a-glucosidase. Kinetic analysis of a selected fraction showed that it inhibited ?-amylase via a mixed mechanism (Ki = 0.029 mg/mL) but displayed an uncompetitive mode for ?-glucosidase inhibition (Ki = 0.333 mg/mL). Therefore, it is inferred that M. oleifera seed proteins encode potentially therapeutic peptide sequences that could be further processed to formulate potential antidiabetic agents.
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Silvestre, Marialice Pinto Coelho, Harriman Aley Morais, Mauro Ramalho Silva, Viviane Dias Medeiros Silva, and Mariana Wanessa Santana de Souza. "Action of protease from Aspergillus sojae and pancreatin in the hydrolysis of whey protein concentrate." Revista Brasileira de Pesquisa em Alimentos 3, no. 1 (June 13, 2013): 19. http://dx.doi.org/10.14685/rebrapa.v3i1.69.
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<p>The preparation of hydrolysates from whey protein concentrate with high contents of di- and tripeptides and free amino acids, and reduced amount of large peptides, was the objective of this study. The actions of a protease from Aspergillus sojae and a pancreatin at six enzyme:substrate ratios, pH 7.0, at 50 °C for 5 h were evaluated. The size-exclusion-high performance liquid chromatography and the method of the Correct Fraction Area were used for the fractionation and quantification of peptides and free amino acids in the hydrolysates. It was observed that the type of enzyme and the enzyme: substrate ratio affected significantly the peptide profile of the hydrolysates. The chromatograms obtained by the action of two enzymes were different and varied according to the specificity or enzymatic activity. The best peptide profile was found for the hydrolysate obtained using pancreatin at an enzyme: substrate ratio of 8:100 that showed the smallest amount of large peptides (41.13%), and the greatest di- and tripeptide (6.46%) and free amino acid (8.22%) contents.</p><p> </p><p>DOI: http://dx.doi.org/10.14685/rebrapa.v3i1.69</p><br />
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Bak, Kathrine H., Sandra S. Waehrens, Yu Fu, Ching Yue Chow, Mikael A. Petersen, Jorge Ruiz-Carrascal, Wender L. P. Bredie, and René Lametsch. "Flavor Characterization of Animal Hydrolysates and Potential of Glucosamine in Flavor Modulation." Foods 10, no. 12 (December 4, 2021): 3008. http://dx.doi.org/10.3390/foods10123008.
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Bovine (meat and heart) and porcine (hemoglobin and plasma) raw materials were hydrolyzed by Protease A (both endo- and exopeptidase activity), with or without glucosamine added during the enzyme inactivation step. Hydrolysates were characterized via peptide analysis (yield, UV- and fluorescence scanning spectroscopy, and peptide size distribution via size exclusion chromatography), sensory evaluation, and volatile compound analysis via gas chromatography mass-spectrometry (GC-MS) to determine if glucosamine-induced Maillard reaction improved taste and flavor. Porcine hemoglobin produced the most flavor-neutral hydrolysate, and could expectedly have the broadest application in food products. Both bovine meat and -heart hydrolysates were high in umami, and thereby good candidates for savory applications. Porcine plasma hydrolysate was high in liver flavor and would be suitable for addition to certain meat products where liver flavor is desirable. All hydrolysates had low perceived bitterness. Glucosamine-induced Maillard reaction had just a minor influence on the sensory profile via an increased perception of sweet taste (p = 0.038), umami taste (p = 0.042), and yolk flavor (p = 0.038) in the hydrolysates, irrespective of raw material. Glucosamine addition had a statistically significant effect on 13 of 69 volatiles detected in the hydrolysates, but the effect was minor and raw material-specific.
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Tejada, Luis, Laura Buendía-Moreno, Irene Hernández, Adela Abellán, José María Cayuela, Eva Salazar, and Estefanía Bueno-Gavilá. "Bioactivities of Mealworm (Alphitobius diaperinus L.) Larvae Hydrolysates Obtained from Artichoke (Cynara scolymus L.) Proteases." Biology 11, no. 5 (April 20, 2022): 631. http://dx.doi.org/10.3390/biology11050631.
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In this study, we aimed to obtain hydrolysates with bioactive peptides from mealworm (Alphitobius diaperinus L.) larvae using an artichoke (Cynara scolymus L.) enzyme extract. Two types of substrates were used: the raw larvae flour (LF) and its protein extract (PE). The hydrolysis yield, considering the peptide concentration of the hydrolysates, was higher in PE hydrolysates than in LF hydrolysates (6.39 ± 0.59 vs. 3.02 ± 0.06 mg/mL, respectively). However, LF showed a higher antioxidant activity against the DPPH radical than PE (59.10 ± 1.42 vs. 18.79 ± 0.81 µM Trolox Eq/mg peptides, respectively). Regarding the inhibitory activity of angiotensin-I-converting enzyme (ACE), an IC50 value of 111.33 ± 21.3 µg peptides/mL was observed in the PE. The identification of the peptide sequence of both hydrolysates was conducted, and LF and its PE presented 404 and 116 peptides, respectively, most with low molecular weight (<3 kDa), high percentage of hydrophobic amino acids, and typical characteristics of well-known antioxidant and ACE-inhibitory peptides. Furthermore, the potential bioactivity of the sequences identified was searched in the BIOPEP database. Considering the antioxidant and ACE-inhibitory activities, LF hydrolysates contained a larger number of sequences with potential bioactivity than PE hydrolysates.
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Su, Yu-Jhen, Hung-Ju Liao, and Jing-Iong Yang. "Purification and Identification of an ACE-Inhibitory Peptide from Gracilaria tenuistipitata Protein Hydrolysates." Processes 10, no. 6 (June 5, 2022): 1128. http://dx.doi.org/10.3390/pr10061128.
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Edible marine species are valuable sources of bioactive peptides. This study investigated the ACE-inhibitory activity of protein hydrolysates from the red algae Gracilaria tenuistipitata. Fifteen groups of protein hydrolysates were prepared by a two-step enzymatic hydrolysis of G. tenuistipitata: initial hydrolysis with several glycolytic enzymes, followed by three separate proteolytic reactions (Alcalase, Neutrase and Flavourzyme) for 2–10 h. Results showed that the hydrolysate GTN4H had the highest ACE-inhibitory activity in vitro. Furthermore, oral administration of GTN4H significantly reduced systolic blood pressure in spontaneously hypertensive rats. Fraction A derived from GTN4H displayed the highest ACE-inhibitory activity among fractions. Further purification of fraction A by RP-HPLC obtained a purified peptide (MW: 1776 Da) with 17 amino acids and 95.4% ACE-inhibitory activity.
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Devita, Liza, Hanifah Nuryani Lioe, Mala Nurilmala, and Maggy T. Suhartono. "The Bioactivity Prediction of Peptides from Tuna Skin Collagen Using Integrated Method Combining In Vitro and In Silico." Foods 10, no. 11 (November 9, 2021): 2739. http://dx.doi.org/10.3390/foods10112739.
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The hydrolysates and peptide fractions of bigeye tuna (Thunnus obesus) skin collagen have been successfully studied. The hydrolysates (HPA, HPN, HPS, HBA, HBN, HBS) were the result of the hydrolysis of collagen using alcalase, neutrase, and savinase. The peptide fractions (PPA, PPN, PPS, PBA, PBN, PBS) were the fractions obtained following ultrafiltration of the hydrolysates. The antioxidant activities of the hydrolysates and peptide fractions were studied using the DPPH method. The effects of collagen types, enzymes, and molecular sizes on the antioxidant activities were analyzed using profile plots analysis. The amino acid sequences of the peptides in the fraction with the highest antioxidant activity were analyzed using LC-MS/MS. Finally, their bioactivity and characteristics were studied using in silico analysis. The hydrolysates and peptide fractions provided antioxidant activity (6.17–135.40 µmol AAE/g protein). The lower molecular weight fraction had higher antioxidant activity. Collagen from pepsin treatment produced higher activity than that of bromelain treatment. The fraction from collagen hydrolysates by savinase treatment had the highest activity compared to neutrase and alcalase treatments. The peptides in the PBN and PPS fractions of <3 kDa had antidiabetic, antihypertensive and antioxidant activities. In conclusion, they have the potential to be used in food and health applications.
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Cunha, Sara A., Ezequiel R. Coscueta, Paulo Nova, Joana Laranjeira Silva, and Maria Manuela Pintado. "Bioactive Hydrolysates from Chlorella vulgaris: Optimal Process and Bioactive Properties." Molecules 27, no. 8 (April 13, 2022): 2505. http://dx.doi.org/10.3390/molecules27082505.
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Microalgae have been described as a source of bioactive compounds, such as peptides. Microalgae are easy to produce, making them a sustainable resource for extracting active ingredients for industrial applications. Several microalgae species have interesting protein content, such as Chlorella vulgaris with around 52.2% of protein, making it promising for peptide hydrolysate production. Therefore, this work focused on the production of water-soluble hydrolysates rich in proteins/peptides from the microalgae C. vulgaris and studied bioactive properties. For that, a design of experiments (DOE) was performed to establish the optimal conditions to produce hydrolysates with higher levels of protein, as well as antioxidant and antihypertensive properties. Four experimental factors were considered (cellulase percentage, protease percentage, hydrolysis temperature, and hydrolysis duration) for three responses (protein content, antioxidant activity, and antihypertensive activity). The optimal conditions determined by the DOE allowed producing a scaled-up hydrolysate with 45% protein, with antioxidant activity, measured by oxygen radical absorbance capacity assay, of 1035 µmol TE/g protein, IC50 for angiotensin-converting enzyme inhibition activity of 286 µg protein/mL, and α-glucosidase inhibition of 31% (30 mg hydrolysate/mL). The obtained hydrolysates can be used as functional ingredients for food and nutraceuticals due to their antioxidant, antihypertensive, and antidiabetic potential. Moreover, the antioxidant potential of the extracts may be relevant for the cosmetic industry, especially in antiaging formulations.
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Ding, Ko, Moon, and Lee. "Protective Effects of Novel Antioxidant Peptide Purified from Alcalase Hydrolysate of Velvet Antler Against Oxidative Stress in Chang Liver Cells in Vitro and in a Zebrafish Model In Vivo." International Journal of Molecular Sciences 20, no. 20 (October 19, 2019): 5187. http://dx.doi.org/10.3390/ijms20205187.
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Velvet antler has a long history in traditional medicine. It is also an important healthy ingredient in food as it is rich in protein. However, there has been no report about antioxidant peptides extracted from velvet antler by enzymatic hydrolysis. Thus, the objective of this study was to hydrolyze velvet antler using different commercial proteases (Acalase, Neutrase, trypsin, pepsin, and α-chymotrypsin). Antioxidant activities of different hydrolysates were investigated using peroxyl radical scavenging assay by electron spin resonance spectrometry. Among all enzymatic hydrolysates, Alcalase hydrolysate exhibited the highest peroxyl radical scavenging activity. Alcalase hydrolysate was then purified using ultrafiltration, gel filtration, and reverse-phase high performance liquid chromatography. The purified peptide was identified to be Trp-Asp-Val-Lys (tetrapeptide) with molecular weight of 547.29 Da by Q-TOF ESI mass spectroscopy. This purified peptide exhibited strong scavenging activity against peroxyl radical (IC50 value, 0.028 mg/mL). In addition, this tetrapeptide showed significant protection ability against AAPH-induced oxidative stress by inhibiting of reactive oxygen species (ROS) generation in Chang liver cells in vitro and in a zebrafish model in vivo. This research suggests that the tetrapeptide derived from Alcalase-proteolytic hydrolysate of velvet antler are excellent antioxidants and could be effectively applied as functional food ingredients and pharmaceuticals.
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Spellman, David, Gerard O'Cuinn, and Richard J. FitzGerald. "Physicochemical and sensory characteristics of whey protein hydrolysates generated at different total solids levels." Journal of Dairy Research 72, no. 2 (December 8, 2004): 138–43. http://dx.doi.org/10.1017/s0022029904000688.
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Whey protein hydrolysates were generated at different total solids (TS) levels (50–300 g/l) using the commercially available proteolytic preparation Debitrase™ HYW20, while enzyme to substrate ratio, pH and temperature were maintained constant. Hydrolysis proceeded at a faster rate at lower TS reaching a degree of hydrolysis (DH) of 16·6% at 300 g TS/l, compared with a DH of 22·7% at 50 g TS/l after 6 h hydrolysis. The slower breakdown of intact whey proteins at high TS was quantified by gel-permeation HPLC. Reversed-phase (RP) HPLC of hydrolysate samples of equivalent DH (~15%) generated at different TS levels indicated that certain hydrophobic peptide peaks were present at higher levels in hydrolysates generated at low TS. Sensory evaluation showed that hydrolysates with equivalent DH values were significantly (P<0·0005) less bitter when generated at 300 g TS/l (mean bitterness score=25·4%) than hydrolysates generated at 50 g TS/l (mean bitterness score=39·9%). A specific hydrophobic peptide peak present at higher concentrations in hydrolysates generated at low TS was isolated and identified as β-lactoglobulin f(43–57), a fragment having the physical and chemical characteristics of a bitter peptide.
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Maky, Mohamed Abdelfattah, and Takeshi Zendo. "Identification of a Novel Bioactive Peptide Derived from Frozen Chicken Breast Hydrolysate and the Utilization of Hydrolysates as Biopreservatives." Biology 12, no. 9 (September 8, 2023): 1218. http://dx.doi.org/10.3390/biology12091218.
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Frozen chicken breast was hydrolyzed by treatment with thermolysin enzyme to obtain a chicken hydrolysate containing bioactive peptides. After that, a peptide was purified from the chicken hydrolysate utilizing a Sep-Pak C18 cartridge and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weight of the chicken peptide was 2766.8. Protein sequence analysis showed that the peptide was composed of 25 amino acid residues. The peptide, designated as C25, demonstrated an inhibitory action on the angiotensin-converting enzyme (ACE) with a half maximal inhibitory concentration (IC50) value of 1.11 µg/mL. Interestingly, C25 showed antimicrobial activity against multi-drug resistant bacteria Proteus vulgaris F24B and Escherichia coli JM109, both with MIC values of 24 µg/mL. The chicken hydrolysate showed antioxidant activity with an IC50 value of 348.67 µg/mL. Furthermore, the proliferation of aerobic bacteria and Enterobacteriaceae as well as lipid oxidation were significantly reduced when the chicken hydrolysate was used as a natural preservative during cold storage of chicken breasts. Hydrolysates derived from muscle sources have the potential to be used in formulated food products and to contribute positively to human health.
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Lestari, Diana, Joshua Evan, and Maggy Thenawidjaja Suhartono. "FRAKSI PEPTIDA ANTIOKSIDAN DARI KASEIN SUSU KAMBING." Jurnal Teknologi dan Industri Pangan 31, no. 2 (December 2020): 188–96. http://dx.doi.org/10.6066/jtip.2020.31.2.188.
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Milk bioactive peptides are derivative of milk protein produced either through enzymatic activity, digestive processes, or fermentation, that give functional properties. The study aimed to obtain bioactive peptides fraction derived from goat’s milk casein through hydrolysis by papain, analyze the profiles of protein and peptides, and also test the antioxidative activity. The casein isolate was hydrolyzed by papain in a ratio of 100: 0.5 (v/v) at pH 7.0 and 50ºC. Analysis of protein concentration was carried out by the Bradford method and protein profile by SDS-PAGE. Antioxidant assay was carried out by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) method. A 1,000 ppm ascorbic acid solution was used as positive control. Peptide fractionation was done by membrane filtration with a cut off of 10 kD and 30 kDa. The protein concentration of casein hydrolysates decreased significantly after hydrolysis process with papain. The electrophoresis results showed six protein bands in casein with molecular weight of 7-33 kDa. After the hydrolysis process, all hydrolysates only contained two protein bands with molecular weights of 8 and 5 kDa. The hydrolysis process increased the antioxidant activity of the casein. P0 and P2 hydrolysates had the highest antioxidant activity, and fractions with the highest antioxidant activity were fraction <10 kDa from P0 hydrolysate at 67.89% and 10-30 kDa from P2 hydrolysate at 73.82%. Molecular weight and hydrolysis time affected the antioxidant activity of the hydrolysates. Peptides below 30 kDa have antioxidant activity, whereas those above 30 kDa do not have any antioxidant activity. The antioxidant activity of the peptides decreases upon hydrolysis for more then 2 minutes.
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Zinina, O. V., A. D. Nikolina, D. V. Khvostov, M. B. Rebezov, S. N. Zavyalov, and R. V. Akhmedzyanov. "Protein hydrolysate as a source of bioactive peptides in diabetic food products." Food systems 6, no. 4 (January 13, 2024): 440–48. http://dx.doi.org/10.21323/2618-9771-2023-6-4-440-448.
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Protein hydrolysates are a promising active component in specialized food products. Due to the presence of bioactive peptides with enzyme inhibiting activity in their composition, protein hydrolysates exert different physiological effects. The aim of the research was to establish the potential hypoglycemic activity of the protein hydrolysate of broiler chicken stomachs in whey and to develop a beverage on its basis for patients with diabetes mellitus. Protein hydrolysates obtained from microbial fermentation of muscular stomachs of broiler chickens in whey were assessed by UHPLC coupled to mass-spectrometry. Using the BioPEp database, the molecular weight distribution of peptides in the hydrolysates was determined. In addition, bioactive peptides showing the inhibitory activity toward enzymes dipeptidyl peptidase‑4 and amylase were revealed. Based on the obtained hydrolysates, recipes of beverages for patients with diabetes mellitus were modeled in the Excel software program with regard to the recommendations for nutrition of this population group. According to the obtained recipes, beverages were produced in the laboratory conditions and their taste was assessed. An effect of the beverage on glucose reduction in the blood of laboratory animals was assessed upon single peroral administration with a dose of 1.3 ml before the main meal. The results of the investigation of the peptide composition of protein hydrolysates showed the presence of bioactive peptides (SY, VW, SW) in them with the inhibitory activity toward enzymes dipeptidyl peptidase‑4 and amylase confirmed by the BioPep database. The highest amount of the above indicated bioactive peptides (37.1 mg/100 g hydrolysate) was in the protein hydrolysate produced by fermentation of raw materials with propionic acid bacteria. The beverage produced on the basis of the protein hydrolysate and lemon juice was more acceptable for consumers in terms of taste than the beverage with the taste of cacao. The results of the in vivo trials showed that the beverage based on the protein hydrolysate was effective in reducing sugar in blood of both healthy rats and rats with diabetes mellitus. The blood sugar level in the healthy animals of the G1 group (without using the beverage) increased by 151% relative to the initial values, which was a higher value compared to the G2 group (with the use of the beverage), where an increase was 87%. A more significant growth in the blood sugar level (61% relative to the initial values) was also observed in the ill animals in the G3 group (without using the beverage), while this increase was 46% in the G4 group (with the use of the beverage). Thus, the results of the study show the prospects of using the protein hydrolysates from broiler chicken stomachs in whey as an active hypoglycemic component in beverages for patients with diabetes mellitus. However, more profound research is necessary including studies on the representative group of patients.
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Habibie, Ahmad, Tri Joko Raharjo, Respati Tri Swasono, and Endah Retnaningrum. "Antibacterial activity of active peptide from marine macroalgae Chondrus crispus protein hydrolysate against Staphylococcus aureus." Pharmacia 70, no. 4 (October 5, 2023): 983–92. http://dx.doi.org/10.3897/pharmacia.70.e112215.
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Macroalgae is a protein source with the potential to yield antimicrobial peptides (AMPs) that exhibit a wide range of biological activities. This study aimed to find bioactive peptide-based antibacterial compounds from marine macroalgae Chondrus crispus protein hydrolysate. The peptides were isolated by solid phase extraction with a strong cation exchanger from trypsin-digested and α-chymotrypsin-digested hydrolysates. Certain fractions of the hydrolyzed protein displayed a good inhibition zone, with the α-chymotrypsin-digested fraction eluted at pH 9 exhibiting the highest inhibition against Gram-negative bacteria Staphylococcus aureus. Several peptides were characterized as cationic helical peptides with hydrophobicity percentages of 16.67–77.78%. The potential antibacterial peptide P01 KKNVTTLAPLVF was identified as an α-helical cationic antibacterial peptide with 0.525 GRAVY value, amphipathic structure, and +2 total charge. Moreover, strong interaction was observed between P07 SAGSGNEGLSGW and P20 RTASSR peptide with DNA gyrase and DHFR receptors from S. aureus with binding energy -8.0 and -7.3 kcal/mol, respectively.
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Mendez, Rufa, and Jung Yeon Kwon. "Streamlining Bioactive Peptide Discovery With In Silico Prospecting: An investigation on Seaweed Pacific Dulse." Current Developments in Nutrition 6, Supplement_1 (June 2022): 315. http://dx.doi.org/10.1093/cdn/nzac053.056.
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Abstract Objectives Bioactive hydrolysates and peptides from seaweed sources have been shown to exert beneficial effects in both in vitro and in vivo models for metabolic health. However, the discovery approach relies heavily on the conventional hydrolysate preparation and screening model selection, both driven by resource availability and time constraints. Considering the potential for functional food and therapeutics development, efficient and cost-effective strategies are needed to scope out as much prospect that can be screened for increased chances of hits to find potent, stable, and commercializable bioactive peptides (BAPs). This work aimed to identify multifunctional BAPs from seaweed Pacific Dulse, and to determine which hydrolytic condition can favor the release of more BAPs of interest from this protein-rich macroalgae. Methods Virtual hydrolysates were prepared from dulse proteins using three digestion platforms (ExPASy, SystemsBio, and Rapid Peptide Generator) under three production stream contexts (hydrolysate preparation, gastrointestinal digestion, and microbial fermentation). Peptide products were then subjected to in silico bioactivity prospecting for anti-inflammatory, antidiabetic, and antihypertensive potential. Stability in the intestine and blood was predicted along with potential toxicity. Non-toxic and stable peptides predicted to have multifunctionalities were shortlisted for bioactivity validation, and production streams predicted to generate most number of BAPs were noted for test hydrolysate production. Results With our approach, we identified 13 novel prospect BAPs that have multiple bioactivities, high stability, and low toxicity. Hydrolysate production using bromelain and ficin favored the 5–10aa long mBAPs generation. Simulated gastrointestinal digestion and microbial fermentation also showed promise in the release of some BAPs of interest. Conclusions When consumed in either hydrolyzed, whole, or fermented form, BAPs can be generated from seaweed Pacific Dulse proteins. Bioactivity testing of the novel BAPs identified, and microscale production of the promising BAP production stream are underway. Funding Sources Oregon Agricultural Experiment Station.
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Taroncher, Mercedes, Yelko Rodríguez-Carrasco, Tone Aspevik, Katerina Kousoulaki, Francisco J. Barba, and María-José Ruiz. "Cytoprotective Effects of Fish Protein Hydrolysates against H2O2-Induced Oxidative Stress and Mycotoxins in Caco-2/TC7 Cells." Antioxidants 10, no. 6 (June 18, 2021): 975. http://dx.doi.org/10.3390/antiox10060975.
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Many studies report the potent antioxidant capacity for fish protein hydrolysates, including radical scavenging activity and inhibition ability on lipid peroxidation (LPO). In this study, the in vitro cytotoxicity of protein hydrolysates from different salmon, mackerel, and herring side streams fractions was evaluated in the concentration range from 1 to 1:32 dilution, using cloned human colon adenocarcinoma cells TC7 (Caco-2/TC7) by MTT and PT assays. The protein hydrolysates’ antioxidant capacity and oxidative stress effects were evaluated by LPO and reactive oxygen species (ROS) generation, respectively. The antioxidant capacity for pure and bioavailable hydrolysate fraction was also evaluated and compared. Additionally, mycotoxin levels were determined in the fish protein hydrolysates, and their cytoprotective effect against T-2 toxin was evaluated. Both hydrolysates and their bioavailable fraction induced similar cell viability rates. The highest cytoprotective effect was obtained for the salmon viscera protein hydrolysate (HSV), which increased the cell viability by 51.2%. ROS accumulation induced by H2O2 and LPO was suppressed by all pure hydrolysates. The cytoprotective effect of hydrolysates was observed against T-2. Moreover, the different fish fraction protein hydrolysates contain variable nutrients and unique bioactive peptide composition showing variable bioactivity, which could be a useful tool in developing dietary supplements with different target functional properties.
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Molinari, Giovanni S., Michal Wojno, Genciana Terova, Macdonald Wick, Hayden Riley, Jeffrey T. Caminiti, and Karolina Kwasek. "A Novel Approach in the Development of Larval Largemouth Bass Micropterus salmoides Diets Using Largemouth Bass Muscle Hydrolysates as the Protein Source." Animals 13, no. 3 (January 21, 2023): 373. http://dx.doi.org/10.3390/ani13030373.
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This study’s objectives were to determine the effect of Largemouth Bass (LMB) muscle hydrolysates obtained using same-species digestive enzymes and the degree of LMB muscle hydrolysis when included in the first feeds of growth performance and survival, skeletal development, intestinal peptide uptake, and muscle-free amino acid composition of larval LMB. LMB muscle was mixed with digestive enzymes from adult LMB, and hydrolyzed for 1.5, 3, and 6 h, respectively. Five diets were produced, the intact diet containing non-hydrolyzed muscle and four diets with 37% muscle hydrolysate inclusion. Those diets were characterized by their level of each hydrolysate (presented as a ratio of 1.5, 3, and 6 Ts hydrolysates): 1:1:1, 1:3:6, 1:3:1, 6:3:1 for diets A, B, C, and D, respectively. To account for gut development, one group of larval LMB was fed a weekly series of diets B, C, and D to provide an increasing molecular weight profile throughout development. This group was compared against others that received either; (1) diets D, C, and B; (2) diet A; or (3) intact diet. The initial inclusion of the hydrolysates significantly improved the total length of the larval LMB; however, neither the hydrolysate inclusion nor the series of dietary molecular weight profiles improved the overall growth of larval LMB. The inclusion of hydrolysates significantly decreased the occurrence of skeletal deformities. The degree of hydrolysis did not have a significant effect on the parameters measured, except for intestinal peptide uptake, which was increased in the group that received the most hydrolyzed diet at the final time of sampling. The lack of overall growth improvement suggests that while the hydrolysates improve the initial growth performance, further research is necessary to determine the optimal molecular weight profile, hydrolysate inclusion level, and physical properties of feeds for larval LMB.
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Garcia-Vaquero, Marco, Leticia Mora, and Maria Hayes. "In Vitro and In Silico Approaches to Generating and Identifying Angiotensin-Converting Enzyme I Inhibitory Peptides from Green Macroalga Ulva lactuca." Marine Drugs 17, no. 4 (March 30, 2019): 204. http://dx.doi.org/10.3390/md17040204.
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A protein extract was generated from the macroalga Ulva lactuca, which was subsequently hydrolysed using the food-grade enzyme papain and angiotensin-converting Enzyme I and renin inhibitory peptides identified using a combination of enrichment strategies employing molecular weight cutoff filtration and mass spectrometry analysis. The generated hydrolysates with the most promising in vitro activity were further purified using preparative RP-HPLC and characterised. The 1 kDa hydrolysate (1 kDa-UFH), purified and collected by preparative RP-HPLC at minutes 41‒44 (Fr41‒44), displayed statistically higher ACE-I inhibitory activities ranging from 96.91% to 98.06%. A total of 48 novel peptides were identified from these four fractions by LC-MS/MS. A simulated gastrointestinal digestion of the identified peptide sequences was carried out using in silico enzyme cleavage simulation tools, resulting in 86 peptide sequences that were further assessed for their potential activity, toxicity and allergenicity using multiple predictive approaches. All the peptides obtained in this study were predicted to be non-toxic. However, 28 out of the 86 novel peptides released after the in silico gastrointestinal digestion were identified as potential allergens. The potential allergenicity of these peptides should be further explored to comply with the current labelling regulations in formulated food products containing U. lactuca protein hydrolysates.
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Forghani, Bita, Afshin Ebrahimpour, Jamilah Bakar, Azizah Abdul Hamid, Zaiton Hassan, and Nazamid Saari. "Enzyme Hydrolysates fromStichopus horrensas a New Source for Angiotensin-Converting Enzyme Inhibitory Peptides." Evidence-Based Complementary and Alternative Medicine 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/236384.
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Stichopus horrensflesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) ofStichopus horrenshydrolysates (SHHs) was also assessed. Alcalase hydrolysate showed the highest DH value (39.8%) followed by flavourzyme hydrolysate (32.7%). Overall, alcalase hydrolysate exhibited the highest ACE inhibitory activity (IC50value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC50value of 2.24 mg/mL), trypsin hydrolysate (IC50value of 2.28 mg/mL), papain hydrolysate (IC50value of 2.48 mg/mL), bromelain hydrolysate (IC50value of 4.21 mg/mL), and protamex hydrolysate (IC50value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC50values of alcalase and flavourzyme hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.
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Vázquez, José Antonio, Isabel Rodríguez-Amado, Carmen G. Sotelo, Noelia Sanz, Ricardo I. Pérez-Martín, and Jesus Valcárcel. "Production, Characterization, and Bioactivity of Fish Protein Hydrolysates from Aquaculture Turbot (Scophthalmus maximus) Wastes." Biomolecules 10, no. 2 (February 15, 2020): 310. http://dx.doi.org/10.3390/biom10020310.
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The valorization of wastes generated in the processing of farmed fish is currently an issue of extreme relevance for the industry, aiming to accomplish the objectives of circular bioeconomy. In the present report, turbot (Scophthalmus maximus) by-products were subjected to Alcalase hydrolysis under the optimal conditions initially defined by response surface methodology. All the fish protein hydrolysates (FPHs) showed a high yield of digestion (>83%), very remarkable degrees of hydrolysis (30–37%), high content of soluble protein (>62 g/L), an excellent profile of amino acids, and almost total in vitro digestibility (higher than 92%). Antioxidant and antihypertensive activities were analyzed in all cases, viscera hydrolysates being the most active. The range of average molecular weights (Mw) of turbot hydrolysates varied from 1200 to 1669 Da, and peptide size distribution showed that the hydrolysate of viscera had the highest content of peptides above 1000 Da and below 200 Da.
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Gribakin, S. G., I. S. Stovolosov, and T. Е. Lavrova. "Comparative characteristics of the palatability of extensively hydrolyzed formulas: results of a questionnaire survey among medical doctors." Voprosy detskoj dietologii 18, no. 5 (2020): 42–48. http://dx.doi.org/10.20953/1727-5784-2020-5-42-48.
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Objective. To compare the palatability of six extensively hydrolyzed formulas used in the Russian Federation for diet therapy in case of cow’s milk protein allergy. Materials and methods. А direct taste-testing of six specialized formulas with a subsequent questionnaire survey was performed among 336 paediatricians and paediatric allergologists. Results. A whey protein hydrolysate formula containing galacto- and fructooligosaccharides with lactose reduced contents scored higher (8.0 ± 1.8 out of 10, p < 0.01). On the whole, whey protein hydrolysates are more palatable compared to casein hydrolysates (5.7 ± 1.7 vs 3.5 ± 2.1, p < 0.01). Conclusion. Extensively hydrolyzed formulas differ significantly in their taste attributes. Whey protein hydrolysates containing prebiotic oligosaccharides and lactose have the best palatability among other extensively hydrolyzed formulas. Key words: cow’s milk protein allergy, extensively hydrolyzed formulas, hydrolysate taste, peptide size
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Mei, De Jun, Guo Ping Yu, and An Min Sun. "Preparation, Purification and Identification of Antioxidant Peptides with Bienzyme Hydrolysis from Rice Bran Protein." Advanced Materials Research 610-613 (December 2012): 72–80. http://dx.doi.org/10.4028/www.scientific.net/amr.610-613.72.
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The rice bran protein (RBP) was then hydrolyzed with various proteases (papain, flavorzyme, neutrase, protamex, and trypsin) to prepare antioxidant peptides. The rice bran protein hydrolysates (RBPH) were assessed using method of DPPH radical scavenging ability. Hydrolysate prepared with papain and flavorzyme (activity ratio 1:1) was found to have the highest antioxidant activity (IC50=6.778±0.21 mg/ml). This hydrolysate was purified using ultrafiltration, RBPH-III (Mw＜3KDa) had the highest DPPH and hydroxyl radical scavenging activity (IC50 value of 6.56±0.28, 5.43±0.22, respectively) and highest reducing power activity (1.02±0.18 at 4 mg/mL). Later, RBPH-III was fractionated by SP-SephadexC-25 cation-exchange column into six fractions (A–F), fraction F with the highest DPPH scavenging activity, was then separated by size exclusion chromatography on a SephadexG-25 into three major fractions (F1–F3). Fraction F2 exhibited the highest DPPH scavenging activity was choose to fractionate by reversed-phase high performance liquid chromatography (RP-HPLC), seven antioxidant peptides were isolated, The F2-5 peptide displayed the highest DPPH radical-scavenging activity (58.2±1.63%; at 250 μg/ml) among these peptides, the amino acids composition of F2-5 was determined, which might play an important role on its antioxidant activity. In addition, purified peptide did show remarkable inhibition rate on SGC-7901 cells proliferation, and it also revealed the dose-dependent relationship. The results of this study suggest that rice bran protein hydrolysates are good source of natural antioxidants.
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Claustre, Jean, Férial Toumi, Aurélien Trompette, Gérard Jourdan, Henri Guignard, Jean Alain Chayvialle, and Pascale Plaisancié. "Effects of peptides derived from dietary proteins on mucus secretion in rat jejunum." American Journal of Physiology-Gastrointestinal and Liver Physiology 283, no. 3 (September 1, 2002): G521—G528. http://dx.doi.org/10.1152/ajpgi.00535.2001.
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The hypothesis that dietary proteins or their hydrolysates may regulate intestinal mucin discharge was investigated in the isolated vascularly perfused rat jejunum using an enzyme-linked immunosorbent assay for rat intestinal mucins. On luminal administration, casein hydrolysate [0.05–5% (wt/vol)] stimulated mucin secretion in rat jejunum (maximal response at 417% of controls). Lactalbumin hydrolysate (5%) also evoked mucin discharge. In contrast, casein, and a mixture of amino acids was without effect. Chicken egg albumin and its hydrolysate or meat hydrolysate also did not modify mucin release. Interestingly, casein hydrolysate-induced mucin secretion was abolished by intra-arterial TTX or naloxone (an opioid antagonist). β-Casomorphin-7, an opioid peptide released from β-casein on milk ingestion, induced a strong mucin secretion (response at 563% of controls) that was inhibited by naloxone. Intra-arterial β-casomorphin-7 also markedly increased mucin secretion (410% of controls). In conclusion, two enzymatic milk protein hydrolysates (casein and lactalbumin hydrolysates) and β-casomorphin-7, specifically, induced mucin release in rat jejunum. The casein hydrolysate-induced mucin secretion is triggered by a neural pathway and mediated by opioid receptor activation.
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Abioye, Raliat O., Caleb Acquah, Pei Chun Queenie Hsu, Nico Hüttmann, Xiaohong Sun, and Chibuike C. Udenigwe. "Self-assembly and Hydrogelation Properties of Peptides Derived from Peptic Cleavage of Aggregation-prone Regions of Ovalbumin." Gels 8, no. 10 (October 9, 2022): 641. http://dx.doi.org/10.3390/gels8100641.
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Egg white protein hydrolysate generated with pepsin was investigated for the presence of peptides with self-assembly and hydrogelation properties. Incubation of the hydrolysates for 16 h resulted in aggregates with significantly (p < 0.05) lower free amino nitrogen and sulfhydryl contents, and higher particle diameter and surface hydrophobicity compared to the hydrolysates. LC-MS/MS analysis of the aggregates resulted in identification of 429 ovalbumin-derived peptides, among which the top-six aggregation-prone peptides IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, YCPIAIMSA, MMYQIGLF, and VYSFSLASRL were predicted using AGGRESCAN by analysis of the aggregation “Hot Spots”. NIFYCPIAIM had the highest thioflavin T fluorescence intensity, particle diameter (5611.3 nm), and polydispersity index (1.0) after 24 h, suggesting the formation of β-sheet structures with heterogeneous particle size distribution. Transmission electron microscopy of MMYQIGLF, and VYSFSLASRL demonstrated the most favorable peptide self-assembly, based on the formation of densely packed, intertwined fibrils. Rheological studies confirmed the viscoelastic and mechanical properties of the hydrogels, with IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, and VYSFSLASRL forming elastic solid hydrogels (tan δ < 1), while YCPIAIMSA and MMYQIGLF formed viscous liquid-like hydrogels (tan δ > 1). The results provide valuable insight into the influence of peptide sequence on hydrogelation and self-assembly progression, and prospects of food peptides in biomaterial applications.
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Bougatef, Hajer, Cristina de la Vega-Fernández, Assaad Sila, Ali Bougatef, and Oscar Martínez-Alvarez. "Identification of ACE I-Inhibitory Peptides Released by the Hydrolysis of Tub Gurnard (Chelidonichthys lucerna) Skin Proteins and the Impact of Their In Silico Gastrointestinal Digestion." Marine Drugs 21, no. 2 (February 17, 2023): 131. http://dx.doi.org/10.3390/md21020131.
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Tub gurnard is a highly abundant fishery species caught as a discard in the Mediterranean Sea. This work proposes its valorisation through the release of potential antihypertensive peptides and glycosaminoglycans (GAGs) through the controlled hydrolysis of tub gurnard skin proteins. Four proteases (Esperase, Alcalase, Trypsin and Pronase E) were used to obtain potent angiotensin converting enzyme I (ACE)-inhibitory hydrolysates. Peptides and GAGs were separated and evaluated for their antihypertensive potential by fluorometry. The peptide-rich fractions derived from the Esperase and Alcalase hydrolysates showed very low IC50 values (47 and 68 μg/mL, respectively). Only the GAGs from the Trypsin and Esperase hydrolysates were relevant ACE inhibitors (63 and 52% at 1 mg/mL, respectively). The peptide composition of the most potent ACE-inhibitory fractions derived from the Esperase and Alcalase hydrolysates (IC50 values of 33 and 29 μg/mL, respectively) was analysed by RP-LC-ESI-MS/MS. The analysis suggests that the ACE-inhibitory activity is related to the peptide hydrophobicity, as well as to the presence of specific residues at any of the last four C-terminal positions. The in silico gastrointestinal digestion of these fractions yielded small peptides with antihypertensive potential.
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Martin Alain, Mune Mune. "Prediction and Evaluation of Bioactive Properties of Cowpea Protein Hydrolysates." Journal of Food Biochemistry 2023 (February 13, 2023): 1–12. http://dx.doi.org/10.1155/2023/9095113.
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Cowpea protein hydrolysates were prepared using thermolysin, alcalase, and trypsin and analysed for bioactive properties, and then, the release of bioactive peptides was investigated in silico. It was found that the degree of hydrolysis reached 48% after 24 h hydrolysis with alcalase. The hydrolysate prepared using alcalase showed higher ACE inhibitory (62%) and DPPH scavenging activity (19%). SDS-PAGE analysis revealed that vignin was the major protein in cowpea protein isolate. In silico analysis indicated the presence of potential bioactive peptides with potent bioactivity in the primary structure of proteins. The 3D structure of proteins was built, upon which bioactive peptides were mapped using their location in the primary structure. The secondary structure and solvent accessible surface around each bioactive peptide were then calculated. On this basis, the higher degree of hydrolysis and bioactive properties of cowpea protein hydrolysate prepared by alcalase were explained, and structural factors influencing the release of bioactive peptides were investigated.
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Pavlovic, Neda, Jelena Jovanovic, Verica Djordjevic, Bojana Balanc, Branko Bugarski, and Zorica Knezevic-Jugovic. "Production and characterization of liposomes with encapsulated bioactive soy protein hydrolysate." Chemical Industry 74, no. 5 (2020): 327–39. http://dx.doi.org/10.2298/hemind200530030p.
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Soy proteins known for their high nutritional value and pronounced techno-functional properties, can be hydrolyzed by using proteolytic enzymes and thus converted into hydrolysates rich in di-, tri- and oligopeptides. The resulting peptides are carriers of valuable biological activities, which make the soy hydrolysates very important in functional food applications as techno-functional and bioactive ingredients. However, commercial incorporation and application of soy protein hydrolysates can be hinderedby their low bioavailability and instability, bitter taste, hygroscopicity and possibility to interact with the food matrix. The aim of this research is encapsulation of the soy protein hydrolysate in liposomes in order to overcome the stated shortcomings, while preserving the biological activities that protein hydrolysates exhibit. The soy hydrolysate was prepared by a two-step enzymatic hydrolysis of a soy protein concentrate using commercial food-grade proteases, endoprotease from Bacillus amyloliquefaciens (Neutrase?) and egzo- and endoprotease from Aspergillus oryzae (Flavourzyme?) and encapsulated within liposomes. The liposomes were produced by a thin film method using a commercial lipid mixture (Phospolipon? 90G) containing mainly phosphatidylcholine. Next, the obtained multilamellar vesicles (MLV) with the soy protein hydrolysate were treated by high-intensity ultrasound waves generated by using (1) an ultrasonic probe at a frequency of 20 kHz and (2) an ultrasonic bath with a frequency 40 kHz. The smallest (310 nm) and uniform (unimodal size distribution) liposomes with the highest efficiency of peptide encapsulation (19 %) were obtained by the probe sonication. The presented results showed that incorporation of the soy protein hydrolysates was achieved within the liposome membrane and caused an increase in the liposome size in all tested formulations, namely: from 297 to 310 nm by using the ultrasonic probe, from 722 to 850 nm by using the ultrasonic bath, while in formulations without the ultrasonic treatments the increase from 2818 to 3464 nm was recorded. The entrapped peptides caused enlargement of all liposomes and the increase in negative charge of zeta potential values, which in the case of MLV liposomes was below -30 mV, indicating high stability of these liposomes. Significant antioxidant activity of the probe-sonicated liposomal formulation was confirmed by the ABTS scavenging ability and iron-chelating activity. Release studies conducted under simulated gastrointestinal conditions confirmed that liposomes provide prolonged release of encapsulated soy protein hydrolysates as compared to diffusion of the free hydrolysate. In the first 75 min, only 20 % of liposome encapsulated soy peptides diffused, which is 2.2-fold lower as compared to the diffusion of the non-encapsulated soy hydrolysate. Liposome encapsulated soy protein hydrolysates may provide the possibility for application in the areas such as food science and technology, with the aim to enhance the nutritional value and shelf life of food products, and develop functional foods.
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Zhao, Lei, Yang-Chao Luo, Cheng-Tao Wang, and Bao-Ping Ji. "Antioxidant Activity of Protein Hydrolysates from Aqueous Extract of Velvet Antler (Cervus elaphus) as Influenced by Molecular Weight and Enzymes." Natural Product Communications 6, no. 11 (November 2011): 1934578X1100601. http://dx.doi.org/10.1177/1934578x1100601130.
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The crude protein hydrolysates from aqueous extract of velvet antler (AEVA) were prepared by simulated gastrointestinal digestion (SGI, pepsin-pancreatin) using pancreatin-pepsin, alcalase and neutrase. The resulting hydrolysates were separated by sequential ultrafiltration into four fractions. The antioxidant activities of peptide fractions were evaluated by 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, ferric reducing antioxidant power (FRAP), 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging and Fe2+-chelating assays. Results showed that the hydrolysate prepared by SGI had a low degree of hydrolysis, which was significantly improved with altered proteases, such as pancreatin-pepsin and alcalase. Antioxidant activities of peptide fractions varied with molecular weight (MW) and the enzyme used. Generally, low-MW peptide fractions had higher ABTS radical scavenging activity and Fe2+-chelating ability, and high-MW peptide fractions were more effective in DPPH radical scavenging activity and reducing power.
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Miyamoto, Honoka, Erwina Safitri, Takeshi Nagai, and Masataka Saito. "Characterization of Fish Skin Hydrolysates Exhibiting Dipeptidyl Peptidase IV Inhibitory Activity." Indonesian Food and Nutrition Progress 1, no. 1 (May 8, 2024): 1. http://dx.doi.org/10.22146/ifnp.88534.
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Dipeptidyl peptidase IV (DPP-IV) inhibitors are antidiabetic drugs that can lower blood sugar levels. There are still few reports on the DPP-IV inhibitory activity of peptides obtained from discarded fish skin. Therefore, we prepared various enzymatic hydrolysates using the skins of six fish species and investigated their DPP-IV inhibitory effects. As a result, it was found that the DPP-IV inhibitory activity of yellowtail hydrolysate by Alcalase was higher than that of other enzymes. In addition, the IC50 after ethanol fractionation was found to be lower in yellowtail and eel skin hydrolysate. Amino acid composition analysis showed that the hydrolysate obtained from the skin of the yellowtail contained the highest amount of Gly, followed by Pro, Hyp, and Ala, indicating that it was a peptide derived from type I collagen. Fractionation with ethanol showed that the DPP-IV inhibitory components were contained in the low molecular weight fraction. The artificial digestion test observed no DPP-IV inhibitory activity or average molecular weight change. The DPP-IV inhibitory peptide obtained from fish skin has the potential to be applied as a food material to various food products.
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Xiong, Jun Juan, Li Jun Ding, and Xue Ling Lai. "Antioxidative Activity of Protein Hydrolysates from Spanish Mackerel by Alcalase." Advanced Materials Research 236-238 (May 2011): 2890–93. http://dx.doi.org/10.4028/www.scientific.net/amr.236-238.2890.
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To utilize low-value fish, Spanish mackerel protein was hydrolyzed using alcalase for production of antioxidant peptide. The antioxidant activities of antioxidant peptide from Spanish mackerel protein were evaluated. Results: The radical-scavenging properties on hydroxyl and superoxide of protein hydrolysates were 53.11% and 23.1%. And their reducing power was increased with the peptide content of the hydrolysates. The hydrolysates significantly inhibited lipid peroxidation in linoleic acid emulsion system, and effectively inhibit autoxidation of linoleic acid; and the inhibition ability increased with the increasing of peptide content in hydrolysates. The hydrolysates inhibited the activity of LOX to a certain extent. Conclusion: The hydrolysates from Spanish mackerel protein exhibited high antioxidative activity.