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Journal articles on the topic 'Soybean protein hydrolysates'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Li, Wenzhi, Tiantian Zhao, Jianan Zhang, Changping Wu, Mouming Zhao, and Guowan Su. "Comparison of Neuroprotective and Cognition-Enhancing Properties of Hydrolysates from Soybean, Walnut, and Peanut Protein." Journal of Chemistry 2016 (2016): 1–8. http://dx.doi.org/10.1155/2016/9358285.

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Hydrolysates were prepared from soybean, walnut, and peanut protein by papain, respectively. Their amino acid compositions and molecular weight distributions, the effects of various hydrolysates on H2O2-induced injury PC12 cells, and cognition of mice were investigated, respectively. Results showed that the three hydrolysates were dominated by the peptides with 1–3 KDa with large amount of neurotrophic amino acids. All the hydrolysates exhibited much stronger inhibitory activity against H2O2-induced toxicity than cerebrolysin, and soy protein hydrolysate showed the highest activity. Moreover, the hydrolysates also could reduce the rate of nonviable apoptotic cells at the concentration of 2 mg/mL. The test of animal’s cognition indicated that three hydrolysates could present partly better effect of improving recurred memory ability of normal mice and consolidated memory ability of anisodine-treated mice than piracetam. Therefore, soybean, walnut, and peanut protein hydrolysates were recommended as a potential food raw material for prevention or treatment of neurodegenerative disorders.

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2

Ngoc, Ngo Minh. "ANTIOXIDANT ACTIVITIES OF HYDROLYSATES ORIGINATED FROM SOYBEAN AND SOY MILK RESIDUE." Vietnam Journal of Science and Technology 55, no. 5A (March 24, 2018): 134. http://dx.doi.org/10.15625/2525-2518/55/5a/12188.

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Soybean (Glycine max) and soy milk residue (okara) are protein-rich materials. Soybean possesses the highest protein content among different types of beans (protein content of soybean varies from 40–42 %). Soy milk residue, a by-product of the soy milk manufacturing industry, contains approximately 27 % protein (by dry weight). A number of recent studies have investigated the improvement of functional properties of protein contained in soybean and okara by fermentation or by the use of proteolytic enzymes. The aim of this study was to evaluate the antioxidant activities of soybean and okara hydrolysates obtained by the fermentation with Aspergillus oryzae or by using proteolytic enzymes (neutrase and flavourzyme). DPPH radical scavenging assay was used to determine the antioxidant activities of hydrolysates. The concentration of peptides required to scavenge DPPH radical by 50 % (IC50 value) was used to evaluate the antioxidant activity of peptides produced obtained from hydrolysates. The results showed that when fermented with A. oryzae, the okara hydrolysate had higher antioxidant activity than the soybean hydrolysate, with IC50 values of 0.447 mg/ml and 3.95 mg/ml, respectively. The hydrolyzed okara obtained from hydrolysis using Neutrase had higher antioxidant activity than the one obtained from hydrolysis using Flavourzyme, with IC50 values of0.200 mg/ml and 0.407 mg/ml, respectively. Different peptide fractions obtained from the hydrolysates using cut-off membrane (10 kDa, 3 kDa and 1 kDa) possessed different antioxidant activities. The < 1 kDa peptide fraction exhibited the highest antioxidant activity with an IC50 value of 0.158 mg/ml.

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3

Soria-Hernández, Cintya G., Sergio O. Serna-Saldívar, and Cristina Chuck-Hernández. "Comparison of Physicochemical, Functional and Nutritional Properties between Proteins of Soybean and a Novel Mixture of Soybean-Maize." Applied Sciences 10, no. 19 (October 8, 2020): 6998. http://dx.doi.org/10.3390/app10196998.

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Vegetable proteins are potential low-cost alternatives to solve the protein deficiency of the world population. A protein extracted from a mixture of soybean meal and maize germ was developed to offer more protein alternatives with high nutritional value. In this study, physicochemical, functional, and nutritional characteristics of isolates and hydrolysates of soybean and counterparts extracted from a soybean meal-maize germ were compared. The isolate and hydrolysate of the soybean-maize blend had a protein content of 93.9% and 73.6%, respectively. These protein mixtures contained 10% and 52% more solubility, 303.9%, and 22.7% more emulsifying capacity, 4.5% and 4.2% higher foam density and 36.3% and 1.2% more coagulation capacity compared to the soybean isolate and hydrolysate. Electrophoretic profiles of soybean-maize proteins showed four additional bands to the typical soybean pattern of 56, 55, 52 and 18 kDa, which could correspond to globulins and zeins from maize. The isolate extracted from the mixture of soybean meal and maize is a new alternative to provide the necessary amino acids for proper physical and mental development. Additionally, it has a high potential to be used as an ingredient by the food industry due to its excellent functionality and nutritional value.

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4

Tchorbanov, Bozhidar, Margarita Marinova, and Lydia Grozeva. "Debittering of Protein Hydrolysates by Lactobacillus LBL-4 Aminopeptidase." Enzyme Research 2011 (August 24, 2011): 1–7. http://dx.doi.org/10.4061/2011/538676.

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Yoghurt strain Lactobacillus LBL-4 cultivated for 8–10 h at pH ~6.0 was investigated as a considerable food-grade source of intracellular aminopeptidase. Cell-free extract manifesting >200 AP U/l was obtained from cells harvested from 1 L culture media. Subtilisin-induced hydrolysates of casein, soybean isolate, and Scenedesmus cell protein with degree of hydrolysis 20–22% incubated at 45∘C for 10 h by 10 AP U/g peptides caused an enlarging of DH up to 40–42%, 46–48%, and 38–40% respectively. The DH increased rapidly during the first 4 h, but gel chromatography studies on BioGel P-2 showed significant changes occurred during 4–10 h of enzyme action when the DH increased gradually. After the digestion, the remained AP activity can be recovered by ultrafiltration (yield 40–50%). Scenedesmus protein hydrolysate with DH 20% was inoculated by Lactobacillus LBL-4 cells, and after 72 h cultivation the DH reached 32%. The protein hydrolysates (DH above 40%) obtained from casein and soybean isolate (high Q value) demonstrated a negligible bitterness while Scenedesmus protein hydrolysates (low Q value) after both treatments were free of bitterness.

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5

Riyanto, Bambang, Wini Trilaksani, and Rika Lestari. "Sport Nutrition Drinks Based on Octopus Protein Hydrolysate." Jurnal Pengolahan Hasil Perikanan Indonesia 19, no. 3 (December 26, 2016): 339. http://dx.doi.org/10.17844/jphpi.v19i3.14540.

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Sport nutrition drinks are well-known in escalating athlete’s performance and endurance. These product developed from whey protein hydrolysates and soybean protein hydrolysates have already been recognized, however expansion from marine product is comparatively rare. Octopus (Octopus cyanea) widely acknowledged containing taurine and rich in amino acids is potential to be developed as ingredient for sport nutrition drink. The aims of this study were to create and characterize sport nutrition drinks based on marine peptides through Octopus protein hydrolyzate. Octopus protein hydrolysate has 77.78 ± 2.69% degree of hydrolysis and 751.02 ± 10.63 mg / 100g taurine. Sports nutrition drinks with the addition of 4% Octopus protein hydrolyzate was acceptable sensory panelists, and the serving size of 600 ml contained taurine 726.06 ± 0.82 mg and detected 17 types of amino acids.

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6

Riyanto, Bambang, Wini Trilaksani, and Rika Lestari. "Sport Nutrition Drinks Based on Octopus Protein Hydrolysate." Jurnal Pengolahan Hasil Perikanan Indonesia 19, no. 3 (February 6, 2017): 339. http://dx.doi.org/10.17844/jphpi.v19i3.15111.

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<p>Abstract<br />Sport nutrition drinks are well-known in escalating athlete’s performance and endurance. These product developed from whey protein hydrolysates and soybean protein hydrolysates have already been recognized, however expansion from marine product is comparatively rare. Octopus (Octopus cyanea) widely acknowledged containing taurine and rich in amino acids is potential to be developed as ingredient for sport nutrition drink. The aims of this study were to create and characterize sport nutrition drinks based on marine peptides through Octopus protein hydrolyzate. Octopus protein hydrolysate has 77.78±2.69% degree of hydrolysis and 751.02±10.63 mg / 100g taurine. Sports nutrition drinks with the addition of 4% Octopus protein hydrolyzate was acceptable sensory panelists, and the serving size of 600 ml contained taurine 726.06±0.82 mg and detected 17 types of amino acids.</p>

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7

Alberto Panizzolo, Luis. "Emulsifying Properties of Hydrolysates Isolated from Soybean Protein." International Journal of Nutrition and Food Sciences 4, no. 2 (2015): 223. http://dx.doi.org/10.11648/j.ijnfs.20150402.24.

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8

Qian, Fang, Ying Wang, Zi-jian Wen, Shu-juan Jiang, Yan-feng Tuo, and Guang-qing Mu. "Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates." Journal of Food Science and Technology 55, no. 3 (February 5, 2018): 1021–27. http://dx.doi.org/10.1007/s13197-017-3015-8.

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9

Iwaniak, Anna, Monika Hrynkiewicz, Piotr Minkiewicz, Justyna Bucholska, and Małgorzata Darewicz. "Soybean (Glycine max) Protein Hydrolysates as Sources of Peptide Bitter-Tasting Indicators: An Analysis Based on Hybrid and Fragmentomic Approaches." Applied Sciences 10, no. 7 (April 6, 2020): 2514. http://dx.doi.org/10.3390/app10072514.

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The aim of this study was to analyze soybean proteins as sources of peptides likely to be bitter using fragmentomic and hybrid approaches involving in silico and in vitro studies. The bitterness of peptides (called parent peptides) was theoretically estimated based on the presence of bitter-tasting motifs, particularly those defined as bitter-tasting indicators. They were selected based on previously published multilinear stepwise regression results. Bioinformatic-assisted analyses covered the hydrolysis of five major soybean-originating protein sequences using bromelain, ficin, papain, and proteinase K. Verification of the results in experimental conditions included soy protein concentrate (SPC) hydrolysis, RP-HPLC (for monitoring the proteolysis), and identification of peptides using RP-HPLC-MS/MS. Discrepancies between in silico and in vitro results were observed when identifying parent peptide SPC hydrolysate samples. However, both analyses revealed that conglycinins were the most abundant sources of parent peptides likely to taste bitter. The compatibility percentage of the in silico and in vitro results was 3%. Nine parent peptides with the following sequences were identified in SPC hydrolysates: LSVISPK, DVLVIPLG, LIVILNG, NPFLFG, ISSTIV, PQMIIV, PFPSIL, DDFFL, and FFEITPEK (indicators are in bold). The fragmentomic idea of research might provide a supportive method for predicting the bitterness of hydrolysates. However, this statement needs to be confirmed experimentally.

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10

Yi, Guofu, Jalal ud Din, Fen Zhao, and Xinqi Liu. "Effect of soybean peptides against hydrogen peroxide induced oxidative stress in HepG2 cells via Nrf2 signaling." Food & Function 11, no. 3 (2020): 2725–37. http://dx.doi.org/10.1039/c9fo01466g.

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11

Li, Li, Zuo-Yi Yang, Xiao-Qun Yang, Gui-He Zhang, Shu-Ze Tang, and Feng Chen. "Debittering effect of Actinomucor elegans peptidases on soybean protein hydrolysates." Journal of Industrial Microbiology & Biotechnology 35, no. 1 (October 18, 2007): 41–47. http://dx.doi.org/10.1007/s10295-007-0264-y.

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12

Lovšin-Kukman, I., M. Zelenik-Blatnik, and V. Abram. "Bitterness intensity of soybean protein hydrolysates—chemical and organoleptic characterization." Zeitschrift für Lebensmittel-Untersuchung und -Forschung 203, no. 3 (May 1996): 272–76. http://dx.doi.org/10.1007/bf01192877.

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13

Calzoni, Eleonora, Alessio Cesaretti, Silvia Tacchi, Silvia Caponi, Roberto Maria Pellegrino, Francesca Luzi, Francesco Cottone, Daniele Fioretto, Carla Emiliani, and Alessandro Di Michele. "Covalent Immobilization of Proteases on Polylactic Acid for Proteins Hydrolysis and Waste Biomass Protein Content Valorization." Catalysts 11, no. 2 (January 26, 2021): 167. http://dx.doi.org/10.3390/catal11020167.

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The recovery of the protein component and its transformation into protein hydrolysates, generally carried out chemically, gives great added value to waste biomasses. The production of protein hydrolysates through enzymatic catalysis would guarantee to lower the environmental impact of the process and raise product quality, due to the reproducible formation of low molecular weight peptides, with interesting and often unexplored biological activities. The immobilization of the enzymes represents a good choice in terms of stability, recyclability and reduction of costs. In this context, we covalently linked proteases from Aspergillus oryzae to polylactic acid an eco-friendly biopolymer. The hydrolytic efficiency of immobilized enzymes was assessed testing their stability to temperature and over time, and checking the hydrolysis of model biomasses (casein and bovine serum albumin). Soybean waste extracts were also used as proof of principle.

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14

Geng, Zhong Hua, En Qi Liu, Jian Ping Zhang, Shang Long Chen, Yong Li, and Yong Hua Wu. "Isolation and Identification of Antioxidant Peptides from Black Soybean Protein." Applied Mechanics and Materials 618 (August 2014): 298–302. http://dx.doi.org/10.4028/www.scientific.net/amm.618.298.

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The aim of this work was to isolate and identify antioxidant peptides from black soybean protein hydrolysates (BSH) by using the ultrafiltration (UF) and macroporous adsorption resin (MAR), and the fraction BSP-DA-c performed high antioxidant activity was further purified using consecutive methods on Sephadex G-25 column and reversed phase high-performance liquid chromatography (RH-HPLC). Two highly purified antioxidant peptides SBP3 and BSPb were got, and their amino acid sequences were confirmed as Trp-Asn-Pro and Tyr-Asn-Ile by automated Edman degradation with a protein sequencer, respectively.

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15

Velı́šek, J., K. Ledahudcová, B. Kassahun, M. Doležal, and V. Kubelka. "Chlorine-containing Compounds Derived from Saccharides in Protein Hydrolysates. II. Levulinic Acid Esters in Soybean Meal Hydrolysates." LWT - Food Science and Technology 26, no. 5 (October 1993): 430–33. http://dx.doi.org/10.1006/fstl.1993.1085.

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16

Zhao, Fei, Daofang Zhang, Xiangyang Li, and Haizhou Dong. "High-Pressure Homogenization Pretreatment before Enzymolysis of Soy Protein Isolate: the Effect of Pressure Level on Aggregation and Structural Conformations of the Protein." Molecules 23, no. 7 (July 19, 2018): 1775. http://dx.doi.org/10.3390/molecules23071775.

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The high-pressure homogenization (HPH) treatment of soybean protein isolate (SPI) before enzymatic hydrolysis using bromelain was investigated. Homogenization pressure and cycle effects were evaluated on the enzymatic degree of hydrolysis and the antioxidant activity of the hydrolysates generated. The antioxidant activity of SPI hydrolysates was analyzed by 1,1-dipheny-2-picrylhydrazyl (DPPH). The sizes and structures of the SPI-soluble aggregate after HPH treatment were analyzed using dynamic and static laser light scattering. The changes in the secondary structure, as measured by Fourier transform infrared spectroscopy (FTIR) and the macromorphology of SPI, were measured by scanning electron microscope (SEM). These results suggested that the HPH treatment (66.65%) could increase the antioxidant activities of the SPI hydrolysates compared with the control (54.18%). SPI hydrolysates treated at 20 MPa for four cycles obtained higher DPPH radical-scavenging activity than other samples. The control was predicted to be a hard sphere, and SPI treatment at 10 MPa was speculated to be Gaussian coil, polydisperse, and then the high-pressure treated SPI became a hollow sphere. Changes in the secondary structures showed protein aggregate formation and rearrangements. The image of SPI varied from a globular to a clump structure, as observed by the SEM. In conclusion, combining HPH treatment and enzymolysis could be an effective way to improve the antioxidant activity of the SPI.

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17

Hongfei, Zhao, Bai Fengling, Zhou Fang, Piotr Walczak, Jiang Xiangning, and Zhang Bolin. "Characterization of Soybean Protein Hydrolysates able to Promote the Proliferation ofStreptococcus ThermophilusST." Journal of Food Science 78, no. 4 (March 12, 2013): M575—M581. http://dx.doi.org/10.1111/1750-3841.12075.

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18

Yang, Rui Wen, Jia Wang, and Song Yi Lin. "Isolation and Purification of Soybean Antioxidant Peptides." Advanced Materials Research 881-883 (January 2014): 811–14. http://dx.doi.org/10.4028/www.scientific.net/amr.881-883.811.

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The soybean protein was hydrolyzed by Alcalase Food grade (FG) 2.4 L and the degree of hydrolysis (DH) were determined. The DH increased with the hydrolysis time increasing during 3.0 h. Then the hydrolysates was isolated by ultrafiltration membrane (1, 3, 10 kDa) and antioxidant activity was evaluated based on DPPH radical scavenging activity. The fraction of 1-3 kDa possessed the higher antioxidant activity than the other fractions (P < 0.05). Sephadex G-25 gel column was used to purify the three kinds of peptides and the eluted volume was investigated.

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19

Matemu, Athanasia, Soichiro Nakamura, and Shigeru Katayama. "Health Benefits of Antioxidative Peptides Derived from Legume Proteins with a High Amino Acid Score." Antioxidants 10, no. 2 (February 20, 2021): 316. http://dx.doi.org/10.3390/antiox10020316.

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Legumes such as soybean, chickpea, lentil, cowpea, and mung bean, are valuable sources of protein with a high amino acid score and can provide bioactive peptides. This manuscript presents a review on legume-derived peptides, focusing on in vitro and in vivo studies on the potential antioxidative activities of protein hydrolysates and their characterization, amino acid sequences, or purified/novel peptides. The health implications of legume-derived antioxidative peptides in reducing the risks of cancer and cardiovascular diseases are linked with their potent action against oxidation and inflammation. The molecular weight profiles and amino acid sequences of purified and characterized legume-derived antioxidant peptides are not well established. Therefore, further exploration of legume protein hydrolysates is necessary for assessing the potential applications of antioxidant-derived peptides in the functional food industry.

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20

Wang, Huan, Xiaohong Tong, Yue Yuan, Xinhui Peng, Qiaozhi Zhang, Shuang Zhang, Changyuan Xie, et al. "Effect of Spray-Drying and Freeze-Drying on the Properties of Soybean Hydrolysates." Journal of Chemistry 2020 (January 20, 2020): 1–8. http://dx.doi.org/10.1155/2020/9201457.

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The use of enzyme-assisted aqueous extraction to extract soybean oil will produce soy protein hydrolysates (SPH) that have good antioxidant properties but are bitter and hygroscopic. To microencapsulate these hydrolysates, soy protein isolate/maltodextrin mixtures were used as the carrier. The effects of spray-drying and freeze-drying on the bitterness, hygroscopicity, and antioxidant properties were compared. The properties of different dried samples were compared using solubility, hygroscopicity, moisture content, water activity, flowability, and glass transition temperature (Tg). The results showed that the spray-drying was more effective than freeze-drying. Hygroscopicity was reduced to 18.2 g/100 g, and the Tg value was raised to 80.8°C. The morphology was analyzed using scanning electron microscopy, and the antioxidant properties of the samples were measured using the ABTS˙+ radical scavenging activity. The results showed that spray-dried SPH had more carrier masking, which weakened bitterness, reduced moisture absorption, and had no significant negative impact on its oxidation resistance, solubility, and flowability, and spray-drying after carrier encapsulation of SPH improved the recovery rate.

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21

Lv, Ying, Shuntang Guo, and Baichong Yang. "Aggregation of hydrophobic soybean protein hydrolysates: Changes in molecular weight distribution during storage." LWT - Food Science and Technology 42, no. 4 (May 2009): 914–17. http://dx.doi.org/10.1016/j.lwt.2008.11.006.

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22

Song, Peng, Lei Cheng, Kangming Tian, Meng Zhang, Suren Singh, Dandan Niu, Bernard Prior, Nokuthula Peace Mchunu, and Zheng-Xiang Wang. "A novel aminopeptidase with potential debittering properties in casein and soybean protein hydrolysates." Food Science and Biotechnology 29, no. 11 (September 16, 2020): 1491–99. http://dx.doi.org/10.1007/s10068-020-00813-8.

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23

Chen, Chong, Dongxiao Sun-Waterhouse, Jie Zhao, Mouming Zhao, Geoffrey I. N. Waterhouse, and Weizheng Sun. "Soybean protein isolate hydrolysates-liposomes interactions under oxidation: Mechanistic insights into system stability." Food Hydrocolloids 112 (March 2021): 106336. http://dx.doi.org/10.1016/j.foodhyd.2020.106336.

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24

Ham, Kyung-Sik, Peter Albersheim, and Alan G. Darvill. "Generation of β-glucan elicitors by plant enzymes and inhibition of the enzymes by a fungal protein." Canadian Journal of Botany 73, S1 (December 31, 1995): 1100–1103. http://dx.doi.org/10.1139/b95-364.

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The biosynthesis and accumulation of phytoalexins is a well-studied plant defense response. Plants synthesize and accumulate phytoalexins in response to microbial infection or elicitor treatment. The β-glucan heptaglucoside is a well-studied phytoalexin elicitor isolated from partial acid hydrolysates of Phytophthora sojae f.sp. glycines (Psg) mycelial walls. Using the soybean – Psg system, we have demonstrated that endo-1,3-β-glucanases (EC 3.2.1.39) are the principal soybean enzymes involved in generating phytoalexin oligoglucoside elicitors from mycelial walls. We have also recently observed that Psg secretes a protein that inhibits the soybean endo-1,3-β-glucanase activity that could release elicitors from fungal mycelial walls. This inhibitor protein, which has been purified to homogeneity, does not inhibit endo-1,3-β-glucanases of the fungus or a tobacco pathogenesis-related endo-1,3-β-glucanase. The existence of the inhibitor protein in Psg suggests that pathogens have evolved specific proteins to inhibit the fungal wall-degrading enzymes of their host plants, just as plants have evolved proteins (e.g., pectic enzyme inhibitors) to inhibit plant cell wall degrading enzymes secreted by their pathogens. It seems possible that pathogens secrete inhibitors of other pathogenesis-related proteins (e.g., chitinases) and that the interplay of hydrolases and their inhibitors could determine the outcome of plant – pathogen interactions. Key words: oligosaccharin, phytoalexin, endo-1,3-β-glucanase, glucanase inhibitor protein, elicitor.

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25

KANG, Hyeog, Seung Gwan LEE, and Young Dong CHO. "Identification of glycinin in vivo as a polyamine-conjugated protein via a γ-glutamyl linkage." Biochemical Journal 332, no. 2 (June 1, 1998): 467–73. http://dx.doi.org/10.1042/bj3320467.

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To identify a polyamine-conjugated protein by the action of transglutaminase in the absence of radiolabelled polyamine, extracts prepared from the leaves and developing soybean seeds were investigated for the specific activity of transglutaminase and the content of free polyamines. We identified the major storage protein, glycinin, as a polyamine-conjugated protein. This was established by the following procedures: (1) immunolocalization with antibody against putrescine prepared in rabbit against putrescine–BSA conjugate; (2) immunocross-reactivity on nitrocellulose transblot of the purified glycinin subunits by using antibody against putrescine; (3) identification of polyamines in acid hydrolysates of purified glycinin; (4) release of polyamines in proteolytic digests through the catalytic action of γ-glutamylamine cyclotransferase, an enzyme specific for the disassembly of γ-glutamylamines. The activity of γ-glutamylamine cyclotransferase was also identified in soybean seeds.

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26

Lv, Ying, Qi Liu, Xiaolan Bao, Wuxia Tang, Baichong Yang, and Shuntang Guo. "Identification and Characteristics of Iron-Chelating Peptides from Soybean Protein Hydrolysates Using IMAC-Fe3+." Journal of Agricultural and Food Chemistry 57, no. 11 (June 10, 2009): 4593–97. http://dx.doi.org/10.1021/jf9000204.

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27

Martinez-Villaluenga, Cristina, Vermont P. Dia, Mark Berhow, Neal A. Bringe, and Elvira Gonzalez de Mejia. "Protein hydrolysates from β-conglycinin enriched soybean genotypes inhibit lipid accumulation and inflammationin vitro." Molecular Nutrition & Food Research 53, no. 8 (August 2009): 1007–18. http://dx.doi.org/10.1002/mnfr.200800473.

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28

Kodera, Tomohiro, Minao Asano, and Noriki Nio. "Characteristic Property of Low Bitterness in Protein Hydrolysates by a Novel Soybean Protease D3." Journal of Food Science 71, no. 9 (November 2006): S609—S614. http://dx.doi.org/10.1111/j.1750-3841.2006.00179.x.

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29

Bao, X. L., Y. Lv, B. C. Yang, C. G. Ren, and S. T. Guo. "A Study of the Soluble Complexes Formed during Calcium Binding by Soybean Protein Hydrolysates." Journal of Food Science 73, no. 3 (February 28, 2008): C117—C121. http://dx.doi.org/10.1111/j.1750-3841.2008.00673.x.

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30

Fu, Jing, Li Li, and Xiao-Quan Yang. "Specificity of Carboxypeptidases from Actinomucor elegans and Their Debittering Effect on Soybean Protein Hydrolysates." Applied Biochemistry and Biotechnology 165, no. 5-6 (August 20, 2011): 1201–10. http://dx.doi.org/10.1007/s12010-011-9338-4.

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31

González-Espinosa de los Monteros, L. A., E. Ramón-Gallegos, N. Torres-Torres, and R. Mora-Escobedo. "Effect of Germinated Soybean Protein Hydrolysates on Adipogenesis and Adipolysis in 3T3-L1 Cells." Plant Foods for Human Nutrition 66, no. 4 (November 2011): 355–62. http://dx.doi.org/10.1007/s11130-011-0263-z.

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32

Reyes-Díaz, Aline, Carmen Lizette Del-Toro-Sánchez, José Carlos Rodríguez-Figueroa, Santiago Valdéz-Hurtado, Francisco Javier Wong-Corral, Jesús Borboa-Flores, María Fernanda González-Osuna, Liliana Maribel Perez-Perez, and Ricardo Iván González-Vega. "Legume Proteins as a Promising Source of Anti-Inflammatory Peptides." Current Protein & Peptide Science 20, no. 12 (December 16, 2019): 1204–17. http://dx.doi.org/10.2174/1389203720666190430110647.

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Legume proteins are precursors of bioactive components, such as peptides. In the present paper, different types of legume as sources of bioactive peptides and hydrolysates are considered and discussed based on their anti-inflammatory effect. Peptides with anti-inflammatory activity were included from in vitro and in vivo studies. Current strategies for obtaining bioactive peptides, as well as their structure and impact on health, were also reviewed. It was discovered that peptides derived from legume protein, mainly soybean and bean, can regulate several inflammatory markers, which include prostaglandin E2 (PGE2), nitric oxide (NO), inducible nitric oxide synthase (iNOS), cyclooxygenase 2 (COX- 2), cytokines, and chemokines. So far, lunasin, VPY and γ-glutamyl peptides have been identified with anti-inflammatory activity but their mechanisms have not been fully elucidated. Furthermore, it is necessary to gather more information about hydrolysates containing peptides and single peptides with antiinflammatory activity. Considering the wide diversity, legume may be promising components to produce peptides efficient to ameliorate inflammatory disorders.

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33

Li, Lin, Hui He, Daize Wu, Derong Lin, Wen Qin, Demei Meng, Rui Yang, and Qing Zhang. "Rheological and textural properties of acid-induced soybean protein isolate gel in the presence of soybean protein isolate hydrolysates or their glycosylated products." Food Chemistry 360 (October 2021): 129991. http://dx.doi.org/10.1016/j.foodchem.2021.129991.

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34

Zhao, Fei, Xuemei Liu, Xiuzhen Ding, Haizhou Dong, and Wentao Wang. "Effects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Soy Protein Isolate." Molecules 24, no. 20 (October 9, 2019): 3637. http://dx.doi.org/10.3390/molecules24203637.

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The objective of this study was to investigate the effects of different high-intensity ultrasonication (HIU) pretreatment on the structure and properties of soybean protein isolate (SPI) as well as enzymatic hydrolysis of SPI by bromelain and antioxidant activity of hydrolysates. The HIU-treated SPI fractions showed a decrease in the proportion of α-helices and β-turns and an increase in the content of β-sheets and random coils based on Fourier-transform infrared spectroscopy. Near-infrared spectra and fluorescence spectra analyses provided support for the changes in secondary and tertiary structures of SPI after ultrasound treatment. The particle size of SPI decreased from 217.20 nm to 141.23 nm and the absolute zeta potential increased. Scanning electron microscopy showed that HIU treatment changed apparent morphology. Dynamic and static light scattering of ultrasonicated samples showed that SPI structure had changed from hard-sphere to hollow-sphere or polydisperse and monodisperse gaussian coils. HIU pretreatment significantly increased the hydroxyl-radical scavenging and the degree of hydrolysis of the SPI hydrolysates.

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Wu, Yong Hua, En Qi Liu, Jian Ping Zhang, Shang Long Chen, Yong Li, and Zhong Hua Geng. "In Vivo Antioxidant Activity of Black Soybean Peptide in Aging Mice Caused by D-Galactose." Applied Mechanics and Materials 618 (August 2014): 421–25. http://dx.doi.org/10.4028/www.scientific.net/amm.618.421.

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Black soybean peptides (BSPs) with potent antioxidant activity were purified from black soybean protein hydrolysates (BSH) by using the ultrafiltration (UF) and macroporous adsorption resin (MAR), andin vivoantioxidant activity of the fraction BSP-DA-c was evaluated in aging mice induced byD-galactose. The results showed that orally administration of BSP-DA-c fraction at the dose of 500 and 1000 mg/kg per day could remarkably increase (P<0.05) the activity of SOD and GSH-Px in liver and the activity of GSH-Px in serum, the contents of MDA in serum and liver were reduced significantly (P<0.05), inferred that BSP-DA-c had strong antioxidant activity in mice.

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36

Sitanggang, Azis Boing, Jessica Eka Putri, Nurheni Sri Palupi, Emmanuel Hatzakis, Elvira Syamsir, and Slamet Budijanto. "Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review." Molecules 26, no. 13 (June 23, 2021): 3822. http://dx.doi.org/10.3390/molecules26133822.

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The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from Aspergillus sp.), a temperature of 37 °C, a reaction time of 18 h, pH 8.2, and an E/S ratio of 2%. On the other hand, the best enzymatic conditions for producing peptide hydrolysates with high ACEi activity are through sequential hydrolytic activity by the combination of pepsin-pancreatic, an E/S ratio for each enzyme is 10%, the temperature and reaction time for each proteolysis are 37 °C and 0.74 h, respectively, pH for pepsin is 2.0, whereas for pancreatin it is 7.0. As an underutilized pulse, the studies on the enzymatic hydrolysis of velvet bean proteins in producing ACEi peptides are limited. Conclusively, the activity of soybean-based ACEi peptides is found to depend on their molecular sizes, the amino acid residues, and positions. Hydrophobic amino acids with nonpolar side chains, positively charged, branched, and cyclic or aromatic residues are generally preferred for ACEi peptides.

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Lee, Yong Kwon, Seung Yeul Kim, Ki Heon Kim, Bok-Hwan Chun, Kweon-Haeng Lee, Duk Jae Oh, and Namhyun Chung. "Use of soybean protein hydrolysates for promoting proliferation of human keratinocytes in serum-free medium." Biotechnology Letters 30, no. 11 (July 9, 2008): 1931–36. http://dx.doi.org/10.1007/s10529-008-9796-0.

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38

Liddle, R. A., G. M. Green, C. K. Conrad, and J. A. Williams. "Proteins but not amino acids, carbohydrates, or fats stimulate cholecystokinin secretion in the rat." American Journal of Physiology-Gastrointestinal and Liver Physiology 251, no. 2 (August 1, 1986): G243—G248. http://dx.doi.org/10.1152/ajpgi.1986.251.2.g243.

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Because of prior difficulties in measuring plasma cholecystokinin (CCK) levels, it has not been established which components of food stimulate CCK secretion in rats. In the present study, we used a sensitive and specific bioassay for measuring plasma CCK and determined the effects of proteins, protein hydrolysates, amino acids, fats, starch, and glucose on CCK secretion in this species. Intact proteins were the only stimulants of CCK release. Solutions of 18% casein and 0.2% soybean trypsin inhibitor caused prompt increases in plasma CCK levels from 0.5 +/- 0.2 to 7.9 +/- 1.9 and 8.0 +/- 2.0 pM, respectively, within 5 min of orogastric administration. The proteins lactalbumin and bovine serum albumin caused smaller elevations in circulating CCK. In contrast, hydrolysates of casein and lactalbumin and the amino acids L-phenylalanine and L-tryptophan did not stimulate CCK release. In addition, plasma CCK levels did not increase with the feeding of fat, starch, or glucose. The ability of proteins to stimulate CCK secretion paralleled their ability to inhibit trypsin activity in vitro. Furthermore, the plasma CCK response to casein was completely abolished by the simultaneous administration of trypsin. These studies indicate that proteins are the major food stimulants of CCK release in the rat and that the effects of proteins are related to inhibition of intraluminal protease activity.

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Li, Xinxiu, Peihong Fan, Meitong Zang, and Jie Xing. "Rapid Determination of Oligopeptides and Amino Acids in Soybean Protein Hydrolysates using High-Resolution Mass Spectrometry." Phytochemical Analysis 26, no. 1 (July 7, 2014): 15–22. http://dx.doi.org/10.1002/pca.2531.

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Lv, Ying, He Liu, Jianhua Ren, Xin Li, and Shuntang Guo. "The positive effect of soybean protein hydrolysates—calcium complexes on bone mass of rapidly growing rats." Food & Function 4, no. 8 (2013): 1245. http://dx.doi.org/10.1039/c3fo30284a.

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41

Salgado, Pablo R., Graciela B. Fernández, Silvina R. Drago, and Adriana N. Mauri. "Addition of bovine plasma hydrolysates improves the antioxidant properties of soybean and sunflower protein-based films." Food Hydrocolloids 25, no. 6 (August 2011): 1433–40. http://dx.doi.org/10.1016/j.foodhyd.2011.02.003.

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Lv, Ying, Xiaolan Bao, He Liu, Jianhua Ren, and Shuntang Guo. "Purification and characterization of caclium-binding soybean protein hydrolysates by Ca2+/Fe3+ immobilized metal affinity chromatography (IMAC)." Food Chemistry 141, no. 3 (December 2013): 1645–50. http://dx.doi.org/10.1016/j.foodchem.2013.04.113.

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43

Cui, Chun, Mouming Zhao, Boen Yuan, Yuanhong Zhang, and Jiaoyan Ren. "Effect of pH and Pepsin Limited Hydrolysis on the Structure and Functional Properties of Soybean Protein Hydrolysates." Journal of Food Science 78, no. 12 (November 26, 2013): C1871—C1877. http://dx.doi.org/10.1111/1750-3841.12309.

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44

Farzamirad, Vahid, and >Rotimi E. Aluko. "Angiotensin-converting enzyme inhibition and free-radical scavenging properties of cationic peptides derived from soybean protein hydrolysates." International Journal of Food Sciences and Nutrition 59, no. 5 (January 2008): 428–37. http://dx.doi.org/10.1080/09637480701592897.

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Darmawan, Rudy, Neal A. Bringe, and Elvira Gonzalez de Mejia. "Antioxidant Capacity of Alcalase Hydrolysates and Protein Profiles of Two Conventional and Seven Low Glycinin Soybean Cultivars." Plant Foods for Human Nutrition 65, no. 3 (September 2010): 233–40. http://dx.doi.org/10.1007/s11130-010-0185-1.

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Song, Na, Chen Tan, Meigui Huang, Ping Liu, Karangwa Eric, Xiaoming Zhang, Shuqin Xia, and Chengsheng Jia. "Transglutaminase cross-linking effect on sensory characteristics and antioxidant activities of Maillard reaction products from soybean protein hydrolysates." Food Chemistry 136, no. 1 (January 2013): 144–51. http://dx.doi.org/10.1016/j.foodchem.2012.07.100.

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Liu, H., X. L. Bao, Y. Lv, J. T. Xu, and S. T. Guo. "Separation and Evaluation of Soybean Protein Hydrolysates Prepared by Immobilized Metal Ion Affinity Chromatography with Different Metal Ions." Journal of Chromatographic Science 50, no. 8 (May 25, 2012): 714–20. http://dx.doi.org/10.1093/chromsci/bms071.

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Mora-Escobedo, R., Maria del Carmen Robles-Ramírez, Eva Ramón-Gallegos, and Rafael Reza-Alemán. "Effect of Protein Hydrolysates from Germinated Soybean on Cancerous Cells of the Human Cervix: An In Vitro Study." Plant Foods for Human Nutrition 64, no. 4 (August 18, 2009): 271–78. http://dx.doi.org/10.1007/s11130-009-0131-2.

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Kukman, I. Lovs̄in, M. Zelenik-Blatnik, and V. Abram. "Isolation of low-molecular-mass hydrophobic bitter peptides in soybean protein hydrolysates by reversed-phase high-performance liquid chromatography." Journal of Chromatography A 704, no. 1 (June 1995): 113–20. http://dx.doi.org/10.1016/0021-9673(95)00014-e.

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50

Hara, Hiroshi, Takuji Suzuki, Kei-ichi Tamura, Hiroshi Narakino, and Shuhachi Kiriyama. "Differential digestibility of a synthetic slowly digestible peptide, oligo-L-methionine, in rats fed soybean protein or its hydrolysates." Journal of Nutritional Biochemistry 6, no. 1 (January 1995): 38–42. http://dx.doi.org/10.1016/0955-2863(94)00006-8.

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