Soybeans are rich in proteins and phytochemicals such as isoflavones and phenolic compounds. It is an excellent source of peptides with numerous biological functions, including anti-inflammatory, anticancer, and antidiabetic activities. Soy bioactive peptides are small building blocks of proteins that are released after fermentation or gastrointestinal digestion as well as by food processing through enzymatic hydrolysis, often in combination with novel food processing techniques (i.e., microwave, ultrasound, and high-pressure homogenization), which are associated with numerous health benefits. Various studies have reported the potential health benefits of soybean-derived functional peptides, which have made them a great substitute for many chemical-based functional elements in foods and pharmaceutical products for a healthy lifestyle. This review provides unprecedented and up-to-date insights into the role of soybean peptides in various diseases and metabolic disorders, ranging from diabetes and hypertension to neurodegenerative disorders and viral infections with mechanisms were discussed. In addition, we discuss all the known techniques, including conventional and emerging approaches, for the prediction of active soybean peptides. Finally, real-life applications of soybean peptides as functional entities in food and pharmaceutical products are discussed.
Soybean (Glycine max) is a legume of the family Fabaceae (Leguminosae), which originated ~5,000 years ago in East Asia. Currently, the USA, Brazil, and Argentina account for ~34, 30, and 17% of the global soybean production, respectively. China, Japan, Mexico, and many European countries are the main soybean-importing countries, and their export products are oil, meal, and seed, which account for 80% of their known export value (1). Standard soybean seeds with 13% of moisture comprise 19% oil and 68% meal fractions (2, 3). polyglyceryl 10 stearate
Soybean is a potent source of vegetable proteins and phytochemicals, such as isoflavones and phenolic compounds, because of its amino acid composition, high availability, and low cost, making it the second largest source of vegetable oil globally (4, 5). It consists of protein (30–35%), lipids (20%), dietary fiber (9%), and moisture (8.5%) based on the dry weight of soybean seeds (6). Various environmental conditions and genetic modifications affect the soybean protein composition which has an influence on soybean health-promoting properties for the production of functional soybean-based products (7). Albumins and globulins are the two main proteins in soybean, and the latter is considered the main protein component of soybeans. The two major storage proteins of soybean are β-conglycinin (βCG, 7S) and glycinin (11S), which account for 80–90% of the total protein in soybean (8–10). Soybean dietary proteins have been shown to have health benefits owing to their therapeutic nature as a result of the presence of functional peptides (11, 12). Functional motifs of a protein are termed peptides. Soybean-derived peptides have gained considerable interest because of their potential health benefits associated with metabolism, brain function, and cognitive ability, as well as their immunomodulatory, antioxidative, antithrombotic, anti-inflammatory, antihypertensive, antidiabetic, antiviral, and mineral-binding roles (13–17).
Soybean-derived peptides are also known to attenuate the severity of metabolic and age-related chronic disorders, such as cancer, hypocholesterolemia, obesity, and alcohol-induced liver injury (18–20). Several peptides derived from soybeans have been reported to exert multiple benefits and are termed multifunctional soybean peptides. Lunasin (5.5 kDa molecular weight), comprising 43 amino acids, is a multifunctional soybean peptide (21). This peptide has been reported to ameliorate several chronic diseases and metabolic conditions including cancer, hypertension, oxidative stress, and inflammation (22, 23). It is often utilized as a dietary supplement because of its high availability and heat stability.
Apart from the plethora of functional peptides in soybeans, isoflavones are also present as glycosides (24). They can lower the risk of oxidative damage to DNA and low-density lipoprotein (LDL) by free radical stress and increase the antioxidant function of enzymes that play a role in the defense system of the human body. They can bind to reactive oxidative species, improve glutathione production, and vitamins E and C, which also work effectively as antioxidants (25, 26). Moreover, these isoflavones can decrease cancer promoters that produce oxidative stress, such as xanthine and tetradecanoylphorbol-13-acetate (TPA) (27). Isoflavones are reported to act as potential antidepressants (28). Genistein is a widely existing and well-known isoflavone, which is associated with a decreased risk of various diseases that are linked to humans, such as tumors, by the enzymatic intervention (29). Genistein has been shown to be helpful in the regulation of gene transcription through DNA methylation and histone modification (30).
Soybeans are known to be a complete protein because they contain all the five key amino acids required for proper nutrition. The traditional methods of acquiring these peptides include the following techniques: (i) hydrolytic activities of enzymes (e.g., trypsin, pepsin, and papain) (31), (ii) microbial fermentation by Lactobacillus and yeast (32, 33), (iii) combined enzymatic and microbial treatment (34), and (iv) food processing by high pressure and enzymatic hydrolysis (35). Enzymatic hydrolysis is the most convenient and common method because of its high stability and production of many other useful molecules during fermentation, such as surfactants, bacteriocins, polysaccharides, amino acids, vitamins, and many other biomolecules (36). Lactic acid fermentation has proven to be the best method for bioactive peptide production and protein hydrolysis in soybean (37). Soybean fermentation causes the hydrolysis of soybean protein into specific bioactive peptides (38). The latest research trend is to predict functional peptides in different types of vegetable proteins using emerging techniques, such as machine learning algorithms, and to predict the potential of several peptides (39, 40).
The commercial use of soy protein in several food products is currently very popular, particularly in protein-based meat products for vegetarians (4). Figure 1 shows a general depiction of soybean-derived peptides in food products and their functional benefits.
Figure 1. Functional applications of soybean-derived peptides.
However, the application of soybean peptides to food and feed still faces several challenges that hinder their effective use. The purpose of this review article is to provide recent updates on the functional and biological potential of soybean peptides and discuss conventional and emerging techniques to release these peptides from soybean. Finally, we discuss the practical applications of soybean peptides as functional ingredients in food and feed.
Many soybean components have shown biological activity, including but not limited to proteins, peptides, saponins, and isoflavones (41). Soybean peptides have received special attention because of their huge diversity and associated biological potential. Several studies have revealed its anti-atherosclerotic, anticancer, antioxidative, anti-inflammatory, antiviral, antidiabetic, anti-inflammatory, and cardioprotective effects (Table 1).
Table 1. Health benefits of soybean-derived peptides.
Beyond its high nutritional value, soybean contains a large variety of useful substances, such as bioactive peptides. When soybean proteins break down, peptide pieces hidden inside their core assemblies are released. These peptide fragments exhibit a wide range of biological and functional properties. These peptides are produced from glycinin and beta-conglycinin (which includes three subunits, such as alpha, α′, and beta), the progenitors of the majority of isolated peptides (82). Fatty acid (FA) synthase (FAS) inhibition, triglyceride and cholesterol reduction, effectiveness against obesity and diabetes, and lipid metabolism enhancement are properties attributed to soybean peptides (83). Some studies have shown that soybean peptides have many functions, including hypocholesterolemia, outcomes against cancer, angiotensin-converting enzyme (ACE), hypertension, and regulation of the immune system, while additional uses and benefits are constantly being uncovered (84, 85). Immunomodulatory peptides belong to a complex class of biologically active peptides that contain substances with various mechanisms of action. Several studies have shown that soybean peptides exert immunoregulatory effects (Table 1). For instance, in the macrophage cell lines RAW 264.7 and THP-1 (86), lunasin displayed anti-inflammatory effects by reducing the generation of cyclooxygenase-2 (COX-2), E2 (PGE2), and nitric oxide (NO), as well as the expression of inducible NO synthase (iNOS). Additionally, interleukin-6 and interleukin-1 production was suppressed by lunasin, and its anti-inflammatory effects were linked to the repression of the NF-κB pathway. The ability of lunasin to inhibit integrins is likely responsible for its anti-inflammatory effects. The complete sequence is important for the anti-inflammatory benefits of lunasin fragments (21, 87). According to some studies, lunasin can reduce the production of tumor necrosis factor-alpha (TNF-α) which has anti-inflammatory effects. Lunasin demonstrates immunomodulatory activity against cancer by interacting with the cytokine's interleukin-2 (IL-2) and interleukin-12 (IL-12). This blend activates cells called natural killer (NK) cells to increase interferon-gamma (IFN-γ) production. Granzyme B (GZMB) and granulocyte-macrophage colony-stimulating factor (CSF2) expression were both elevated by a combination of lunasin/IL-2/IL-12, although transforming growth factor beta receptor 2 (TGFBR2) and transforming growth factor beta 1 (TGFB1) expression were decreased (88). As a result, the ability of lunasin to modulate gene expression is associated with its immunomodulatory properties. The combination of lunasin and IL-12 significantly increased H3 acetylation at the interferon gamma (IFNG) locus and decreased it at the TGFB1 locus, indicating an epigenetic mechanism (18). A peptide without either the RGD motif or the aspartic acid (D)-tail, however, had an impact comparable to that of full-length lunasin, indicating that they were not linked to a synergistic augmentation of IFN production. Therefore, the N-terminus and/or central regions of lunasin are linked to the immunomodulatory function of the compound. The reduction in cholesterol levels is attributed to lactostatin, which is β-lactoglobulin (IIAEK), which regulates these levels by controlling the channels of the calcium-associated signaling pathway of MAPK. Cholesterol 7α-hydroxylase (CYP7A1) is the limiting enzyme involved in the degradation of cholesterol and cells of HepG2, mediating transactivation, which is induced by lactostatin. The activity of this enzyme is controlled by calcium channels and the extracellular signal-regulated kinase (ERK) pathway (60). Various peptides have been shown to play important roles in lowering cholesterol and lipid content (Table 1). Glycinin hydrolysis with trypsin and pepsin revealed two peptides that were converted into IAVPTGVA (Soy1) and LPYP peptides, which were shown to be absorbed by Caco-2 cells (89). They either act as hypocholesterolemic or hypoglycemic agents and can inhibit HMGCoA reductase and stimulate the LDL receptor pathway, which, in turn, reduces cholesterol. Additionally, there was an increase in the intensity of phosphorylation on Ser 872 of HMGCoA reductase, which is the operative form of HMGCoA reductase, through the stimulation of the adenosine monophosphate-activated protein kinase (AMPK) pathway. Stimulation of AMPK and Akt/protein kinase B pathways is linked to the ability to regulate glucose metabolism and uptake (89). Inhibition of glycogen synthase (GS) and glycogen synthase kinase-3β (GSK3) is caused by the activation of Akt (phosphorylation at Ser 473), which further controls the activity of GS by modifying glycogen formation in hepatic cells. In addition, the upregulation effect of hepatocytes on extracellular free glucose is also determined by the expression level of glucose transporter type 1 (GLUT1) and glucose transporter 4 (GLUT4).
Superoxide anions (O2−), hydrogen peroxide (H2O2), and hydroxyl radicals are examples of reactive oxygen species (ROS) that are essential for everyday bodily functions (OH). However, when ROS accumulates beyond the capacity of the cellular antioxidant defense system, metabolic disorders such as cardiovascular disease, Alzheimer's disease, type 2 diabetes (T2D), and certain types of cancer may develop (90, 91). Additionally, ROS are produced chemically or enzymatically in food systems, and their interactions with dietary ingredients result in unfavorable tastes and carcinogens. Therefore, soy protein hydrolysates and constitutive peptides have been employed to prevent food systems from degrading due to ROS and to shield the human body from harmful effects. The fraction with the lowest molecular weight (SPH-I, MW3 kDa) demonstrated the strongest radical scavenging ability and reducing power as well as the best potency in controlling H2O2-induced oxidative stress in Caco-2 cells (92). It would be interesting to isolate bioactive peptides with cytoprotective and antioxidant properties. These peptides also greatly reduced lipid peroxidation and intracellular ROS formation, which protected Caco-2 cells from H2O2-induced oxidative damage (p < 0.05). Furthermore, SPH-IC and SPH-ID significantly increased the ROS-mediated response to inflammation by preventing interleukin-8 release (p > 0.05) (80). The amino acid makeup of lunasin has been linked to its antioxidant action. In a study, lunasin was shown to decrease lipid peroxidation, shown 2, 2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) radical scavenging activity (ABTS•+), and prevent the production of ROS caused by lipopolysaccharide. After scavenging peroxyl and superoxide radicals, chelating ferrous ions, and reducing intracellular ROS levels, the antioxidant activity of lunasin was further proven (90, 93). According to Fernández-Tomé et al. (94), under oxidative stress, lunasin inhibits an increase in the activity of glutathione peroxidase and catalase, lowers intracellular ROS and protein carbonyl levels, and increases cytosolic glutathione levels. In some experiments, the inhibition of dipeptidyl peptidase-IV (DPP-IV) activity by Soy1 and LPYP is a favorable outcome for the prevention of diabetes (95). Using BIOPEP, an initial examination of their structures indicated that angiotensin-converting enzymes might be potent inhibitors. Consequently, a bottom-side-up approach was established to clarify hypotensive activity in vitro. Similarly, in another study using molecular modeling, their capacity to act as inhibitors was competitive with this enzyme (51). Production of low insulin or resistance to insulin causes dysregulation of the glucose balance which results in T2D. To manage T2D, a considerable focus is on natural remedies, especially food elements. DPP-IV, alpha-amylase, and alpha-glucosidase are essential for controlling blood glucose levels. It is believed that the suppression of these enzymes by bioactive peptides could be the most efficient method for managing T2D. The peptides obtained from food are being focused on as novel inhibitors because DPP-IV, which is present in the cell membrane and blood, is responsible for the inhibition of incretin hormones, such as stomach inhibitory polypeptide and glucagon-like peptide-1 (72). For the efficient control of T2D and other metabolic disorders, the inhibitory peptide DPP-IV (IAVPTGVA) obtained from soybean may be utilized.
Small protein fragments known as soy peptides are produced through enzymatic hydrolysis in vitro, fermentation (such as fermentation caused by bacteria containing lactic acid), processing of food such as modification of pH, heat treatment, isolation of protein, processing through ultra-high-pressure (96, 97), and GI digestion (specific and non-specific proteases from the pancreas, small intestine, and stomach, including pepsin, trypsin, and chymotrypsin). Table 2 shows the different methods used to produce soybean peptides. Soy protein also affects peptide composition through enzymatic hydrolysis or bacteria-mediated fermentation (6). Diverse functional features of soy peptides with various compositions have also been noted when producing tofu in terms of quality, yield, and texture (109). The digestion of food in the digestive tract can also produce peptides. Proteins are hydrolyzed by digestive enzymes, resulting in peptides of various lengths and free amino acids. Pepsin acts at the stomach level in in vitro systems, randomly hydrolyzing peptide bonds to create relatively large peptides and a mixture of acids from the pancreas and pancreatins. Trypsin, chymotrypsin, elastase, and carboxypeptidases are the only peptidases that constitute pancreatins. Except for trypsin, all enzymes hydrolyze peptide bonds, resulting in peptides with various amino acid sequences (110).
Table 2. Various methods for soybean-based peptide generation.
Chemical-based techniques and fermentation with microbes are the conventional methods used for hydrolyzing soybean peptides. There are a few examples of the chemical-based approaches mentioned above (Table 2). Advanced fermentation methods (fungus, yeast, or germ) and enzymatic treatments are two examples of processing technology (111). In addition to physical techniques, recent studies have highlighted the significance of enzymatic hydrolysis. Peptides, considered biowaste, are obtained from sources of protein by hydrolysis through enzymes and have been used as an assuring method. It has been reported that a meal of soybean contains two soybean lines that are high in oleic acid and one high-protein line when utilized from peptides are bioactive and are effective against cancer cells at multiple sites. GI enzymes and alcalase are used to resist GI to obtain fractions of soy peptides (75).
A viscozyme multi-enzyme complex was employed by de Figueiredo et al. (112) to pretreat okara (soybean waste product), which enhanced the conventional alkaline preparation procedure and increased the protein extraction rate. The major goal of this study was to suggest three techniques for producing low-molecular-weight peptides from okara. High-pressure homogenization and mixed enzyme hydrolysis were followed by alkaline protease hydrolysis and the alkali-dissolved acid precipitation method for alkaline protease hydrolysis and protein extraction, respectively. The findings of this study were an increase in the added value of okara and the production of biologically active peptides from soybean waste. In another study, a method for producing low-molecular-weight peptides (HPH-VAP) from okara was proposed using high-pressure homogenization-assisted double enzymes. To compare the effects of the various procedures, the rates of protein extraction, peptide structure, antioxidant capacity, and immunological characteristics were evaluated. The results demonstrated that the protein extraction rate of this method increased by 69 and 51%, compared to earlier methods. The results showed that it increased NO levels, cytokine production, and cell phagocytic capabilities (IL-6, IFN–γ, and TNF-α) (113).
This study evaluated the impact of fermentation on the nutritional value of food and food-grade soybeans. Both were fermented for 48 h by Aspergillus oryzae GB-107 in a bed-packed solid fermenter. After fermentation, nutritional and trypsin inhibitor levels were compared to those of soybean meal and raw soybeans. Compared to raw soybeans and soybean meals, fermented soybeans and soybean meals contained 10% higher crude protein (P < 0.05). The essential amino acid profile remained unchanged during the fermentation. Most trypsin inhibitors were removed by fermentation of both soybeans and soybean meal (P < 0.05). Although fermentation significantly reduced the number of large peptides (60 kDa) compared to raw soybeans, it significantly increased the number of small peptides (20 kDa) (P < 0.05). Fermented soybean meal contained more small peptides (20 kDa) than soybean meal (P < 0.01); however, soybean meal contained 22.1% larger peptides (60 kDa) than fermented soybean meal. In general, fermentation reduces the peptide size in soybeans and soybean meals, eliminates trypsin inhibitors, and increases protein content (108). The purpose of this study was to assess the bioactivities, such as galactosidase and glucosidase activities, and the growth behavior of Lactobacillus cultures in the soymilk medium. Among the 10 Lactobacillus cultures in the soymilk medium used in this study, L. casei (NK9) and L. fermentum (M2) were chosen because of their improved growth patterns and higher levels of glucosidase and galactosidase activities during fermentation. Additionally, soymilk fermented with M2 had stronger ACE-inhibitory (48.44%) proteolytic activity (0.67 OD) than NK9 (proteolytic activity: 0.48 OD and ACE-inhibitory activity:41.33%) (9). Using specific Lactobacillus cultures during the fermentation of soy milk, peptides were produced that were recognized by MALDI-TOF spectrometry as having effective ACE-inhibitory activity. Using the BIOPEP database, the identified ACE-inhibitory peptide arrangements from fermented soymilk were characterized (107).
IAVPTGVA (Soy1) and LPYP, two soybean peptides with multiple behavioral functions, have shown hypoglycemic and hypocholesterolemic effects in vitro. According to a preliminary structural screening conducted using BIOPEP, they may be significant ACE inhibitors. As a result, a bottom-up method was established to explain the in vitro hypotensive activity. With IC50 values of 14.7 ± 0.28 and 5.0 ± 0.28 M (Caco-2 cells) and 6.0 ± 0.35 and 6.8 ± 0.20 M (HK-2 cells), correspondingly, LPYP and Soy1 decreased the renal and intestine ACE enzyme activity. In addition, molecular modeling studies have suggested that they have the potential to function as competitive inhibitors of this enzyme. To improve stability and hypotensive qualities, a viable method for the non-toxic regulation of their release from a nanomaterial was devised by encapsulation into a RADA16-assembling peptide (51). AHTPs have been perceived in various organisms, and their anti-hypertensive activity in the laboratory for the identification of peptides is time- and resource-consuming. Before verification through experiments, computational techniques that comprise the stout learning of machines can recognize capable AHTPs. The research proposed Ensemble-AHTPpred, a collective learning of a machine-containing algorithm comprising maximum gradient boosting (XGB), a support vector machine (SVM), and a random forest (RF), to enhance the robustness of the final predictive model and incorporate various heterogeneous algorithms. To analyze or explain the characteristics of the predicted peptide, computed features such as transitions, n-grams, various physicochemical properties, secondary structure-related information, and amino acid composition (AACs) were used. Above 90%, was achieved on the liberated inspection data using the Ensemble-AHTPpred tool. Furthermore, based on the latest studies, the method was practical for innovative empirically authorized AHTPs that were not overlaid with the test and datasets that are based on training, and these AHTPs might specifically be predicted by the tool (119).
Soybean-derived peptides have gained great popularity as one of the most economical and easily accessible peptides, with a plethora of functional applications in the food, feed, and pharmaceutical industries. Thermal and gastrointestinal stability (including pH) are crucial parameters for the practical application of soybean peptides in food and feed (120). A study reported that the interfacial and emulsifying characteristics of soy peptides varied based on the degree of hydrolysis. A peptide with the lowest degree of hydrolysis was found to be an excellent functional agent for the emulsification of not only silicon oil and liquid paraffin but also soybean oil (121). Novel nanoparticles derived from soy peptides have shown great potential as oil–water emulsion stabilizers and effective food-grade emulsifiers, with the potential to replace surfactants and polymers (122). These studies indicate that soy peptides had previously unappreciated emulsifying activity and great interfacial properties, which make them useful for the food processing industry. Soy peptides have exceptional assimilating properties, and there is a need to determine whether the foaming properties of egg white powder can be enhanced by using soy peptides as foaming agents. There is some evidence that 9–12% of soy peptides at pH 7 improve the foaming properties of egg white powder by conferring it a more flexible secondary structure, uniform size, more surface hydrophobicity, and foam elasticity (123).
The effect of soybean-derived peptides on the quality attributes (physicochemical, sensory, and microbiological) of yogurt was evaluated under storage (3 weeks) conditions. The enzymatic hydrolysis of soy whey protein was performed using trypsin at 45°C for 4 h. Various concentrations of soy peptides (6.5, 13, and 17 mg/mL) were incorporated into yogurt. Increasing the peptide content enhanced antioxidant activity; however, viscosity and syneresis were reduced. During 3 weeks of storage, acidity (from 1.04 to 1.14%), syneresis (from 15.23 to 19.84%), and viscosity (from 5.31 to 8.04) of yogurt increased while pH (from 4.54 to 4.37) and antioxidant activity (from 12.55 to 9.32) decreased. The incorporation of 13 mg/mL of peptide showed a maximum decline in Escherichia coli (0.25 CFU/mL) and Staphylococcus aureus (0.79 CFU/mL) levels. Therefore, we conclude that soy whey-derived peptides can be used as a natural preservative of yogurt (124).
A previous study determined the thermal and pH stability of antioxidative and ACE-inhibitory peptides derived from soybean peptides after fermentation with L. plantarum strain C2. It was concluded that the peptides were thermally stable over a wide temperature range (25–121°C) and pH range (4, 6–8, 13, 14). These stability features indicate the potential thermal resistance of soy peptides in food processing and gastrointestinal digestion at low pH (76). Soy-derived bioactive peptides or soy protein isolates are relatively more economical, even when compared to peptides derived from different dairy proteins (125). They have been reported to promote the growth of some probiotic bacteria, making them a potential prebiotic in food and feed. For instance, Lacticaseibacillus rhamnosus has been shown to utilize both hydrophobic (with 3–5 amino acid residues) and hydrophilic peptides (with >5 amino acid residues) (126). Similarly, soy peptides and proteins have been reported to promote growth and confer competitive advantages to Lactobacillus rhamnosus over Escherichia coli (127, 128). Furthermore, the antimicrobial potential of soybean peptides (53, 128) makes them a great additive to enhance the shelf-life of food and various animal feeds. Kefir is fermented milk that has been consumed for thousands of years. It originated in parts of Eastern Europe and the lush regions of the Caucasus Mountains. Isoflavone biotransformation and flavor production during soymilk kefir fermentation were found to be cultivar- and culture-specific (129–131).
The increasing trend in scientists exploring soybean, their proteins, the synthesis of bioactive peptides, and the discovery of new health benefits associated with soybean will surely help improve human health. The consumption of soy products is promising for reducing various chronic diseases, such as cancer and diabetes. These health benefits are associated with the raw soy protein or derived soy bioactive peptides obtained by processing. Bioactive peptides are primarily generated by enzymes, fermentation, and gastrointestinal digestion. Soy peptides' bioregulatory mechanisms, structural configuration, and mechanism identification are in the developing stage; therefore, research should be conducted on a large scale to identify all of these aspects. This research will lead to the identification of new bioactive peptides and new roles in health, and hence, will improve public health.
YZ drafted the manuscript. GC collected the data and results. CW and JD modified the manuscript. All authors contributed to the article and approved the submitted version.
This study was supported by the Heilongjiang Major Science and Technology Project (2021ZX12B06) and the Central Guidance on Local Science and Technology Development Fund (DQKJJYD0001).
YZ and GC were employed by Hangzhou Joyoung Soymilk & Food Co., Ltd.
The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article, or claim that may be made by its manufacturer, is not guaranteed or endorsed by the publisher.
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Keywords: soybean, functional peptides, plant food, health, fermentation
Citation: Zhu Y, Chen G, Diao J and Wang C (2023) Recent advances in exploring and exploiting soybean functional peptides—a review. Front. Nutr. 10:1185047. doi: 10.3389/fnut.2023.1185047
Received: 13 March 2023; Accepted: 09 May 2023; Published: 15 June 2023.
Copyright © 2023 Zhu, Chen, Diao and Wang. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Jingjing Diao, ZGlhb2ppbmc2MiYjeDAwMDQwOzE2My5jb20=
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