Academic literature on the topic 'Peptide hydrolysates'
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Journal articles on the topic "Peptide hydrolysates"
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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.
Dissertations / Theses on the topic "Peptide hydrolysates"
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Shirako, Saki. "Structure and biological activities of hydrophobic short chain pyroglutamyl peptides in fermented foods and food protein hydrolysates." Kyoto University, 2020. http://hdl.handle.net/2433/253335.
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Kyoto University (京都大学)0048
新制・課程博士
博士(農学)
甲第22499号
農博第2403号
新制||農||1077(附属図書館)
学位論文||R2||N5279(農学部図書室)
京都大学大学院農学研究科応用生物科学専攻
(主査)教授 佐藤 健司, 教授 菅原 達也, 准教授 豊原 治彦
学位規則第4条第1項該当
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Outman, Ahlam. "Production de peptides anticancéreux à partir des hydrolysats d'hémoglobine humaine et bovine, avec des propriétés additionnelles antibactériennes et antioxydantes." Electronic Thesis or Diss., Université de Lille (2022-....), 2023. http://www.theses.fr/2023ULILR082.
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L'hémoglobine, la protéine prédominante dans le cruor, responsable de la couleur rouge du sang chez les mammifères, est reconnue pour être une source riche en peptides bioactifs après hydrolyse par la pepsine porcine. Ces peptides sont principalement connus pour leurs propriétés antimicrobiennes. Cependant, ces derniers se démarquent par leur capacité à cibler spécifiquement les cellules cancéreuses tout en préservant les cellules saines à prolifération rapide. Cette thèse vise à élaborer une stratégie de valorisation de l'hémoglobine humaine et bovine, en produisant des peptides bioactifs, puis en explorant leur potentiel dans la lutte contre le cancer, tout en évaluant leurs propriétés anticancéreuses, antibactériennes et antioxydantes.Dans ce travail, le potentiel de l'hémoglobine humaine à contenir des peptides bioactifs a d'abord été étudié in silico en comparaison avec l'hémoglobine bovine à l'aide d'outils bioinformatiques. Les résultats de blast ont montré une identité élevée, 88% et 85% respectivement, indiquant une forte similarité entre les chaînes α et β. Les conditions d'hydrolyse enzymatique (23°C, E/S = 1/11, pH 3,5) ont été validé sur l'hémoglobine humaine et a permis une production efficace du peptide α137-141. En effet, plus de 60% de la production totale de peptides α137-141 est obtenue en seulement 30 minutes d'hydrolyse, atteignant un pic de production à 3 h. De plus, le mécanisme d'hydrolyse enzymatique de ces deux types d'hémoglobine suit un schéma similaire, selon un mécanisme zipper.L'hydrolyse enzymatique a également été réalisée à hautes concentrations en hémoglobine (1, 2, 8 et 10%, p/v), permettant de produire l'α137-141 à grande échelle.Ensuite, les résultats ont montré une forte activité antimicrobienne des hydrolysats peptidiques contre six souches bactériennes, indépendamment du niveau de concentration initiale du substrat. Les hydrolysats ont également montré une forte activité antioxydante, mesurée par quatre tests différents. De plus, les activités antimicrobiennes et antioxydantes des hydrolysats d'hémoglobine humaine et bovine ont montré peu ou pas de différence significative, seul le niveau de concentration étant le facteur déterminant de leur activité.Le potentiel anticancéreux des peptides bioactifs issus de l'hydrolyse enzymatique de l'hémoglobine a été étudié. Les résultats obtenus à travers deux approches distinctes ont mis en lumière leur potentiel prometteur en tant qu'agents anticancéreux. L'investigation de paramètres clés tels que la concentration initiale d'hémoglobine, le degré d'hydrolyse et les caractéristiques structurales des peptides antimicrobiens avait mis en évidence l'influence de ces facteurs sur l'activité antimitotique des peptides. Le peptide α137-141 se distingue par une forte inhibition de la croissance des radicelles, avec des valeurs d'IC50 exceptionnellement basses, soit 10 à 15 fois supérieures à d'autres fractions, attribuées à son fort potentiel antimicrobien. Les analyses in vitro ont renforcé l'hypothèse selon laquelle l'inhibition de la synthèse protéique joue un rôle essentiel dans le mécanisme anticancéreux de ces peptides.Enfin, les résultats de l'étude par spectrométrie de masse ont montré la présence d'un certain nombre de peptides bioactifs, dont la majorité présente des caractéristiques similaires à celles mentionnées dans la littérature. De nouveaux peptides bioactifs ont également été identifiés dans l'hémoglobine humaine, tels que les peptides antibactériens PTTKTYFPHF (α37-46), FPTTKTYFPH (α36-45), TSKYR (α137-141) et STVLTSKYR (α133-141), ainsi que l'antioxydant TSKYR (α137-141) dont trois autres peptides opioïdes, un inhibiteur de l'ECA, un agent anticancéreux. Cette thèse offre une nouvelle approche innovante, combinant des propriétés antimicrobiennes, antioxydantes et anticancéreuses, ouvrant la voie à des traitements plus efficaces et moins nocifs pour les patientsHemoglobin, the predominant protein in cruor responsible for the red colour of mammalian blood, is known to be a rich source of bioactive peptides after hydrolysis by porcine pepsin. These peptides are mainly known for their antimicrobial properties. However, these peptides stand out for their ability to specifically target cancer cells while preserving rapidly proliferating healthy cells. The aim of this thesis is to develop a strategy for adding value to human and bovine haemoglobin by producing bioactive peptides and then exploring their potential in the fight against cancer, while assessing their anti-cancer, anti-bacterial and antioxidant properties.In this work, the potential of human hemoglobin to contain bioactive peptides was first studied in silico in comparison with bovine hemoglobin using bioinformatics tools. Blast results showed high identity, 88% and 85% respectively, indicating high similarity between α and β chains. The enzymatic hydrolysis conditions (23°C, E/S = 1/11, pH 3.5) were validated on human hemoglobin and enabled efficient production of the α137-141 peptide. Indeed, more than 60% of the total α137-141 peptide production was obtained in just 30 minutes of hydrolysis, reaching a production peak at 3 h. Furthermore, the mechanism of enzymatic hydrolysis of these two types of haemoglobin follows a similar pattern, according to a zipper mechanism. Enzymatic hydrolysis was also performed at high haemoglobin concentrations (1, 2, 8 and 10%, w/v), enabling large-scale production of α137-141.Next, the results showed strong antimicrobial activity of the peptide hydrolysates against six bacterial strains, independent of the initial substrate concentration level. The hydrolysates also showed strong antioxidant activity, measured by four different tests. In addition, the antimicrobial and antioxidant activities of the human and bovine haemoglobin hydrolysates showed little or no significant difference, with only the concentration level being the determining factor in their activity.The anticancer potential of bioactive peptides derived from the enzymatic hydrolysis of haemoglobin was studied. The results obtained using two distinct approaches highlighted their promising potential as anti-cancer agents. The investigation of key parameters such as the initial concentration of haemoglobin, the degree of hydrolysis and the structural characteristics of the antimicrobial peptides highlighted the influence of these factors on the antimitotic activity of the peptides. The α137-141 peptide stood out for its strong inhibition of rootlet growth, with exceptionally low IC50 values, 10 to 15 times higher than other fractions, attributed to its strong antimicrobial potential. In vitro analyses reinforced the hypothesis that inhibition of protein synthesis plays an essential role in the anti-cancer mechanism of these peptides.Finally, the results of the mass spectrometry study showed the presence of a number of bioactive peptides, the majority of which have characteristics similar to those reported in the literature. New bioactive peptides were also identified in human hemoglobin, such as the antibacterial peptides PTTKTYFPHF (α37-46), FPTTKTYFPH (α36-45), TSKYR (α137-141) and STVLTSKYR (α133-141), as well as the antioxidant TSKYR. (α137-141) including three other opioid peptides, an ACE inhibitor, an anticancer agent. This thesis offers a new innovative approach, combining antimicrobial, antioxidant and anticancer properties, paving the way for more effective and less harmful treatments for patients
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Groleau, Paule Émilie. "Étude des interactions peptide-peptide dans un mélange de peptides issu d'un hydrolysat trypsique de ¿-lactoglobuline et de leur influence sur le fractionnement par nanofiltration." Doctoral thesis, Université Laval, 2003. http://hdl.handle.net/20.500.11794/17853.
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Les hydrolysats enzymatiques de protéines de lactosérum sont riches en peptides fonctionnels et bioactifs, ce qui justifient l’intérêt de les fractionner afin de concentrer ou purifier ces molécules. Les techniques membranaires présentent un fort potentiel pour la séparation de ces hydrolysats à l’échelle industrielle, mais des interactions peptide-peptide semblent affecter leur efficacité. Cette étude visait donc à caractériser les interactions peptide-peptide dans un mélange de peptides issus d’un hydrolysat trypsique de β-LG, à identifier les conditions physico-chimiques et les peptides responsables de ces interactions, puis à évaluation l’influence de ces interactions sur le fractionnement de cet hydrolysat par nanofiltration. La focalisation isoélectrique a d’abord été utilisée pour fractionner l’hydrolysat et a permis de démontrer la formation d’agrégats peptidiques à pH acide. Une étude de turbidimétrie a par la suite mis en évidence la solubilité de l’hydrolysat en fonction du pH et de certaines conditions physico-chimiques. Les agrégats obtenus à pH 4 ont été centrifugés et séparés, puis les peptides responsables de cette agrégation ont été identifiés. Parmi ces peptides, la présence de fragments chymotrypsiques a justifié une étude subséquente sur l’activité résiduelle chymotrypsique dans la préparation trypsique, et son impact sur le phenomène d’agrégation des peptides à pH acide. La dernière partie de cette étude a permis d’évaluer l’impact des agrégats peptidiques sur le fractionnement par nanofiltration de l’hydrolysat trypsique de β-LG. Il a été démontré que les interactions peptide-peptide ne nuisent pas au fractionnement, mais semblent plutôt être bénéfiques, et ce en modifiant la couche de polarisation créée en cours de filtration.Whey protein enzymatic hydrolysates contain several functional and bioactive peptides which justify their fractionatation to isolate such interesting molecules. Membrane separation technologies have an excellent potential for peptide separation but peptide-peptide interactions seem to reduce their efficiency. The objectives of this study were to demonstrate the occurrence of peptide-peptide interactions in a tryptic hydrolysate of β-LG, to identify the optimal physico-chemical conditions and peptides responsible of such interactions, as well as to evaluate the influence of such interactions on the fractionation of this hydrolysate by nanofiltration. Isoelectric focusing was used to fractionate the hydrolysate and to demonstrate a peptidic aggregation phenomena at acidic pH. Turbidimetry was then used to highlight the solubility of the hydrolysate according to the pH and some physico-chemical conditions. Peptide aggregates formed at pH 4 were centrifuged and separated, and peptides responsible for this aggregation were identified. From these peptides, the presence of chymotryptic peptides has justified a study of the impact of residual chymotryptic activity in the tryptic preparation on the aggregation phenomena. The second part of this work allowed the evaluation of the effect of these aggregates on the fractionation of the tryptic hydrolysate of β-LG by nanofiltration. It was shown that peptide-peptide interactions do not impair the fractionation. On the contrary, these interactions taking place in the polarized layer may have a positive impact on the fractionation.
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Cho, Myong J. "Characterization of bitter peptides from soy protein hydrolysates /." free to MU campus, to others for purchase, 2000. http://wwwlib.umi.com/cr/mo/fullcit?p9998475.
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Onuh, John Oloche. "Antihypertensive and Antioxidant Properties of Chicken Skin Protein Hydrolysates: In vitro, in vivo, and Metaboloics Studies." Elsevier Publishers, Inc, 2013. http://hdl.handle.net/1993/30628.
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The objective of this work was to produce bioactive peptides from the enzymatic hydrolysis of chicken skin proteins that could be used to treat hypertension, oxidative stress and associated health conditions using a metabolomics approach. Enzymatic hydrolysis of chicken thigh and breast muscle skin proteins was carried out using alcalase or a combination of pepsin/pancreatin (PP) at 1–4% enzyme concentrations. Chicken skin protein hydrolysates (CSPH) were each fractionated by membrane ultrafiltration into different molecular weight peptides (<1, 1–3, 3–5 and 5–10 kDa). Investigation of their in vitro antihypertensive and antioxidant activities showed that alcalase hydrolysates had significantly (p < 0.05) higher ACE-inhibitory activity compared to PP hydrolysates. ACE inhibition was inversely related to size of ultrafiltration membrane peptides. Renin-inhibitory activity varied from 15–36%, and was dependent on the type of protease; PP hydrolysates showed significantly (p < 0.05) higher inhibition than alcalase hydrolysates. CSPHs also significantly (p < 0.05) scavenged antioxidant radicals, increasing with enzyme concentration but decreased as peptide size increased. Kinetics studies revealed that peptide-dependent enzyme inhibition pattern was mostly of the mixed-type for both ACE and renin. Short-term (24 hr) oral administration of 100 mg peptides/kg body weight to spontaneously hypertensive rats (SHRs) led to maximum systolic blood pressure (SBP) reduction of –32.67 and –31.33 mmHg after 6 h for chicken thigh skin hydrolysate and chicken breast skin hydrolysate, respectively. During a 6-week feeding trial, CSPH at 1.0 and 0.5% feed substitutions had significant (p<0.05) antihypertensive effects in SHRs (-36 and -31 SBP reductions, respectively). SBP reduction was directly related to lower plasma ACE but not renin activity. Plasma total antioxidant capacity of the rats was also high. Metabolomics analysis revealed several metabolites with significant changes (≥ 2-fold changes, p < 0.05) in urine and plasma of SHRs fed CSPH, such as Symmetric Dimethylarginine (SDMA), N2-acetyl-L-ornithine, buthionine sulfoximine, uric acid, Vitamin E succinate, L-isoleucine and phospholipids which may be considered important biomarkers/pathways for hypertension and oxidative stress. We conclude that CSPHs may be used as ingredients to formulate functional foods and nutraceuticals for the management of oxidative stress and hypertension-related diseases.October 2015
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Le, Coeur Catherine. "Contribution à l'étude d'un hydrolysat pepsique de myoglobine de muscle squelettique rouge de thon Thunnus Albacares : caractérisation des peptides issus de l'hydrolyse étude de l'association hème-peptide." La Rochelle, 1996. http://www.theses.fr/1996LAROS011.
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L’hydrolyse pepsique de la myoglobine de muscle squelettique rouge de thon Thunnus Albacares génère un mélange de peptides et d'heme. En vue de caractériser les peptides de cet hydrolysat, nous les avons purifiés par une méthode de chromatographie liquide haute performance mise au point au laboratoire. Il a ainsi été montré que la chromatographie d'exclusion, associée à la chromatographie en phase inverse permettait de résoudre efficacement ce mélange de peptides, malgré sa complexité. La composition en acides aminés des peptides a été déterminée par la méthode du picotag complétée par la méthode de la dérivée seconde qui est une méthode spectrale permettant de détecter et de quantifier les acides aminés aromatiques. La séquence des peptides a ensuite été déduite de la comparaison de leur composition en acides aminés avec la séquence connue de la myoglobine de thon. Ce travail nous a permis de définir les sites de coupure de la pepsine dans nos conditions expérimentales et de les comparer avec ceux décrits dans la littérature. La recherche de peptides actifs n'a pas permis de mettre en évidence dans notre mélange de peptides opioïdes, ni de peptides activateur ou inhibiteur de la croissance cellulaire. Par contre, certaines fractions peptidiques présentent une activité inhibitrice de l'enzyme de conversion de l'angiotensine et d'autres une activité inhibitrice des contractions de l'iléon de cobaye. Des fractions présentent en outre une capacité de fixation de l'heme supérieure à celle de la molécule native. Le type de liaisons existant entre l'heme et les peptides en mélange n'a pas été clairement défini, mais il semblerait que l'heme se lie aux peptides, non pas par des liaisons fortes de type covalentes mais plutôt par des liaisons faibles, facilement détruites lors des processus de purification ou simplement par variation de PH.
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Sion, Ludivine. "Bio production à l’échelle pilote d’un hydrolysat peptidique à partir de sang entier bovin et porcin pour l’industrie du Petfood et l’alimentation animale : Identification et caractérisation des peptides actifs." Thesis, Lille, 2019. http://www.theses.fr/2019LIL1R023.
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Le sang brut issu des abattoirs est une source importante de protéines. Il est actuellement peu valorisé, essentiellement par séchage ou par récupération de molécules plasmatiques après séparation centrifuge du plasma et du cruor. Ce co-produit est principalement composé d’hémoglobine, protéine riche en peptides actifs, tels que les peptides antimicrobiens, après hydrolyse par la pepsine porcine. L’objectif est de proposer une nouvelle stratégie de valorisation du sang, sans séparation plasma-cruor, tout en conservant les peptides bioactifs historiquement identifiés lors de l’hydrolyse pepsique de l’hémoglobine purifiée. Cette nouvelle voie, mise au point puis optimisée à l’échelle laboratoire, a été technologiquement transférée à l’échelle pilote. L’hydrolyse pepsique du sang a été premièrement mise au point à la concentration de 1% (p/v) en hémoglobine. Cette hydrolyse a mis en évidence la coexistence des mécanismes enzymatiques de type zipper et one-by-one pour l’apparition de la population peptidique. Les conditions d’hydrolyses (concentration en hémoglobine, choix de la pepsine, rapport enzyme-substrat, acide et temps d’hydrolyse) ont été optimisées en fixant une décoloration complète de l’hydrolysat ainsi que la conservation de la population peptidique. L’hydrolysat bioactif ainsi obtenu présente des propriétés antimicrobiennes et antioxydantes. Son analyse par spectrométrie de masse a permis la caractérisation de cet hydrolysat en terme de peptides issus de l’hémoglobine. Il ne possède aucune masse supérieure à 10 kDa, lui procurant ainsi une bonne digestibilité: son utilisation en alimentation animale en tant que complément alimentaire apparaît prometteuseRaw blood from slaughterhouses is an important source of proteins. This co-product, currently undervalued, is mainly composed of hemoglobin, a protein rich in active peptides such as antimicrobial peptides, after hydrolysis by porcine pepsin.The aim of this thesis is to propose a new strategy for the valorization of whole blood, without plasma-cruor separation. Preservation of identified bioactive peptides by pepsic hydrolysis of purified hemoglobin is required. This new way of blood valorization, developed and then optimized at laboratory scale, has been technologically transferred on a pilot scale (80 L).The pepsic hydrolysis of 70% bovine 30% porcine blood was first developed at 1% (w/v) of hemoglobin (23°C, 200 mL). This hydrolysis has demonstrated the coexistence of zipper and one by one enzymatic mechanism for the appearance of the peptide population. Hydrolysis parameters (hemoglobin concentration, industrial grade pepsin, enzyme-substrate proportion, acid allowing the sustainability of the hydrolysis pH and hydrolysis time) were optimized by fixing a complete discoloration of the hydrolysate as well as the preservation of the peptide population.The bioactive hydrolysate thus obtained contains antimicrobial and antioxidant properties. Mass spectrometry analysis has shown the hydrolysate composition in terms of peptides derived from hemoglobin. No mass above 10 kDa have been found, providing it with a good digestibility: its use in pet food as a food supplement seems promising
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Mas, Capdevila Anna. "Hydrolysates and peptides from chicken foot proteins to manage hypertension." Doctoral thesis, Universitat Rovira i Virgili, 2018. http://hdl.handle.net/10803/666287.
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La hipertensió arterial es considera un dels problemes de salut pública més importants en la nostra societat. El tractament d’aquesta patologia es basa en una combinació de canvis en l’estil de vida i tractament farmacològic. No obstant, per aquells pacients en fases de desenvolupament de la malaltia i que encara no necessiten tractament farmacològic, l’ús de nutricèutics o aliments funcionals amb propietats antihipertensives està rebent molta atenció ja que podria ser una bona estratègia per evitar el desenvolupament de la hipertensió.
En aquest sentit, aquesta tesi té com a objectiu principal l’obtenció de pèptids antihipertensius a partir de la hidròlisi de proteïnes de pota de pollastre, un subproducte de la indústria avícola. Així, mitjançant la hidròlisi de la proteïnes de pota de pollastre sota condicions d’hidròlisi optimitzades es va obtenir un hidrolitzat, Hpp11, que mostrava efecte antihipertensiu després d’una administració aguda i crònica. L’hidrolitzat Hpp11 administrat agudament produïa l’efecte antihipertensiu mitjançant la reducció de l’activitat de l’enzim convertidor d’angiotensina, mentre que després d’una administració crònica, l’efecte antihipertensiu estava mediat per una millora en la funció endotelial. Addicionalment es van caracteritzar els pèptids presents en l’Hpp11 i dos d’ells, AVFQHNCQE i QVGPLIGRYCG van mostrar efecte antihipertensiu. En particular, el pèptid AVFQHNCQE no era absorbit i produïa el seu efecte antihipertensiu mitjançant la interacció amb receptors opioides presents en el tracte gastrointestinal. La interacció aquests receptors desencadenava un efecte antihipertensiu mediat pel vasodilatador òxid nítric, del qual se’n veia augmentada la seva biodisponibilitat gràcies a l’efecte antioxidant i de millora de la funció endotelial que també mostrava el pèptid.
Els resultats d’aquesta tesi obren les portes a l’ús del l’hidrolitzat i dels pèptids antihipertensius obtinguts en aliments funcionals o nutricèutics que permetrien el control i prevenció del desenvolupament de la hipertensió.La hipertensión arterial se considera uno de los problemas de salud pública más importante de nuestra sociedad. El tratamiento de esta patología se basa en una combinación de cambios en el estilo de vida y tratamiento farmacológico. No obstante, para esos pacientes que se encuentran en fase de desarrollo de la enfermedad i que aún no requieren de tratamiento farmacológico, el uso de nutraceuticos o alimentos funcionales con propiedades antihipertensivas está recibiendo mucha atención ya que podrían ser una buena estrategia para evitar el desarrollo de la hipertensión. En este sentido, esta tesis tiene como objetivo principal la obtención de péptidos antihipertensivos a partir de la hidrólisis de proteínas de pata de pollo, un subproducto de la industria avícola. Así, mediante la hidrólisis de las proteínas de la pata de pollo bajo condiciones de hidrólisis optimizadas se obtuvo un hidrolizado, Hpp11, que mostró efecto antihipertensivo después de una administración aguda y crónica. El hidrolizado Hpp11 administrado agudamente producía el efecto antihipertensivo mediante la reducción de la actividad de la enzima convertidora de angiotensina, mientras que después de su administración crónica, el efecto antihipertensivo estaba mediado por una mejora en la función endotelial. Adicionalmente se caracterizaron los péptidos presentes en Hpp11 y dos de ellos AVFQHNCQE y QVGPLIGRYCG mostraron efecto antihipertensivo. En particular, el péptido AVFQHNCQE no era absorbido y producía su efecto antihipertensivo mediante la interacción con receptores opioides presentes en el tracto gastrointestinal. La interacción con estos receptores desencadenaba un efecto antihipertensivo mediado por el vasodilatador óxido nítrico, del cual se veía aumentada su biodisponibilidad gracias al efecto antioxidante y de mejora de la función endotelial que también mostró el péptido. Los resultados de esta tesis abren las puertas al uso del hidrolizado y de los péptidos antihipertensivos obtenidos en alimentos funcionales o nutraceuticos que permitirían el control y prevención del desarrollo el a hipertensión.
Hypertension is considered one of the most important public health problems in our society. The treatment of this pathology is based on lifestyle modifications and pharmacology treatment. However, for those patients developing hypertension, whose blood pressure is not high enough to warrant pharmacology treatment, the use nutraceuticals or functional foods with antihypertensive properties have attracted considerable interest as good strategy to avoid the development of hypertension In this regard, this thesis aims to obtain antihypertensive peptides through the hydrolysis of chicken foot proteins, a by-product from poultry industries. Thus, through the hydrolysis of chicken foot proteins, it was obtained an hydrolysate, Hpp11, exerting antihypertensive effect after acute and chronic administration. Hpp11 administered acutely produced antihypertensive effect by reducing the activity of angiotensin converting enzyme, while when administered chronically the antihypertensive effect was mediated by an improvement in the endothelial function. Additionally the peptides contained in Hpp11 were characterised and two of them, AVFQHNCQE and QVGPLIGRYCG, showed antihypertensive effect. In particular, the peptide AVFQHNCQE was not absorbed and produced its antihypertensive effect through the interaction with opioid receptors from the gastrointestinal tract. The interaction with those receptors leaded to a nitric oxide-mediated antihypertensive effect. Moreover, the peptide contributed to enhance nitric oxide by exhibiting antioxidant effect and improving endothelial function. The results of this thesis open the doors to the use of the antihypertensive hydrolysate and peptides in functional foods or nutraceuticals for the control and prevention of hypertension.
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Geisenhoff, Heidi. "Bitterness of soy protein hydrolysates according to molecular weight of peptides." [Ames, Iowa : Iowa State University], 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:1473208.
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Gibbs, Bernard F. "Production and characterization of bioactive peptides from soy fermented foods and their hydrolysates." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/NQ50171.pdf.
Full textBook chapters on the topic "Peptide hydrolysates"
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McCalla, Jeff, Terry Waugh, and Eric Lohry. "Protein Hydrolysates/Peptides in Animal Nutrition." In Protein Hydrolysates in Biotechnology, 179–90. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6674-0_10.
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Hou, Yongqing, Zhenlong Wu, Zhaolai Dai, Genhu Wang, and Guoyao Wu. "Protein Hydrolysates in Animal Nutrition." In Bioactive Peptides from Food, 209–32. Boca Raton: CRC Press, 2022. http://dx.doi.org/10.1201/9781003106524-14.
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Batista, Irineu. "Biological Activities of Fish-protein Hydrolysates." In Marine Proteins and Peptides, 111–38. Chichester, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118375082.ch6.
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Fitzgerald, R. J., and H. Meisel. "Milk Protein Hydrolysates and Bioactive Peptides." In Advanced Dairy Chemistry—1 Proteins, 675–98. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-8602-3_20.
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Nongonierma, A. B., M. B. O’Keeffe, and R. J. FitzGerald. "Milk Protein Hydrolysates and Bioactive Peptides." In Advanced Dairy Chemistry, 417–82. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-2800-2_15.
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Shiratsuchi, Eri, Misako Nakaba, Yasutaka Shigemura, Michio Yamada, and Kenji Sato. "Fish-elastin Hydrolysate: Development and Impact on the Skin and Blood Vessels." In Marine Proteins and Peptides, 467–86. Chichester, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118375082.ch23.
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Foltz, Martin, Mylene Portier, and Daniel Tomé. "Food Proteins or Their Hydrolysates as Regulators of Satiety." In Bioactive Proteins and Peptides as Functional Foods and Nutraceuticals, 135–48. Oxford, UK: Wiley-Blackwell, 2010. http://dx.doi.org/10.1002/9780813811048.ch10.
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Saiga, Ai, and Toshihide Nishimura. "Antioxidative Peptides in Porcine Myofibrillar Protein Hydrolysates by Protease Treatment." In ACS Symposium Series, 289–96. Washington, DC: American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0851.ch025.
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Anal, Anil Kumar, Athapol Noomhorm, and Punchira Vongsawasdi. "Protein Hydrolysates and Bioactive Peptides from Seafood and Crustacean Waste: Their Extraction, Bioactive Properties and Industrial Perspectives." In Marine Proteins and Peptides, 709–35. Chichester, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118375082.ch36.
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Maehashi, K., and S. Arai. "Taste Evaluation for Peptides in Protein Hydrolysates from Soybean and Other Plants." In Analysis of Taste and Aroma, 47–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-662-04857-3_4.
Full textConference papers on the topic "Peptide hydrolysates"
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Baba, Waqas, and Sajid Maqsood. "Novel antihypertensive and anticholesterolemic peptides from peptic hydrolysates of camel whey proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qecs2081.
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Hypercholesterolemia and hypertension are major growing concerns that are managed by drugs that inhibit various metabolic enzymes. Milk hydrolysates have been reported to contain various bioactive peptides (BAP) that can inhibit various metabolic enzymes for enhancing human health. As such camel whey proteins were subjected to peptic hydrolysis using a full factorial model (33) with hydrolysis time, temperature, and enzyme concentration as factors. The resulting hydrolysates were analyzed for anti-hypercholesterolemic and hypertensive properties by studying the in vitro inhibition of various enzymatic markers. The hydrolysates with lowest IC50 values were further subjected to LC-MS-QTOF that revealed presence of 185 peptides. Selected peptides that had Peptide Ranker Score greater than 0.8 were further studied for prediction of possible interactions with enzyme markers: pancreatic lipase (PL) cholesterol esterase (CE) and angiotensin converting enzyme (ACE) using in silico analysis. The data generated suggested that most of the peptides could bind active site of PL while as only three peptides could bind active site of CE. Based on higher number of reactive residues in the bioactive peptides (BAP) and greater number of substrate binding sites, FCCLGPVPP was identified as potential CE inhibitory peptide while PAGNFLPPVAAAPVM, MLPLMLPFTMGY, and LRFPL were identified as PL inhibitors. While peptides PAGNFLP, FCCLGPVPP, PAGNFLMNGLMHR, PAVACCLPPLPCHM were identified as potential ACE inhibitors. Molecular docking of selected peptides showed hydrophilic and hydrophobic interactions between peptides and target enzymes. Moreover, due to the importance of renin in managing hypertension, peptides from hydrolysates with high ACE inhibiting potential were predicted for potential to interact with renin using in silico analysis. Molecular docking was subsequently employed to identify how the identified peptides, PVAAAPVM and LRPFL, could interact with renin and potentially inhibit it. Thus, non-bovine (camel) whey hydrolysates might be used as functional ingredients for production of functional foods with antihypertensive and anticholesterolemic properties.
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Bjørlie, Mads, Rachel Irankunda, Jean-Michel Girardet, Sandrine Boschi-Müller, Betül Yesiltas, Charlotte Jacobsen, and Laetitia Canabady-Rochelle. "Screening of Metal-chelating Peptides and Hydrolysates Using Surface Plasmon Resonance and Switchsense." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zszk2778.
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Abstract: Lipid oxidation is, among other factors, catalyzed by the presence of metal ions and efficient metal chelators are therefore highly sought after in the food industry. Among these, natural metal chelators are gaining interest as opposed to their synthetic counterparts such as EDTA. Traditional screening for metal chelation capacity is time consuming and non-specific. The aim of this study was to screen potato protein hydrolysate and synthetic peptides derived from potato protein sequences for their metal-chelating capacity. Seven peptides and two hydrolysates (raw and ultra-filtrated) were studied. Peptides were selected using two different models: an empirical-based bioinformatics approach (AnOxPePred) and a theoretically based model for metal chelation. Surface Plasmon Resonance (SPR) is a label-free, optical technique used to determine the dissociation constant (KD) of a complex formed between immobilized Ni2+ and peptides. The SwitchSENSE technology is another approach used to study Ni2+/peptide affinity. It utilizes the quenching of fluorescence of a fluorophore upon Ni2+ immobilization and the inverse fluorescence increase upon peptide binding onto Ni2+. Both analyses were carried out at pH 7.4. In this study, we successfully determined the dissociation constants (KD) of two peptides (ASH and DHGPKIFEPS) using SPR. These values compare favourably with previous results indicating metal chelating potential. The association rate constant (kon) of all peptides were determined using switchSENSE. Yet, due to bad fitting of the kinetics data obtained with switchSENSE, the KDs of the hydrolysates were only determined with low accuracy.
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Kumrungsee, Thanutchaporn, Norihisa Kato, Toshiro Matsui, and Yongshou Yang. "Plant and gut microbiota-derived protein metabolites and potential health functions." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/envt3719.
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Bioactive peptides can be obtained from protein hydrolysates through in vitro enzymatic hydrolysis, gastrointestinal digestion, and microbial fermentation. Recent emerging research suggests that prebiotic-stimulated gut microbiota also plays a role in generating bioactive peptides and amino acids in gut. In this study, we examined if enzymatic hydrolysis of soybean and wheat germ, plant materials often used in oil industry, can generate antihypertensive peptides and determined if prebiotic digestive enzymes can induce the production of gut microbiota-derived amino acids. In the first experiment, soybean and wheat germ were hydrolyzed by protease enzymes. Then, their hydrolysates were subjected to peptide isolation and identification. Identified peptides were subjected to test for their potential antihypertensive activities. For the second experiment, rodents were fed an Aspergillus-derived protease- or lipase-mixed diet for 2 weeks. Then, cecum contents were collected for bacteria and metabolite analyses. As a result, we found that His-Gly-Lys from soybean hydrolysate strongly inhibited angiotensin II-induced elevated intracellular Ca2+ concentration in vascular smooth muscle cells (VSMCs). Trp-Val and Trp-Ile from wheat germ hydrolysate were found to inhibit Ca2+-calmodulin (CaM)-dependent protein kinase II (CaMK II), a protein kinase promoting hypertension by inducing Ca2+ influx into VSMCs, in rat thoracic aorta rings. These findings suggest the potential of the plant-derived peptides in preventing hypertension and vascular-related diseases. In the second experiment, we found that the dietary protease and lipase increased Bifidobacterium and Lactobacillus probiotics and induced the production of probiotic-derived amino acids, taurine, ornithine, and γ-aminobutyric acid. Since these amino acids have versatile functions including in gut health modulation and brain functions, it can be hypothesized that the dietary prebiotic-digestive enzymes may be beneficial for gut health and brain functions. This study suggests the possibility of applying oil processing by-products in the production of functional food ingredients including bioactive peptides and amino acids.
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Lammi, Carmen. "From the bench to the bedside: the history of lupin bioactive peptides as useful ingredient for the prevention of metabolic syndrome." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/bwgm4089.
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Proteins derived from lupin seeds are gaining attention as a source of bioactive peptides. In fact, several pieces of evidence highlight the biological activities of lupin protein hydrolysates and peptides, including hypocholesterolemic, hypoglycemic, antimicrobial, anti-inflammatory, and immunomodulatory effects. The health-promoting activities of lupin peptides have been tested in different animal models and clinical trials. Briefly, diets containing protein from L. albus or L. angustifolius significantly reduce both total cholesterol and low-density lipoprotein (LDL) cholesterol (LDL-C) levels versus control diets containing casein in a rat or hamster models of hypercholesterolemia. An uncontrolled clinical trial on L. albus and two controlled ones on L. angustifolius have confirmed the hypocholesterolemic activity in humans. In light with these evidences and with a more updated perception of the phenomenon, our study suggests that the observed health-promoting activity does not lie in the native protein, but the mixture of peptides generated from the physiological hydrolysis of proteins during digestion. Indeed, many efforts have been pursued in order to characterize the molecular mechanism through which lupin hydrolysates, obtained different hydrolytic enzymes, exert hypocholesterolemic and anti-diabetic effects in vitro and in vivo. In this context, specific peptides responsible of the biological activity exerted by the peptide mixture were also identified and fully characterized from chemical and biological point of view. Doubtless, our results highlight that lupin hydrolysates may be exploited as new ingredients for the development of dietary supplements or functional foods
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Reinoso, Zain Sanchez, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet, and Sergey Mikhaylin. "Bioactive Peptide Production from Slaughterhouse Blood Proteins: Impact of Pulsed Electric Fields and Ph on Enzyme Inactivation, Antimicrobial and Antioxidant Activities of Peptic Hydrolysates from Bovine and Porcine Hemoglobins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsht2150.
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Slaughterhouse blood is a valuable by-product since multiple bioactive compounds can be derived out of it. Its solid fraction consists mainly of hemoglobin, which is a good source of antimicrobial and antioxidant peptides that can be released by peptic hydrolysis. Nevertheless, this method has limitations such as low yield, expensive cost of enzyme process, and non-eco-friendly production (high energy consumption and chemical reagents requested). Amount the alternative green technologies for protein valorization, pulsed electric field (PEF) stands out since it allows modifying the physicochemical properties of proteins, promoting the enzymatic hydrolysis, enzyme inactivation, and bioactivity enhancement. Thus, this study aimed to evaluate the effect of PEF on the pepsin inactivation and biological activities (antimicrobial and antioxidant) in hemoglobin hydrolysates. Bovine and porcine hemoglobins were hydrolyzed with pepsin for 3 h (37°C, pH 3.0) and treated with PEF (73 pulses, 23.8kV/cm, 90Hz) to inactivate the enzyme. The hydrolysis degree was evaluated, which did not show significant changes after PEF-inactivation of pepsin, whereas the peptide population analysis by RP-UPLC-MS/MS showed some changes in PEF-treated hydrolysates over time, which suggested a residual pepsin activity. Additionally, the impact of pH (3, 7, and 10) on bioactivity was studied. PEF-treatments did not show a significant impact on antimicrobial (antibacterial, antifungal, and anti-yeast activities) and antioxidant activities (DPPH and ORAC). However, higher pH fostered stronger anti-yeast activity (R. mucilaginosa) and DPPH‐scavenging capacity, whereas pH 7 fostered the antifungal activity (M. racemosus). Even though some changes were observed in the peptide population, no negative effects of PEF were found for biological activities. Thus, the utilization of hemoglobin from the meat industry combined with PEF-treatment fits the circular economy concept since derived peptides can be recycled to protect meat and other products against microbial growth and oxidation.
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Novogrodskii, A. S., I. A. Khadyko, O. Iu Khoroshev, and K. Iu Terentev. "Primary analysis of peptide profiles of whey protein hydrolysates cow milk." In ТЕНДЕНЦИИ РАЗВИТИЯ НАУКИ И ОБРАЗОВАНИЯ. НИЦ «Л-Журнал», 2018. http://dx.doi.org/10.18411/lj-12-2018-183.
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Hamin-Neto, Y. A. A., and H. Cabral. "Angiotensin I-Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Whey Milk, Casein and Egg Albumin by Microbial Enzymes and a Commercial Enzyme." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.054.
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Abioye, Raliat, Caleb Acquah, Chibuike Udenigwe, Nico Huttmann, and Pei Chun Queenie Hsu. "Self-assembly and hydrogelation properties of egg white-derived peptides." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/jzku2300.
Full textAbstract:
Functional foods are gaining traction as a source of peptides possessing hydrogelation properties. Analysis of peptides (n=429) in egg white protein hydrolysates resulted in the identification of six peptides: IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, YCPIAIMSA, MMYQIGLF, and VYSFSLASRL as prominent self-assembly candidates based on prediction of their aggregation-prone segments. The objective of this study was to characterize the hydrogel formed via self-assembly of the peptides. Of the six peptides studied, NIFYCPIAIM and MMYQIGLF showed promising self-assembly and hydrogelation properties. Thioflavin T kinetics indicated that NIFYCPIAIM possesses the strongest self-assembly property, confirmed by dynamic light scattering which indicated the largest average particle diameter was achieved after 24 hours. Rheological characterization indicated that all six peptides possessed viscoelastic pseudoplastic properties and some were able to regain some level of viscosity following the exertion of shear stress. Finally, transmission electron microscopy of the six peptides showed the development of fibrillar structures of varying morphologies after 24 hours. The remarkable difference in self-assembly and hydrogelation properties of NIFYCPIAIM, IFYCPIAIMSA and YCPIAIMSA, which share a common sequence YCPIAIM, indicate the importance of amino acid sequence in the formation and property of peptide hydrogels. Identification of the egg white-derived peptides with hydrogelation properties shows a promising future for the use of functional foods in applications of drug delivery systems and tissue engineering, in the food, pharmaceutical, cosmetics, and biomedical sectors.
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Jacobsen, Charlotte, Ann-Dorit Moltke Sorensen, and Dimitra Marinou. "Enzymatic production of antioxidative and antimicrobial hydrolysates from cod solid side-streams." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qmqf3129.
Full textAbstract:
In the last decade, there has been an increased focus and interest in increasing the utilization of existing raw materials and reducing waste especially due to the increasing global population. In the cod filleting industry up to 60% (w/w) of the biomass end up as side-streams e.g., frame, head and gut, which are either used as low value products such as animal feed or are wasted. An example of animal feed is mink feed. However, in Denmark the mink production is closed due to COVID-19 and new utilization possibilities are needed. The cod side-stream used in this study is from Royal Greenland and is very fresh with the possibility of freezing right after production to maintain quality and increase shelf life before further production. Cod frames still contain meat after filleting and could be used as hydrolysates with bioactive properties such as antioxidative and/or antimicrobial activity for food or feed applications. Previous studies have shown that longer peptides (shorter hydrolysis time) potentially have antimicrobial properties and shorter peptides (longer hydrolysis time) have antioxidative properties. Therefore, an experiment was designed using three different types of proteases (Alcalase, Neutrase and Protamex) and different hydrolysis time (½h, 1, 2, 3 and 6h) to produce different hydrolysates. Produced hydrolysates were evaluated for their antioxidative and antimicrobial activities by in vitro antioxidant assay, radical scavenging (DPPH) and metal chelating activity, and by disc diffusion and minimal inhibitory concentration (MIC) assays, respectively. Furthermore, the hydrolysates were also characterized with respect to yield, protein content and degree of hydrolysis. The produced hydrolysates showed antioxidant properties. Highest DPPH activity was obtained with Protamex, where-as highest metal chelating activity surprisingly was obtained for a control (no enzyme added). Unfortunately, no antimicro-bial activity was detected for the produced hydrolysates independent of enzymes and hydrolysis time applied. BBI JU-funded WASEABI project.
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Hatakenaka, Toshiya, Tamaki Kato, and Kouji Okamoto. "Novel Oligopeptides with angiotensin I-converting enzyme inhibitory activity found in an elastase-treated hydrolysate of porcine aortic elastin." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.251.
Full textReports on the topic "Peptide hydrolysates"
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Wong, Eric A., and Zehava Uni. Nutrition of the Developing Chick Embryo: Nutrient Uptake Systems of the Yolk Sac Membrane and Embryonic Intestine. United States Department of Agriculture, June 2012. http://dx.doi.org/10.32747/2012.7697119.bard.
Full textAbstract:
We have examined the developmental changes in composition, amount, and uptake of yolk nutrients (fat, protein, water and carbohydrates) and the expression ofnutrient transporters in the yolk sac membrane (YSM) from embryonic day 11 (Ell) to 21 (E21) and small intestine from embryonic day 15 (E15) to E21 in embryos from young (22-25 wk) and old (45-50 wk) Cobb and Leghorn breeder flocks. The developmental expression profiles for the peptide transporter 1 (PepTl), the amino acid transporters, EAAT3, CAT-1 and BOAT, the sodium glucose transporter (SGLTl), the fructose transporter (GLUT5), the digestive enzymes aminopeptidase N (APN) and sucraseisomaltase (SI) were assayed by the absolute quantification real time PCR method in the YSM and embryonic intestine. Different temporal patterns of expression were observed for these genes. The effect of in ovo injection of peptides (the dipeptide Gly-Sar, purified peptides, trypsin hydrolysate) on transporter gene expression has been examined in the embryonic intestine. Injection of a partial protein hydrolysate resulted in an increase in expression of the peptide transporter PepT2. We have initiated a transcriptome analysis of genes expressed in the YSM at different developmental ages to better understand the function of the YSM.
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Abeyrathne, Sandun, Hyun yong Lee, and Dong Uk Uk Ahn. Enzymatic Hydrolysis of Ovomucin and the Functional and Structural Characteristics of Peptides in the Hydrolysates. Ames (Iowa): Iowa State University, January 2017. http://dx.doi.org/10.31274/ans_air-180814-374.
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