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1

Pérez-Gálvez, Raúl, Carmen Berraquero-García, J. Lizeth Ospina-Quiroga, et al. "Influence of In Vitro Digestion on Dipeptidyl Peptidase-IV (DPP-IV) Inhibitory Activity of Plant-Protein Hydrolysates Obtained from Agro-Industrial By-Products." Foods 13, no. 17 (2024): 2691. http://dx.doi.org/10.3390/foods13172691.

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This study investigates the production of protein hydrolysates with dipeptidyl peptidase-IV (DPP-IV) inhibitory activity from agro-industrial by-products, namely olive seed, sunflower seed, rapeseed, and lupin meals, as well as from two plant protein isolates such as pea and potato. Furthermore, the effect of simulated gastrointestinal digestion on the DPP-IV inhibitory activity of all the hydrolysates was evaluated. Overall, the lowest values of IC50 (1.02 ± 0.09 – 1.24 ± 0.19 mg protein/mL) were observed for the hydrolysates with a high proportion of short-chain [< 1 kDa] peptides (i.e.,
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2

Ratnayani, Ketut, Indriani Wisnu Susanto Panjaitan, and 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, no. 1 (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 tot
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3

Ruiz, Raquel, Raquel Olías, Alfonso Clemente та 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, № 6 (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 vicili
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Awosika, Temitola, and Rotimi E. Aluko. "Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors." Foods 8, no. 6 (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 w
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5

Siriporn, B., P. Thongkorn, S. Waraporn, et al. "Antioxidant polypeptides derived from pigeon pea (Cajanus cajan (L) Mill sp.) by enzymatic hydrolysis." Food Research 8, Supplementary 2 (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,
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6

Hidayat, Meilinah, Sijani Prahastuti, TeresaLiliana Wargasetia, et al. "Role of pea protein hydrolysates as antinephrotoxicity." Journal of Reports in Pharmaceutical Sciences 8, no. 1 (2019): 55. http://dx.doi.org/10.4103/jrptps.jrptps_14_17.

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7

Soral-Śmietana, M., A. Świgoń, R. Amarowicz, and L. Sijtsma. "The solubility of trypsin pea protein hydrolysates." Nahrung / Food 42, no. 03-04 (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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8

Krasnoshtanova, Alla Al'bertovna, and 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, no. 4 (December 15, 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: chym
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9

Stanisavljevic, Nemanja, Goran Vukotic, Ferenc Pastor, et al. "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria." Archives of Biological Sciences 67, no. 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 &lt;10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric
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10

Moreno, Cecilia, Luis Mojica, Elvira González de Mejía, Rosa María Camacho Ruiz, and Diego A. Luna-Vital. "Combinations of Legume Protein Hydrolysates Synergistically Inhibit Biological Markers Associated with Adipogenesis." Foods 9, no. 11 (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
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11

Velyamov, Massimzhan, Zhumatay Urazbayev, Shukhrat Velyamov, Turar Bakytzhan, and Aelina Abitbekova. "Development of technology for producing protein hydrolysates from leguminous plants (peas) for sports nutrition." Scifood 19 (January 1, 2025): 79–95. https://doi.org/10.5219/scifood.6.

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In line with emerging trends, the sports nutrition industry actively seeks cost-effective and health-promoting protein ingredients to replace animal-derived products and transition toward more sustainable practices. Protein concentrates derived from legumes, including peas, have attracted consumer interest due to their rich amino acid profiles and favourable functional properties. Our research aimed to develop and optimise an enzymatic technology for producing protein hydrolysates from locally adapted pea varieties in Kazakhstan. Based on the research findings, optimal technological conditions
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12

Humiski, L. M., and R. E. Aluko. "Physicochemical and Bitterness Properties of Enzymatic Pea Protein Hydrolysates." Journal of Food Science 72, no. 8 (2007): S605—S611. http://dx.doi.org/10.1111/j.1750-3841.2007.00475.x.

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13

Bollati, Carlotta, Ruoxian Xu, Giovanna Boschin, et al. "Integrated Evaluation of the Multifunctional DPP-IV and ACE Inhibitory Effect of Soybean and Pea Protein Hydrolysates." Nutrients 14, no. 12 (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
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14

Dent, Terrence, Allison LeMinh, and Farnaz Maleky. "Comparison of Colorimetric Methods for Measuring the Solubility of Legume Proteins." Gels 10, no. 9 (2024): 551. http://dx.doi.org/10.3390/gels10090551.

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Increasing the use of plant proteins in foods requires improving their physical and chemical properties, such as emulsification, gelation capacity, and thermal stability. These properties determine the acceptability and functionality of food products. Higher protein solubility significantly impacts these properties by affecting denaturation and the stability of emulsifiers or gels. Therefore, developing plant-based protein ingredients requires accurately and conveniently measuring their solubility. Colorimetric solubility methods overcome many issues of more robust combustion and titration met
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15

Uro-Chukwu, Henry Chukwuemeka, Eric Chigozie Okoli, Laura Chioma Okpala, and Franklyn Chidiebere Uro-Chukwu. "Antioxidant and cytotoxic activities of protein hydrolysates from shrimp shell wastes, germinated soybean and pigeon pea flour blends: A mixture response surface methodology approach." Journal of Drug Delivery and Therapeutics 14, no. 6 (2024): 7–14. http://dx.doi.org/10.22270/jddt.v14i6.6616.

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Cancer has high prevalence rate and mortality with conventional chemotherapy and other management protocols being both expensive and inaccessible especially in low/medium income countries (LMIC). Sourcing alternative cheaper and easily accessible treatment from blends of antioxidants sources can reduce the burden of cancer on patients. This work therefore seeks to produce a blend from the protein hydrolysates of shrimp shell waste, germinated soybean and germinated pigeon pea which not only has high antioxidant activity but also can inhibit cervical cancer cell proliferation. In vitro antioxid
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16

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

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17

Frączek, R., E. Kostyra, H. Kostyra, and S. Krawczuk. "Immunoreactive properties of pea protein extract and its trypsin hydrolysates." Journal of Animal and Feed Sciences 16, no. 3 (2007): 472–84. http://dx.doi.org/10.22358/jafs/66803/2007.

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18

Marinova, Margarita D., and Bozhidar P. Tchorbanov. "Preparation of Antioxidant Enzymatic Hydrolysates from Honeybee-Collected Pollen Using Plant Enzymes." Enzyme Research 2010 (January 9, 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 conten
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19

Köstekli Büyükcan, Mine, and Sibel Karakaya. "Comparison of some functional properties and protein profiles of different protein sources with egg components." Italian Journal of Food Science 33, no. 2 (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 red
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20

Barac, Miroljub, Slavica Cabrilo, Sladjana Stanojevic, et al. "Functional properties of protein hydrolysates from pea (Pisum sativum,L) seeds." International Journal of Food Science & Technology 47, no. 7 (2012): 1457–67. http://dx.doi.org/10.1111/j.1365-2621.2012.02993.x.

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21

Zhao, Dan, and Xiaolan Liu. "Purification, Identification and Evaluation of Antioxidant Peptides from Pea Protein Hydrolysates." Molecules 28, no. 7 (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
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22

Rizzello, Carlo Giuseppe, Anna Lavecchia, Valerio Gramaglia, and Marco Gobbetti. "Long-Term Fungal Inhibition by Pisum sativum Flour Hydrolysate during Storage of Wheat Flour Bread." Applied and Environmental Microbiology 81, no. 12 (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
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23

Li, Huan, and >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, no. 3-4 (2006): 178–89. http://dx.doi.org/10.1080/09637480600659144.

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24

Barbana, Chockry, and Joyce Irene Boye. "Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates." Food Research International 43, no. 6 (2010): 1642–49. http://dx.doi.org/10.1016/j.foodres.2010.05.003.

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25

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

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26

Girgih, Abraham T., Dongfang Chao, Lin Lin, Rong He, Stephanie Jung, and 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 (December 2015): 510–16. http://dx.doi.org/10.1016/j.foodchem.2015.05.024.

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27

Zhou, Xue, Heping Cui, Qiang Zhang, et al. "Taste improvement of Maillard reaction intermediates derived from enzymatic hydrolysates of pea protein." Food Research International 140 (February 2021): 109985. http://dx.doi.org/10.1016/j.foodres.2020.109985.

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28

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, no. 4 (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
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29

Szerszunowicz, Iwona, and Szymon Kozicki. "Plant-Derived Proteins and Peptides as Potential Immunomodulators." Molecules 29, no. 1 (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 &gt; 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 biopeptid
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30

Osman, Ali, Abdel-Rahaman M. Merwad, Azza H. Mohamed, and Mahmoud Sitohy. "Foliar Spray with Pepsin-and Papain-Whey Protein Hydrolysates Promotes the Productivity of Pea Plants Cultivated in Clay Loam Soil." Molecules 26, no. 9 (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 tim
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31

Świątecka, Dominika, Aleksander Świątecki, Henryk Kostyra, Katarzyna Marciniak-Darmochwał, and Elżbieta Kostyra. "The impact of pea protein hydrolysates on bacterial physiological activity—An in vitro study." International Journal of Food Microbiology 140, no. 2-3 (2010): 263–70. http://dx.doi.org/10.1016/j.ijfoodmicro.2010.03.015.

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32

Zhang, Yianna Y., Regine Stockmann, Ken Ng, et al. "Characterization of Fe(III)-binding peptides from pea protein hydrolysates targeting enhanced iron bioavailability." Food Chemistry 405 (March 2023): 134887. http://dx.doi.org/10.1016/j.foodchem.2022.134887.

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33

CHENTOUF, Aouatif. "Antioxidant Activity of Food Protein: Yellow Pea Protein Isolate NUTRALYS® S85F in a cell free Environment." Nutrition and Food Processing 4, no. 8 (2021): 01–05. http://dx.doi.org/10.31579/2637-8914/075.

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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, ch
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Panasiuk, R., R. Amarowicz, H. Kostyra та L. Sijtsma. "Determination of α-amino nitrogen in pea protein hydrolysates: a comparison of three analytical methods". Food Chemistry 62, № 3 (1998): 363–67. http://dx.doi.org/10.1016/s0308-8146(97)00164-7.

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35

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

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36

Xia, Yixuan, Ling Zhu, Gangcheng Wu, et al. "Comparative study of various methods used for bitterness reduction from pea (Pisum sativum L.) protein hydrolysates." LWT 159 (April 2022): 113228. http://dx.doi.org/10.1016/j.lwt.2022.113228.

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37

Chao, Dongfang, Rong He, Stephanie Jung, and Rotimi E. Aluko. "Effect of pressure or temperature pretreatment of isolated pea protein on properties of the enzymatic hydrolysates." Food Research International 54, no. 2 (2013): 1528–34. http://dx.doi.org/10.1016/j.foodres.2013.09.020.

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38

Wang, Shuguang, Mouming Zhao, Hongbing Fan, and Jianping Wu. "Peptidomics Study of Plant-Based Meat Analogs as a Source of Bioactive Peptides." Foods 12, no. 5 (2023): 1061. http://dx.doi.org/10.3390/foods12051061.

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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
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39

Витол, И. С. "Characteristics of products of enzymatic modification of legume seeds." Food processing industry, no. 10 (September 28, 2024): 73–76. http://dx.doi.org/10.52653/ppi.2024.10.10.014.

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Биотехнологические способы глубокой переработки семян бобовых культур позволяют получать компоненты, включение которых в рецептуру новых пищевых продуктов обеспечивает повышение пищевой ценности и придание функциональной направленности готовым изделиям. Целью исследования являлась разработка способов получения гидролизатов и структурно-модифицированной цельносмолотой муки семян сои, гороха, нута и чечевицы с использованием двух композиций ферментных препаратов целлюлолитического, протеолитического и фитазного действия. Установлено, что ФП, входящие в состав мультэнзимных композиций, проявляют
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40

Andarwulan, Nuri, and Kalidas Shetty. "Improvement of pea (Pisum sativum) seed vigour response by fish protein hydrolysates in combination with acetyl salicylic acid." Process Biochemistry 35, no. 1-2 (1999): 159–65. http://dx.doi.org/10.1016/s0032-9592(99)00047-3.

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41

Zhang, Xiaogang, Parinya Noisa, and Jirawat Yongsawatdigul. "Chemical and Cellular Antioxidant Activities of In Vitro Digesta of Tilapia Protein and Its Hydrolysates." Foods 9, no. 6 (2020): 833. http://dx.doi.org/10.3390/foods9060833.

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Production of protein hydrolysate as nutraceuticals is typically based on the activity of the hydrolysate, which might not yield the optimal activity under physiological condition due to structural modification of peptides upon gastrointestinal (GI) digestion. This study systematically compared the chemical and cellular antioxidant activities of the in vitro digesta of tilapia protein and its hydrolysates prepared with various degree of hydrolysis (DH) by Alcalase. The enzymes used in the in vitro GI digestion analysis significantly contributed to the peptide content, Trolox equivalent antioxi
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Olagunju, Aderonke I., Olufunmilayo S. Omoba, Victor N. Enujiugha, Adeola M. Alashi, and Rotimi E. Aluko. "Pigeon pea enzymatic protein hydrolysates and ultrafiltration peptide fractions as potential sources of antioxidant peptides: An in vitro study." LWT 97 (November 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, and Jianan Zhang. "Effect of transglutaminase on taste characteristics of pea protein hydrolysates through altering the composition of amino acids and peptides." Food Bioscience 56 (December 2023): 103261. http://dx.doi.org/10.1016/j.fbio.2023.103261.

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Куликов, Д. С., З. И. Калугина, М. Д. Ермолаева, С. Е. Шевченко, and В. А. Бызов. "Modification of functional and technological properties of protein products from peas by domestic bacterial proteases." Food processing industry, no. 8 (August 2, 2024): 93–101. http://dx.doi.org/10.52653/ppi.2024.8.8.018.

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В настоящее время разрабатываются способы увеличения качества, конкурентоспособности и расширения ассортимента отечественных белковых продуктов из растительного сырья путем модификации их функционально-технологических свойств (ФТС). Эффективная модификация ФТС белков достигается обработкой их импортными бактериальными ферментными препаратами (ФП) протеолитического действия. Политика импортозамещения и недостаточность сведений о влиянии российских ферментных препаратов на ФТС белков определяют актуальность данной работы. Цель работы – определение оптимальных параметров протеолиза белковых проду
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Awosika, Temitola O., та 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, № 6 (2019): 2021–34. http://dx.doi.org/10.1111/ijfs.14087.

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Nongonierma, Alice B., and 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, no. 1-3 (2015): 19–29. http://dx.doi.org/10.1007/s13228-015-0039-2.

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Bakratsas, Georgios, Angeliki Polydera, Oskar Nilson, et al. "Mycoprotein Production by Submerged Fermentation of the Edible Mushroom Pleurotus ostreatus in a Batch Stirred Tank Bioreactor Using Agro-Industrial Hydrolysate." Foods 12, no. 12 (2023): 2295. http://dx.doi.org/10.3390/foods12122295.

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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-c
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Ratnayani, Ketut, Putu Ajeng Agustini, Ni Wayan Wisaniyasa, Ni Made Puspawati, and 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, no. 12 (2023): 101–8. http://dx.doi.org/10.20546/ijcmas.2023.1212.013.

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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).
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Häberer, C. D., K. Diepvens, N. Geary, and W. Langhans. "Intragastric infusion of pea protein hydrolysate reduces food intake more than pea protein." Appetite 49, no. 1 (2007): 295. http://dx.doi.org/10.1016/j.appet.2007.03.081.

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Daher, Dahlia, Barbara Deracinois, Alain Baniel, et al. "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, no. 10 (2020): 1354. http://dx.doi.org/10.3390/foods9101354.

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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 casei
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