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Autore: Grafiati

Pubblicato: 8 giugno 2024

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1

Ratnayani, Ketut, Indriani Wisnu Susanto Panjaitan e Ni Made Puspawati. "SCREENING POTENTIAL ANTIOXIDANT AND ANTIBACTERIAL ACTIVITIES OF PROTEIN HYDROLYSATES DERIVED FROM GERMINATED LABLAB BEAN, PIGEON PEA AND KIDNEY BEAN". Journal of Health Sciences and Medicine 1, n. 1 (1 febbraio 2017): 24. http://dx.doi.org/10.24843/jhsm.2017.v01.i01.p07.

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Abstract Protein hydrolysate contains a mixture of various lengths of short peptides chain and free amino acids that may excert biological activities. This research aims to screen potential antioxidant and antibacterial activities of protein hydrolysate produced from three kinds of germinated beans i.e. lablab bean (Lablab purpureus), pigeon pea (Cajanus cajan (L.) Millsp) and kidney bean (Phaseolus vulgaris) through enzymatic hydrolysis process. The steps of research included germination process of the beans prior to total protein isolation, enzymatic hydrolysis of total protein isolates using pancreatin enzyme, evaluation of in vitro antioxidant activity of the hydrolysates protein using DPPH (1,1-diphenyl-2-picryl hydrazyl) method, and antibaterial activity testing towards Eschericia coli and Staphyllococcus aureus bacteria. The results revealed that pancreatine enzyme was able to hydrolyse germinated protein of lablab bean, pigeon pea and kidney bean at the experiment condition applied with degree of hydrolysis 34.12%, 27.44%, and 30,93% respectively. It was also found that protein hydrolysates of lablab bean, pigeon pea, and kidney bean demonstrated antioxidant activity which percentage radical DPPH scavenging activity of 84.02%, 68.97% and 67.89 %. On the other hand, all of those protein hydrolysates did not show any antibacterial activity towards Eschericia coli and Staphyllococcus aureus bacteria.

2

Ruiz, Raquel, Raquel Olías, Alfonso Clemente e Luis A. Rubio. "A Pea (Pisum sativum L.) Seed Vicilins Hydrolysate Exhibits PPARγ Ligand Activity and Modulates Adipocyte Differentiation in a 3T3-L1 Cell Culture Model". Foods 9, n. 6 (16 giugno 2020): 793. http://dx.doi.org/10.3390/foods9060793.

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Legume consumption has been reported to induce beneficial effects on obesity-associated metabolic disorders, but the underlying mechanisms have not been fully clarified. In the current work, pea (Pisum sativum L.) seed meal proteins (albumins, legumins and vicilins) were isolated, submitted to a simulated gastrointestinal digestion, and the effects of their hydrolysates (pea albumins hydrolysates (PAH), pea legumins hydrolysates (PLH) and pea vicilin hydrolysates (PVH), respectively) on 3T3-L1 murine pre-adipocytes were investigated. The pea vicilin hydrolysate (PVH), but not native pea vicilins, increased lipid accumulation during adipocyte differentiation. PVH also increased the mRNA expression levels of the adipocyte fatty acid-binding protein (aP2) and decreased that of pre-adipocyte factor-1 (Pref-1) (a pre-adipocyte marker gene), suggesting that PVH promotes adipocyte differentiation. Moreover, PVH induced adiponectin and insulin-responsive glucose transporter 4 (GLUT4) and stimulated glucose uptake. The expression levels of peroxisome proliferator-activated receptor γ (PPARγ), a key regulator of adipocyte differentiation, were up-regulated in 3T3-L1 cells treated with PVH during adipocyte differentiation. Finally, PVH exhibited PPARγ ligand activity. Lactalbumin or other pea hydrolysates (PAH, PLH) did not exhibit such effects. These findings show that PVH stimulates adipocyte differentiation via, at least in part, the up-regulation of PPARγ expression levels and ligand activity. These effects of PVH might be relevant in the context of the beneficial health effects of legume consumption in obesity-associated metabolic disorders.

3

Awosika, Temitola, e Rotimi E. Aluko. "Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors". Foods 8, n. 6 (10 giugno 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.

4

Siriporn, B., P. Thongkorn, S. Waraporn, S. Wiriyaporn, S. Sinee, A. Chiramet e E. A. Rotimi. "Antioxidant polypeptides derived from pigeon pea (Cajanus cajan (L) Mill sp.) by enzymatic hydrolysis". Food Research 8, Supplementary 2 (26 aprile 2024): 182–89. http://dx.doi.org/10.26656/fr.2017.8(s2).146.

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Pigeon pea (Cajanus cajan (L) Mill sp.) seeds are rich sources of protein in the legume family and their consumption has been associated with the prevention of noncommunicated diseases, which is attributable to their content of bioactive components. Antioxidant protein hydrolysates were produced from pigeon pea protein isolate (PPI) by enzymatic hydrolysis using pancreatin and flavourzyme. The hydrolysates were analyzed for their physicochemical, molecular weight, amino acid composition, and in vitro antioxidant activities. The molecular weights of polypeptides in the hydrolysates were 8, 20, 25 and 48 kDa, which were determined after pancreatin or flavourzyme hydrolysis of the protein isolate for 4 h. Pancreatin-hydrolyzed pigeon pea protein (PPHP) contained high hydrophobic amino acids, especially isoleucine, leucine and valine, which were related to the high content of aromatic amino acids. The hydrolysates obtained from flavourzyme hydrolysis of pigeon pea proteins (PPHF) presented significantly higher capacities to scavenge ABTS˙+ and reduce Fe3 + better than that of PPI, while the PPI exhibited strong DPPH scavenging (98.4 mg trolox equivalent antioxidant capacity). The results indicated that the partial hydrolysis for PPI provided medium to high molecular weight of peptides. Therefore, PPHF could be a promising source of bioactive peptides and a potential ingredient for the formulation of functional foods against oxidative stress

5

Hidayat, Meilinah, Sijani Prahastuti, TeresaLiliana Wargasetia, Vincentius Ferdinand, Roro Wahyudianingsih, AndreanusAndaja Soemardji, SitiFarah Rahmawati, Nova Suliska e Khomaini Hasan. "Role of pea protein hydrolysates as antinephrotoxicity". Journal of Reports in Pharmaceutical Sciences 8, n. 1 (2019): 55. http://dx.doi.org/10.4103/jrptps.jrptps_14_17.

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6

Soral-Śmietana, M., A. Świgoń, R. Amarowicz e L. Sijtsma. "The solubility of trypsin pea protein hydrolysates". Nahrung / Food 42, n. 03-04 (agosto 1998): 217–18. http://dx.doi.org/10.1002/(sici)1521-3803(199808)42:03/04<217::aid-food217>3.3.co;2-u.

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7

Krasnoshtanova, Alla Al'bertovna, e Leonid Viktorovich Shul'ts. "PREPARATION AND EVALUATION OF THE FUNCTIONAL PROPERTIES OF PROTEIN ISOLATES AND HY-DROLYSATES FROM PLANT RAW MATERIALS". chemistry of plant raw material, n. 4 (15 dicembre 2022): 299–309. http://dx.doi.org/10.14258/jcprm.20220410952.

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Animal protein plays a key role in the human diet as the most balanced amino acid composition; however, its consumption often causes allergic reactions. Plant protein serves as a substitute for animal protein. The most promising sources of plant protein are the seeds of cereals, pulses, oilseeds and cereals. Research aim: selection of conditions for obtaining protein isolates and enzymatic hydrolysates having the desired functional properties from different types of vegetable raw materials.Pea, corn and oat flour LLC "FavoritT"; linseed flour LLC NGO "Compass Health". Enzyme preparations: chymotrypsin LLC "Samson-Med"; Protex 40E Genencor; protosubtilin G3x produced by PO "Sibbiofarm" LLC; pancreatin PJSC "Biosintez"; trypsin LLC "Diaem"; beef pepsin OJSC "MHSF". Crude protein content was determined by Kjeldahl method, protein substances - by modified Lowry method. Fat-holding, water-holding, emulsifying and foaming capacities, as well as allergenicity of protein isolates and hydrolysates were determined. Conditions for protein substances extraction from flax, corn, oat and pea flour with the yield of high-molecular protein fraction not less than 70 % of raw protein content were selected. The conditions of protein isolates precipitation to produce preparations containing not less than 85% of protein have been selected. The type of enzyme preparation for hydrolysis - pancreatin - was selected. It was found that in order to increase water- and fat-holding capacity of pea isolate, hydrolysis is possible with duration not exceeding 15 min, for all other isolates hydrolysis is undesirable. The best emulsifying and foam-forming capacities are possessed by linseed hydrolysates after 60 and 90 min of hydrolysis, respectively. Enzymatic hydrolysis was shown to reduce the allergenicity of plant proteins. The obtained hydrolysates of vegetable proteins can be used as ingredients for functional products, as well as for obtaining products with reduced allergenicity.

8

Stanisavljevic, Nemanja, Goran Vukotic, Ferenc Pastor, Desanka Suznjevic, Zivko Jovanovic, Ivana Strahinic, Djordje Fira e Svetlana Radovic. "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria". Archives of Biological Sciences 67, n. 3 (2015): 1033–42. http://dx.doi.org/10.2298/abs150130066s.

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Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW <10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.

9

Moreno, Cecilia, Luis Mojica, Elvira González de Mejía, Rosa María Camacho Ruiz e Diego A. Luna-Vital. "Combinations of Legume Protein Hydrolysates Synergistically Inhibit Biological Markers Associated with Adipogenesis". Foods 9, n. 11 (17 novembre 2020): 1678. http://dx.doi.org/10.3390/foods9111678.

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The objective was to investigate the anti-adipogenesis potential of selected legume protein hydrolysates (LPH) and combinations using biochemical assays and in silico predictions. Black bean, green pea, chickpea, lentil and fava bean protein isolates were hydrolyzed using alcalase (A) or pepsin/pancreatin (PP). The degree of hydrolysis ranged from 15.5% to 35.5% for A-LPH and PP-LPH, respectively. Antioxidant capacities ranged for ABTS•+ IC50 from 0.3 to 0.9 Trolox equivalents (TE) mg/mL, DPPH• IC50 from 0.7 to 13.5 TE mg/mL and nitric oxide (NO) inhibition IC50 from 0.3 to 1.3 mg/mL. LPH from PP–green pea, A–green pea and A–black bean inhibited pancreatic lipase (PL) (IC50 = 0.9 mg/mL, 2.2 mg/mL and 1.2 mg/mL, respectively) (p < 0.05). For HMG-CoA reductase (HMGR) inhibition, the LPH from A–chickpea (0.15 mg/mL), PP–lentil (1.2 mg/mL), A–green pea (1.4 mg/mL) and PP–green pea (1.5 mg/mL) were potent inhibitors. Combinations of PP–green pea + A–black bean (IC50 = 0.4 mg/mL), A–green pea + PP–green pea (IC50 = 0.9 mg/mL) and A–black bean + A–green pea (IC50 = 0.6 mg/mL) presented synergistic effects to inhibit PL. A–chickpea + PP–lentil (IC50 = 0.8 mg/mL) and PP–lentil + A–green pea (IC50 = 1.3 mg/mL) interacted additively to inhibit HMGR and synergistically in the combination of A–chickpea + PP–black bean (IC50 = 1.3 mg/mL) to block HMGR. Peptides FEDGLV and PYGVPVGVR inhibited PL and HMGR in silico, showing predicted binding energy interactions of −7.6 and −8.8 kcal/mol, respectively. Combinations of LPH from different legume protein sources could increase synergistically their anti-adipogenic potential.

10

Humiski, L. M., e R. E. Aluko. "Physicochemical and Bitterness Properties of Enzymatic Pea Protein Hydrolysates". Journal of Food Science 72, n. 8 (ottobre 2007): S605—S611. http://dx.doi.org/10.1111/j.1750-3841.2007.00475.x.

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11

Bollati, Carlotta, Ruoxian Xu, Giovanna Boschin, Martina Bartolomei, Fabrizio Rivardo, Jianqiang Li, Anna Arnoldi e Carmen Lammi. "Integrated Evaluation of the Multifunctional DPP-IV and ACE Inhibitory Effect of Soybean and Pea Protein Hydrolysates". Nutrients 14, n. 12 (8 giugno 2022): 2379. http://dx.doi.org/10.3390/nu14122379.

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Nowadays, notwithstanding their nutritional and technological properties, food bioactive peptides from plant sources garner increasing attention for their ability to impart more than one beneficial effect on human health. Legumes, which stand out thanks to their high protein content, represent valuable sources of bioactive peptides. In this context, this study focused on the characterization of the potential pleotropic activity of two commercially available soybean (SH) and pea (PH) protein hydrolysates, respectively. Since the biological activity of a specific protein hydrolysate is strictly correlated with its chemical composition, the first aim of the study was to identify the compositions of the SH and PH peptides. Peptidomic analysis revealed that most of the identified peptides within both mixtures belong to storage proteins. Interestingly, according to the BIOPEP-UWM database, all the peptides contain more than one active motive with known inhibitory angiotensin converting enzyme (ACE) and dipeptidyl-dipeptidases (DPP)-IV sequences. Indeed, the results indicated that both SH and PH inhibit DPP-IV and ACE activity with a dose-response trend and IC50 values equal to 1.15 ± 0.004 and 1.33 ± 0.004 mg/mL, and 0.33 ± 0.01 and 0.61 ± 0.05 mg/mL, respectively. In addition, both hydrolysates reduced the activity of DPP-IV and ACE enzymes which are expressed on the surface of human intestinal Caco-2 cells. These findings clearly support that notion that SH and PH may represent new ingredients with anti-diabetic and hypotensive effects for the development of innovative multifunctional foods and/or nutraceuticals for the prevention of metabolic syndrome.

12

Lim, Woo Su, Hyun Woo Kim, Min Hyeock Lee e Hyun Jin Park. "Improved printability of pea protein hydrolysates for protein-enriched 3D printed foods". Journal of Food Engineering 350 (agosto 2023): 111502. http://dx.doi.org/10.1016/j.jfoodeng.2023.111502.

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13

Frączek, R., E. Kostyra, H. Kostyra e S. Krawczuk. "Immunoreactive properties of pea protein extract and its trypsin hydrolysates". Journal of Animal and Feed Sciences 16, n. 3 (6 settembre 2007): 472–84. http://dx.doi.org/10.22358/jafs/66803/2007.

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14

Marinova, Margarita D., e Bozhidar P. Tchorbanov. "Preparation of Antioxidant Enzymatic Hydrolysates from Honeybee-Collected Pollen Using Plant Enzymes". Enzyme Research 2010 (9 gennaio 2010): 1–5. http://dx.doi.org/10.4061/2010/415949.

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Enzymatic hydrolysates of honeybee-collected pollen were prepared using food-grade proteinase and aminopeptidases entirely of plant origin. Bromelain from pineapple stem was applied (8 mAU/g substrate) in the first hydrolysis stage. Aminopeptidase (0.05 U/g substrate) and proline iminopeptidase (0.03 U/g substrate) from cabbage leaves (Brassica oleracea var. capitata), and aminopeptidase (0.2 U/g substrate) from chick-pea cotyledons (Cicer arietinum L.) were involved in the additional hydrolysis of the peptide mixtures. The degree of hydrolysis (DH), total phenolic contents, and protein contents of these hydrolysates were as follows: DH (about 20–28%), total phenolics (15.3–27.2 μg/mg sample powder), and proteins (162.7–242.8 μg/mg sample powder), respectively. The hydrolysates possessed high antiradical scavenging activity determined with DPPH (42–46% inhibition). The prepared hydrolysates of bee-collected flower pollen may be regarded as effective natural and functional dietary food supplements due to their remarkable content of polyphenol substances and significant radical-scavenging capacity with special regard to their nutritional-physiological implications.

15

Barac, Miroljub, Slavica Cabrilo, Sladjana Stanojevic, Mirjana Pesic, Milica Pavlicevic, Branislav Zlatkovic e Miodrag Jankovic. "Functional properties of protein hydrolysates from pea (Pisum sativum,L) seeds". International Journal of Food Science & Technology 47, n. 7 (3 maggio 2012): 1457–67. http://dx.doi.org/10.1111/j.1365-2621.2012.02993.x.

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16

Zhao, Dan, e Xiaolan Liu. "Purification, Identification and Evaluation of Antioxidant Peptides from Pea Protein Hydrolysates". Molecules 28, n. 7 (25 marzo 2023): 2952. http://dx.doi.org/10.3390/molecules28072952.

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Food-derived antioxidant peptides can be explored as natural antioxidants due to their potential health benefits. In this study, antioxidant peptides were isolated and purified from pea protein hydrolysates (PPH). The DPPH and ABTS radical scavenging activities were used as indexes to purify the antioxidant peptides by a series of purification steps including ultrafiltration, ion exchange chromatography, G25 gel filtration chromatography, and reversed-phase chromatography. Three novel antioxidant peptides YLVN, EEHLCFR and TFY were identified, which all exhibited strong antioxidant activity in vitro. EEHLCFR showed stronger DPPH scavenging activity with an IC50 value of 0.027 mg/mL. YLVN showed stronger ABTS scavenging activity with an IC50 value of 0.002 mg/mL and higher ORAC values of 1.120 ± 0.231 μmol TE/μmol, which is even better than that of GSH. Three novel antioxidant peptides significantly elevated LO2 cells viability even at the concentration of 0.025 mg/mL, and cell viability enhanced to 53.42 ± 1.19%, 55.78 ± 1.03%, and 51.09 ± 1.06% respectively, compared to that of H2O2 injury group (48.35 ± 0.96%), and prevented the accumulation of ROS by enhancing the activities of antioxidant enzymes in H2O2-induced oxidative stress LO2 cells. The molecular docking results showed that the potential molecular mechanism of the three novel antioxidant peptides may be in high correlation with the activation of the Keap1-Nrf2 pathway by occupying the Keap1-Nrf2 binding site. These results demonstrate that the three novel antioxidant peptides are potential natural antioxidants that can be devoted to medicine or functional food ingredients.

17

Köstekli Büyükcan, Mine, e Sibel Karakaya. "Comparison of some functional properties and protein profiles of different protein sources with egg components". Italian Journal of Food Science 33, n. 2 (31 luglio 2021): 142–55. http://dx.doi.org/10.15586/ijfs.v33i2.2055.

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Emulsifying and foaming properties of plant and animal-sourced proteins; wheat protein hydrolysates (WP1, WP2, and WP3), potato protein isolates (PP1, PP2), pea proteins isolates (PeP1, PeP2), whey protein concentrate (WPC), and buttermilk powder (BMP) were compared with the egg white powder (EWP) and egg yolk powder (EYP). Foaming capacity, stability, emulsion activity, stability, heat stability, morphology, and electrophoretic protein profiles were determined. The proteins representing competitive emulsifying functions were PeP1, WPC, and BMP. Heat treatment for 30 min at 80°C remarkably reduced the emulsion activity (EA) of EYP. Our findings demonstrated that patatin-rich potato protein (PP1), an allergen-free and vegan option, has great potential to replace the foaming function of the egg white. The relationship between the protein profiles of the samples and their functional properties was further discussed in detail.

18

Rizzello, Carlo Giuseppe, Anna Lavecchia, Valerio Gramaglia e Marco Gobbetti. "Long-Term Fungal Inhibition by Pisum sativum Flour Hydrolysate during Storage of Wheat Flour Bread". Applied and Environmental Microbiology 81, n. 12 (10 aprile 2015): 4195–206. http://dx.doi.org/10.1128/aem.04088-14.

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ABSTRACTIn order to identify antifungal compounds from natural sources to be used as ingredients in the bakery industry, water/salt-soluble extracts (WSE) from different legume flour hydrolysates obtained by the use of a fungal protease were assayed againstPenicillium roquefortiDPPMAF1. The agar diffusion assays allowed the selection of the pea (Pisum sativum) hydrolysate as the most active. As shown by the hyphal radial growth rate, the WSE had inhibitory activity towards several fungi isolated from bakeries. The MIC of the WSE was 9.0 mg/ml. Fungal inhibition was slightly affected by heating and variations in pH. The antifungal activity was attributed to three native proteins (pea defensins 1 and 2 and a nonspecific lipid transfer protein [nsLTP]) and a mixture of peptides released during hydrolysis. The three proteins have been reported previously as components of the defense system of the plant. Five peptides were purified from WSE and were identified as sequences encrypted in leginsulin A, vicilin, provicilin, and the nsLTP. To confirm antifungal activity, the peptides were chemically synthesized and tested. Freeze-dried WSE were used as ingredients in leavened baked goods. In particular, breads made by the addition of 1.6% (wt/wt) of the extract and fermented by baker's yeast or sourdough were characterized for their main chemical, structural, and sensory features, packed in polyethylene bags, stored at room temperature, and compared to controls prepared without pea hydrolysate. Artificially inoculated slices of a bread containing the WSE did not show contamination by fungi until at least 21 days of storage and behaved like the bread prepared with calcium propionate (0.3%, wt/wt).

19

Li, Huan, e >Rotimi E. Aluko. "Structural modulation of calmodulin and calmodulin-dependent protein kinase II by pea protein hydrolysates". International Journal of Food Sciences and Nutrition 57, n. 3-4 (gennaio 2006): 178–89. http://dx.doi.org/10.1080/09637480600659144.

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20

Barbana, Chockry, e Joyce Irene Boye. "Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates". Food Research International 43, n. 6 (luglio 2010): 1642–49. http://dx.doi.org/10.1016/j.foodres.2010.05.003.

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21

Tamm, F., S. Herbst, A. Brodkorb e S. Drusch. "Functional properties of pea protein hydrolysates in emulsions and spray-dried microcapsules". Food Hydrocolloids 58 (luglio 2016): 204–14. http://dx.doi.org/10.1016/j.foodhyd.2016.02.032.

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22

Girgih, Abraham T., Dongfang Chao, Lin Lin, Rong He, Stephanie Jung e Rotimi E. Aluko. "Enzymatic protein hydrolysates from high pressure-pretreated isolated pea proteins have better antioxidant properties than similar hydrolysates produced from heat pretreatment". Food Chemistry 188 (dicembre 2015): 510–16. http://dx.doi.org/10.1016/j.foodchem.2015.05.024.

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23

Zhou, Xue, Heping Cui, Qiang Zhang, Khizar Hayat, Jingyang Yu, Shahzad Hussain, Muhammad Usman Tahir, Xiaoming Zhang e Chi-Tang Ho. "Taste improvement of Maillard reaction intermediates derived from enzymatic hydrolysates of pea protein". Food Research International 140 (febbraio 2021): 109985. http://dx.doi.org/10.1016/j.foodres.2020.109985.

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Aluko, Rotimi E. "Determination of Nutritional and Bioactive Properties of Peptides in Enzymatic Pea, Chickpea, and Mung Bean Protein Hydrolysates". Journal of AOAC INTERNATIONAL 91, n. 4 (1 luglio 2008): 947–56. http://dx.doi.org/10.1093/jaoac/91.4.947.

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Abstract Within the primary structure of many pea and mung bean proteins are peptide sequences that can potentially be used in the formulation of therapeutic products for the treatment and prevention of human diseases. However, these peptide sequences need protease treatments before they can be released free of the parent proteins. Unlike chemical hydrolysis, enzymatic treatment enables more efficient tailoring of peptide products without formation of toxic by-products or destruction of amino acids. This review provides information on current methods that have been used to convert inactive pea and mung bean proteins into bioactive peptides. It focuses on 3 main bioactive properties, such as inhibitions of (1) angiotensin converting enzyme (ACE) activity; (2) calmodulin (CaM)-dependent enzymes; and (3) copper-chelating activity. ACE is an established marker for hypertension, high levels of some CaM-dependent enzymes are risk factors for various human diseases including cancer and Alzheimer's disease, and high vascular copper concentrations may potentiate atherosclerosis. Also reviewed are the production and evaluation of activity of hypoallergenic peptides that may offer protection against anaphylactic reactions. The 3 main proteins discussed are chickpea, mung bean, and field pea.

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Szerszunowicz, Iwona, e Szymon Kozicki. "Plant-Derived Proteins and Peptides as Potential Immunomodulators". Molecules 29, n. 1 (29 dicembre 2023): 209. http://dx.doi.org/10.3390/molecules29010209.

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The immune response of humans may be modulated by certain biopeptides. The present study aimed to determine the immunomodulatory potential of plant-derived food proteins and hydrolysates obtained from these proteins via monocatalytic in silico hydrolysis (using ficin, stem bromelainm or pepsin (pH > 2)). The scope of this study included determinations of the profiles of select bioactivities of proteins before and after hydrolysis and computations of the frequency of occurrence of selected bioactive fragments in proteins (parameter A), frequency/relative frequency of the release of biopeptides (parameters AE, W) and the theoretical degree of hydrolysis (DHt), by means of the resources and programs available in the BIOPEP-UWM database. The immunomodulating (ImmD)/immunostimulating (ImmS) peptides deposited in the database were characterized as well (ProtParam tool). Among the analyzed proteins of cereals and legumes, the best precursors of ImmD immunopeptides (YG, YGG, GLF, TPRK) turned out to be rice and garden pea proteins, whereas the best precursors of ImmS peptides appeared to be buckwheat (GVM, GFL, EAE) and broad bean (LLY, EAE) proteins. The highest number of YG sequences was released by stem bromelain upon the simulated hydrolysis of rice proteins (AE = 0.0010–0.0820, W = 0.1994–1.0000, DHt = 45–82%). However, antibacterial peptides (IAK) were released by ficin only from rice, oat, and garden pea proteins (DHt = 41–46%). Biopeptides (YG, IAK) identified in protein hydrolysates are potential immunomodulators, nutraceuticals, and components of functional food that may modulate the activity of the human immune system. Stem bromelain and ficin are also active components that are primed to release peptide immunomodulators from plant-derived food proteins.

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Świątecka, Dominika, Aleksander Świątecki, Henryk Kostyra, Katarzyna Marciniak-Darmochwał e Elżbieta Kostyra. "The impact of pea protein hydrolysates on bacterial physiological activity—An in vitro study". International Journal of Food Microbiology 140, n. 2-3 (giugno 2010): 263–70. http://dx.doi.org/10.1016/j.ijfoodmicro.2010.03.015.

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Zhang, Yianna Y., Regine Stockmann, Ken Ng, James A. Broadbent, Sally Stockwell, Hafiz Suleria, Noor E. Karishma Shaik, Ranjith R. Unnithan e Said Ajlouni. "Characterization of Fe(III)-binding peptides from pea protein hydrolysates targeting enhanced iron bioavailability". Food Chemistry 405 (marzo 2023): 134887. http://dx.doi.org/10.1016/j.foodchem.2022.134887.

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Osman, Ali, Abdel-Rahaman M. Merwad, Azza H. Mohamed e Mahmoud Sitohy. "Foliar Spray with Pepsin-and Papain-Whey Protein Hydrolysates Promotes the Productivity of Pea Plants Cultivated in Clay Loam Soil". Molecules 26, n. 9 (10 maggio 2021): 2805. http://dx.doi.org/10.3390/molecules26092805.

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Papain and pepsin-hydrolyzed whey protein (PAH and PEH, respectively) were prepared and characterized for its degree of hydrolysis, chemical constituents (amino acid and peptides) and antioxidant activity. A field experiment was conducted at El Salheya El Gedida City, Sharqia, Egypt, during the seasons 2019 and 2020, to investigate the biological action of the foliar spray of PAH and PEH on the growth and yield of pea plants cultivated in a clay loam soil. Foliar application of the papain and pepsin-hydrolyzed whey protein (PAH and PEH, respectively) at 1000 and 2000 mg/L was applied three times after 25, 35 and 45 days from planting. All protein foliar spray treatments had significant positive effects on the uptake of N, P and K, simultaneously increasing the contents of all the photosynthetic pigments (Chlorophyll a, Chlorophyll b and Carotenoids) in a concentration-dependent manner. The most conspicuous increase was seen in Chlorophyll b (105% increase), followed by Carotenoids (91% increase). Generally, the favorable increases caused by the second level of application (2000 mg/L) were nearly 2–3 times that of the low level (1000 mg/L). Pod growth and formation indicators, e.g., no. of pod/plant, pod length and no. of seeds/pod, responded more evidently to the hydrolyzed than the intact form of whey protein treatments. Hydrolyzed whey protein foliar spray treatments achieved significantly higher increases in the global field yield components of Pisum sativum plants than the intact form, where peptic hydrolysates were significantly superior to papain hydrolysate. The treatment PEH (2000 mg/L) can be recommended as the most effective bio-stimulating foliar spray treatment for higher plant productivity when applied 25, 35 and 45 days after planting.

29

CHENTOUF, Aouatif. "Antioxidant Activity of Food Protein: Yellow Pea Protein Isolate NUTRALYS® S85F in a cell free Environment". Nutrition and Food Processing 4, n. 8 (8 dicembre 2021): 01–05. http://dx.doi.org/10.31579/2637-8914/075.

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Abstract (sommario):

In recent years, the demand for “all natural” products is increasing because of the increasing limitations on the use of synthetic antioxidants and enhanced public awareness of health issues. Many natural food components like oils and oilseeds, proteins and protein hydrolysates, fruits and vegetables, oat and rice bran, spices, herbs and tea have antioxidant properties. Natural antioxidants from these food components provide oxidative stability to the food product. The antioxidant activity of proteins is mainly due to interactions between their ability to inactivate reactive oxygen species, chelate pro-oxidative transition metals, scavenge free radicals, and reduction of hydroperoxides. The objective of this study was to verify the antioxidant potential of Pea Protein Isolate ‘NUTRALYS® S85F' through different in vitro tests: TOTAL ANTIOXIDANT RADICAL SCAVENGING ACTIVITY (ORAC ASSAY); SUPEROXIDE RADICAL SCAVENGING ACTIVITY (NBT ASSAY); LIPID PEROXIDATION INHIBITION ASSAY (MDA KIT); HYDROXYL RADICAL SCAVENGING ACTIVITY (HRS ASSAY); NITRIC OXIDE SCAVENGING ABILITY NUTRALYS® S85F clearly demonstrates intrinsic antioxidant activities as can be observed from its scavenging activity toward the peroxyl radicals (ORAC), scavenger of the superoxide radicals (NBT), hydroxyl radical scavenging (HRS), prevention of lipid oxidation (MDA) and nitric oxide scavenging (NO) capabilities. Based on our results, NUTRALYS® S85F will provide oxidative stability to food products and health benefits to the consumer.

30

Panasiuk, R., R. Amarowicz, H. Kostyra e L. Sijtsma. "Determination of α-amino nitrogen in pea protein hydrolysates: a comparison of three analytical methods". Food Chemistry 62, n. 3 (luglio 1998): 363–67. http://dx.doi.org/10.1016/s0308-8146(97)00164-7.

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Asen, Nancy D., Ogadimma D. Okagu, Chibuike C. Udenigwe e Rotimi E. Aluko. "Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates". Journal of Functional Foods 106 (luglio 2023): 105590. http://dx.doi.org/10.1016/j.jff.2023.105590.

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32

Xia, Yixuan, Ling Zhu, Gangcheng Wu, Tongtong Liu, Xiaojing Li, Xingguo Wang e Hui Zhang. "Comparative study of various methods used for bitterness reduction from pea (Pisum sativum L.) protein hydrolysates". LWT 159 (aprile 2022): 113228. http://dx.doi.org/10.1016/j.lwt.2022.113228.

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Chao, Dongfang, Rong He, Stephanie Jung e Rotimi E. Aluko. "Effect of pressure or temperature pretreatment of isolated pea protein on properties of the enzymatic hydrolysates". Food Research International 54, n. 2 (dicembre 2013): 1528–34. http://dx.doi.org/10.1016/j.foodres.2013.09.020.

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Wang, Shuguang, Mouming Zhao, Hongbing Fan e Jianping Wu. "Peptidomics Study of Plant-Based Meat Analogs as a Source of Bioactive Peptides". Foods 12, n. 5 (2 marzo 2023): 1061. http://dx.doi.org/10.3390/foods12051061.

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Abstract (sommario):

The demand for plant-based meat analogs (PBMA) is on the rise as a strategy to sustain the food protein supply while mitigating environmental change. In addition to supplying essential amino acids and energy, food proteins are known sources of bioactive peptides. Whether protein in PBMA affords similar peptide profiles and bioactivities as real meat remains largely unknown. The purpose of this study was to investigate the gastrointestinal digestion fate of beef and PBMA proteins with a special focus on their potential as precursors of bioactive peptides. Results showed that PBMA protein showed inferior digestibility than that in beef. However, PBMA hydrolysates possessed a comparable amino acid profile to that of beef. A total of 37, 2420 and 2021 peptides were identified in the gastrointestinal digests of beef, Beyond Meat and Impossible Meat, respectively. The astonishingly fewer peptides identified from beef digest is probably due to the near-full digestion of beef proteins. Almost all peptides in Impossible Meat digest were from soy, whereas 81%, 14% and 5% of peptides in Beyond Meat digest were derived from pea, rice and mung proteins, respectively. Peptides in PBMA digests were predicted to exert a wide range of regulatory roles and were shown to have ACE inhibitory, antioxidant and anti-inflammatory activities, supporting the potential of PBMA as a source of bioactive peptides.

35

Andarwulan, Nuri, e Kalidas Shetty. "Improvement of pea (Pisum sativum) seed vigour response by fish protein hydrolysates in combination with acetyl salicylic acid". Process Biochemistry 35, n. 1-2 (ottobre 1999): 159–65. http://dx.doi.org/10.1016/s0032-9592(99)00047-3.

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Olagunju, Aderonke I., Olufunmilayo S. Omoba, Victor N. Enujiugha, Adeola M. Alashi e Rotimi E. Aluko. "Pigeon pea enzymatic protein hydrolysates and ultrafiltration peptide fractions as potential sources of antioxidant peptides: An in vitro study". LWT 97 (novembre 2018): 269–78. http://dx.doi.org/10.1016/j.lwt.2018.07.003.

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Su, Guowan, Yuxi Xie, Ruili Liu, Guodong Cui, Mouming Zhao e Jianan Zhang. "Effect of transglutaminase on taste characteristics of pea protein hydrolysates through altering the composition of amino acids and peptides". Food Bioscience 56 (dicembre 2023): 103261. http://dx.doi.org/10.1016/j.fbio.2023.103261.

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38

Zhang, Xiaogang, Parinya Noisa e Jirawat Yongsawatdigul. "Chemical and Cellular Antioxidant Activities of In Vitro Digesta of Tilapia Protein and Its Hydrolysates". Foods 9, n. 6 (25 giugno 2020): 833. http://dx.doi.org/10.3390/foods9060833.

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Abstract (sommario):

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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Awosika, Temitola O., e Rotimi E. Aluko. "Inhibition of the in vitro activities of α‐amylase, α‐glucosidase and pancreatic lipase by yellow field pea ( Pisum sativum L.) protein hydrolysates". International Journal of Food Science & Technology 54, n. 6 (4 gennaio 2019): 2021–34. http://dx.doi.org/10.1111/ijfs.14087.

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Nongonierma, Alice B., e Richard J. FitzGerald. "Investigation of the Potential of Hemp, Pea, Rice and Soy Protein Hydrolysates as a Source of Dipeptidyl Peptidase IV (DPP-IV) Inhibitory Peptides". Food Digestion 6, n. 1-3 (7 maggio 2015): 19–29. http://dx.doi.org/10.1007/s13228-015-0039-2.

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41

Bakratsas, Georgios, Angeliki Polydera, Oskar Nilson, Alexandra V. Chatzikonstantinou, Charilaos Xiros, Petros Katapodis e Haralambos Stamatis. "Mycoprotein Production by Submerged Fermentation of the Edible Mushroom Pleurotus ostreatus in a Batch Stirred Tank Bioreactor Using Agro-Industrial Hydrolysate". Foods 12, n. 12 (7 giugno 2023): 2295. http://dx.doi.org/10.3390/foods12122295.

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Abstract (sommario):

The demand for cheap, healthy, and sustainable alternative protein sources has turned research interest into microbial proteins. Mycoproteins prevail due to their quite balanced amino acid profile, low carbon footprint and high sustainability potential. The goal of this research was to investigate the capability of Pleurotus ostreatus to metabolize the main sugars of agro-industrial side streams, such as aspen wood chips hydrolysate, to produce high-value protein with low cost. Our results indicate that P. ostreatus LGAM 1123 could be cultivated both in a C-6 (glucose)- and C-5(xylose)-sugar-containing medium for mycoprotein production. A mixture of glucose and xylose was found to be ideal for biomass production with high protein content and rich amino acid profile. P. ostreatus LGAM 1123 cultivation in a 4 L stirred-tank bioreactor using aspen hydrolysate was achieved with 25.0 ± 3.4 g L−1 biomass production, 1.8 ± 0.4 d−1 specific growth rate and a protein yield of 54.5 ± 0.5% (g/100 g sugars). PCA analysis of the amino acids revealed a strong correlation between the amino acid composition of the protein produced and the ratios of glucose and xylose in the culture medium. The production of high-nutrient mycoprotein by submerged fermentation of the edible fungus P. ostreatus using agro-industrial hydrolysates is a promising bioprocess in the food and feed industry.

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Ratnayani, Ketut, Putu Ajeng Agustini, Ni Wayan Wisaniyasa, Ni Made Puspawati e I. Nengah Wirajana. "Enzymatic Hydrolysis of Pigeon Pea Sprout Protein and its Potential to Generate Savory Taste". International Journal of Current Microbiology and Applied Sciences 12, n. 12 (10 dicembre 2023): 101–8. http://dx.doi.org/10.20546/ijcmas.2023.1212.013.

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Abstract (sommario):

The germination process is one way to improve the quality of legume protein, which will be used as a substrate in the production of protein hydrolysate. This study aims to hydrolyze pigeon pea (Cajanus cajan (L.) Millsp.) sprout protein concentrate by using alcalase enzymes to obtain protein hydrolysate which has the potential to generate a savory or umami taste. The research began with total protein extraction to generate pigeon pea sprout protein concentrate which was then used as a substrate in the hydrolysis process treated with variations ratio of the Enzyme to the Substrate (E/S ratio). Each protein hydrolysate obtained was characterized based on free α-amino content, soluble protein content, and sensory evaluation of the savory taste level. Protein hydrolysis results in the range of E/S ratio 0.1% - 1.5% showed that the E/S ratio 1.5% was able to produce the highest content of free α-amino (2.95±0.08 mg/mL) and soluble protein content (13.69±0.11 mg/mL). Besides that, the highest sensory evaluation score was obtained in the E/S ratio of 1.0%. This result shows that the protein hydrolysate of pigeon pea sprouts can be used as a natural flavor.

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Häberer, C. D., K. Diepvens, N. Geary e W. Langhans. "Intragastric infusion of pea protein hydrolysate reduces food intake more than pea protein." Appetite 49, n. 1 (luglio 2007): 295. http://dx.doi.org/10.1016/j.appet.2007.03.081.

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Daher, Dahlia, Barbara Deracinois, Alain Baniel, Elodie Wattez, Justine Dantin, Renato Froidevaux, Sylvie Chollet e Christophe Flahaut. "Principal Component Analysis from Mass Spectrometry Data Combined to a Sensory Evaluation as a Suitable Method for Assessing Bitterness of Enzymatic Hydrolysates Produced from Micellar Casein Proteins". Foods 9, n. 10 (24 settembre 2020): 1354. http://dx.doi.org/10.3390/foods9101354.

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Abstract (sommario):

Enzymatic hydrolysis of food proteins generally changes the techno-functional, nutritional, and organoleptic properties of hydrolyzed proteins. As a result, protein hydrolysates have an important interest in the food industries. However, they tend to be characterized by a bitter taste and some off-flavors, which limit their use in the food industry. These tastes and aromas come from peptides, amino acids, and volatile compounds generated during hydrolysis. In this article, sixteen more or less bitter enzymatic hydrolysates produced from a milk protein liquid fraction enriched in micellar caseins using commercially available, food-grade proteases were subjected to a sensory analysis using a trained and validated sensory panel combined to a peptidomics approach based on the peptide characterization by reverse-phase high-performance liquid chromatography, high-resolution mass spectrometry, and bioinformatics software. The comparison between the sensory characteristics and the principal components of the principal component analysis (PCA) of mass spectrometry data reveals that peptidomics constitutes a convenient, valuable, fast, and economic intermediate method to evaluating the bitterness of enzymatic hydrolysates, as a trained sensory panel can do it.

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Häberer, Doreen, Maria Tasker, Martin Foltz, Nori Geary, Margriet Westerterp e Wolfgang Langhans. "Intragastric infusion of pea-protein hydrolysate reduces test-meal size in rats more than pea protein". Physiology & Behavior 104, n. 5 (ottobre 2011): 1041–47. http://dx.doi.org/10.1016/j.physbeh.2011.07.003.

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46

Li, Huan, e Rotimi E. Aluko. "Identification and Inhibitory Properties of Multifunctional Peptides from Pea Protein Hydrolysate". Journal of Agricultural and Food Chemistry 58, n. 21 (10 novembre 2010): 11471–76. http://dx.doi.org/10.1021/jf102538g.

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47

Soral-Smietana, Maria, Ryszard Amarowicz, Alicja Swigon e Lolke Sijtsma. "Comparison of solubility of pea protein hydrolysate by three analytical methods". International Journal of Food Sciences and Nutrition 50, n. 6 (gennaio 1999): 407–11. http://dx.doi.org/10.1080/096374899100978.

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48

Sarigiannidou, Krystalia, Davide Odelli, Flemming Jessen, Mohammad Amin Mohammadifar, Fatemeh Ajalloueian, Mar Vall-llosera, Antonio Fernandes de Carvalho e Federico Casanova. "Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength". Colloids and Interfaces 6, n. 4 (7 dicembre 2022): 76. http://dx.doi.org/10.3390/colloids6040076.

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Abstract (sommario):

The effect of a tryptic hydrolysis as well as the effect of ionic strength (0–0.4 M NaCl) was investigated on the oil/water interfacial properties of soluble pea protein hydrolysate (SPPH) at neutral pH and room temperature (20 ± 0.01 °C). SEC-MALS and SDS-Page analysis showed that tryptic hydrolysis created a lower molecular weight polypeptide mixture, whereas FTIR analysis and DSC thermograms demonstrated a more disordered and flexible structure. The bulk properties of SPPH were studied in terms of hydrodynamic diameter and turbidity, where higher particle size (+ ~13 nm) and turbidity were observed at 0.4 M NaCl. Regarding the interfacial properties, the surface activity of SPPH improved by increasing ionic strength, with maximum interfacial pressure (14.28 mN/m) at 0.4 M NaCl. Nevertheless, the addition of NaCl negatively affected the elasticity and strength of the interfacial film, where the sample without salt exhibited the highest dilatational and shear storage modulus in all the frequencies considered.

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Verma, Nitin, Mukesh C. Bansal e Vivek Kumar. "Pea peel waste: A lignocellulosic waste and its utility in cellulase production by Tricoderma reesei under solid state cultivation". BioResources 6, n. 2 (16 marzo 2011): 1505–19. http://dx.doi.org/10.15376/biores.6.2.1505-1519.

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Abstract (sommario):

A wide variety of waste bioresources are available on our planet for conversion into bioproducts. In the biological systems, microorganisms are used to utilize waste as an energy source for the synthesis of valuable products such as biomass proteins and enzymes. The large quantities of byproducts generated during the processing of plant food involve an economic and environmental problem due to their high volumes and elimination costs. After isolation of the main constituent, there are abundant remains which represent an inexpensive material that has been undervalued until now. Pea peel waste is one of the undervalued, unused sources of energy that can serve as a potential source for cellulase production. Batch experiments have been performed, using pea peel waste as a carbon source for cellulase production under solid state cultivation by Trichoderma reesei. It was observed that 30 oC temperature and pH 5.0 are the most favorable conditions for cellulase production by T. reesei. FPase activity significantly increases by incorporation of whey as well as wheat starch hydrolysate in the basal salt media used in the production study. The present study describes the utility of pea peel waste, whey as well as wheat starch hydrolysate in cellulase production by T. reesei. The utilization of economically cheap, pea peel waste for cellulase production could be a novel, cost effective, and valuable approach in cellulase production as well as in solid waste management.

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Liao, Wang, Xinyi Cao, Hui Xia, Shaokang Wang e Guiju Sun. "Pea Protein-Derived Peptides Inhibit Hepatic Glucose Production via the Gluconeogenic Signaling in the AML-12 Cells". International Journal of Environmental Research and Public Health 19, n. 16 (18 agosto 2022): 10254. http://dx.doi.org/10.3390/ijerph191610254.

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Abstract (sommario):

Pea protein is considered to be a high quality dietary protein source, but also it is an ideal raw material for the production of bioactive peptides. Although the hypoglycemic effect of pea protein hydrolysate (PPH) has been previously reported, the underlying mechanisms, in particular its effect on the hepatic gluconeogenesis, remain to be elucidated. In the present study, we found that PPH suppressed glucose production in mouse liver cell-line AML-12 cells. Although both of the gluconeogenic and insulin signaling pathways in the AML-12 cells could be regulated by PPH, the suppression of glucose production was dependent on the inhibition of the cAMP response element-binding protein (CREB)-mediated signaling in the gluconeogenic pathway, but not the activation of insulin signaling. Findings from the present study have unveiled a novel role of PPH underlying its anti-diabetic activity, which could be helpful to accelerate the development of functional foods and nutraceuticals using PPH as a starting material.