Bean Protein Hydrolysates Research Articles

Novel Peptides LFLLP and DFFL from Jack Bean Protein Hydrolysates Suppress the Inflammatory Response in Lipopolysaccharide-Stimulated RAW 264.7 Cells.

The production of inflammatory cytokines such as tumor necrosis factor (TNF)-α by activated macrophage cells plays an important role in the development of intestinal inflammation. The present study investigated the anti-inflammatory effect of the protein hydrolysates prepared from the jack bean (JBPHs), Canavalia ensiformis (L.) DC, using the enzyme Alcalase, in a murine macrophage model, RAW 264.7 cells, which were stimulated by lipopolysaccharides. JBPHs reduced the TNF-α expression at the protein and mRNA levels through the downregulation of cellular signaling pathways involved in nuclear factor kappa B (NF-κB), extracellular signal-regulated kinase (ERK), and p38. A combination of mass spectrometry and in silico approaches identified 10 potential anti-inflammatory peptides in the JBPHs, including LFLLP and DFFL. Interestingly, while LFLLP targeted the NF-κB pathway, DFFL targeted p38 and ERK to suppress the TNF-α production in the RAW 264.7 cells. In addition, LFLLP and DFFL were localized in the cytosol of the cells. These results demonstrated that LFLLP and DFFL were incorporated by RAW 264.7 cells and, at least in part, contributed to the reduction in TNF-α by JBPHs. These peptides isolated from JBPHs may well be utilized as new alternatives to alleviate intestinal inflammation.

Physicochemical and stability analysis of mung bean protein hydrolysates with lipid peroxidation inhibition

This study investigated mung bean protein hydrolysates (MBPH) produced using neutral protease, examining their physicochemical properties, stability, and lipid peroxidation inhibition capabilities. The research revealed that MBPH molecular weight ranged from 17 to 26 kDa and perform various functions, including catalytic, nutrient storage, and binding. Stability assessments showed that MBPH are stable at 45 °C and pH of 7.5 but are light-sensitive and unstable in solution or when combined with sugars. Additionally, increased concentrations of digestive enzymes reduce MBPH stability. Antioxidant tests in vitro and in Caenorhabditis elegans confirmed MBPH's ability to neutralizing radicals, enhance antioxidant enzyme activities, and reduce lipid peroxidation, thereby protecting against oxidative damage. Furthermore, in vivo experiments showed that MBPH extend the lifespan of worms and reduced their body lipid content, indicating potential benefits in mitigating cholesterol-related damage. This research demonstrates the potential of MBPH in inhibiting lipid peroxidation.

Identification and Molecular Mechanism of Anti-inflammatory Peptides Isolated from Jack Bean Protein Hydrolysates: in vitro Studies with Human Intestinal Caco-2BBe Cells

Jack bean (JB), Canavalia ensiformis (L.) DC, is a commonly cultivated legume in Indonesia. It is rich in protein, which can be hydrolyzed, making it potentially a good source of bioactive peptides. Intestinal inflammation is associated with several diseases, and the production of interleukin-8 (IL-8) in intestinal epithelial cells induced by tumor necrosis factor (TNF)-α has an important role in inflammatory reaction. The present study investigated the anti-inflammatory effects of peptides generated from enzymatic hydrolysis of JB protein on human intestinal Caco-2BBe cells. Additionally, in silico approaches were used to identify potential bioactive peptides. JB protein hydrolysate (JBPH) prepared using pepsin and pancreatin reduced the IL-8 expression at protein and mRNA levels in Caco-2BBe cells stimulated with TNF-α. Immunoblot analysis showed that the JBPH reduced the TNF-α-induced phosphorylation of c-Jun-NH(2)-terminal kinase, nuclear factor kappa B (NF-κB), and p38 proteins. Anti-inflammatory activity was observed in the 30% acetonitrile fraction of JBPH separated on a Sep-Pak C18 column. An ultrafiltration method revealed that relatively small peptides (< 3 kDa) had a potent inhibitory effect on the IL-8 production. Purification of the peptides by reversed-phase and anion-exchange high performance chromatography produced three peptide fractions with anti-inflammatory activities. A combination of mass spectrometry analysis and in silico approaches identified the potential anti-inflammatory peptides. Peptides derived from JB protein reduces the TNF-α-induced inflammatory response in Caco-2BBe cells via NF-κB and mitogen-activated protein kinase signaling pathways. Our results may lead to a novel therapeutic approach to promote intestinal health.

The structural characteristics and physicochemical properties of mung bean protein hydrolysate of protamex induced by ultrasound.

The limited physicochemical properties (such as low foaming and emulsifying capacity) of mung bean protein hydrolysate restrict its application in the food industry. Ultrasound treatment could change the structures of protein hydrolysate to accordingly affect its physicochemical properties. The aim of this study was to investigate the effects of ultrasound treatment on the structural and physicochemical properties of mung bean protein hydrolysate of protamex (MBHP). The structural characteristics of MBHP were evaluated using tricine sodium dodecylsulfate-polyacrylamide gel electrophoresis, laser scattering, fluorescence spectrometry, etc. Solubility, fat absorption capacity and foaming, emulsifying and thermal properties were determined to characterize the physicochemical properties of MBHP. MBHP and ultrasonicated-MBHPs (UT-MBHPs) all contained five main bands of 25.8, 12.1, 5.6, 4.8 and 3.9 kDa, illustrating that ultrasound did not change the subunits of MBHP. Ultrasound treatment increased the contents of α-helix, β-sheet and random coil and enhanced the intrinsic fluorescence intensity of MBHP, but decreased the content of β-turn, which demonstrated that ultrasound modified the secondary and tertiary structures of MBHP. UT-MBHPs exhibited higher solubility, foaming capacity and emulsifying properties than MBHP, among which MBHP-330 W had the highest solubility (97.32%), foaming capacity (200%), emulsification activity index (306.96 m2 g-1 ) and emulsion stability index (94.80%) at pH 9.0. Ultrasound treatment enhanced the physicochemical properties of MBHP, which could broaden its application as a vital ingredient in the food industry. © 2023 Society of Chemical Industry.

Identification and molecular binding mechanism of novel pancreatic lipase and cholesterol esterase inhibitory peptides from heat-treated adzuki bean protein hydrolysates

Heat-treated adzuki bean protein hydrolysates exhibit lipid-reducing properties; however, few studies have reported pancreatic lipase (PL) and cholesterol esterase (CE) inhibitory effects and elucidated the underlying mechanisms. In this study, we accomplished the identification of antiobesity peptides through peptide sequencing, virtual screening, and in vitro experiments. Furthermore, the mechanisms were investigated via molecular docking. The findings reveal that the action of pepsin and pancreatin resulted in the transformation of intact adzuki bean protein into smaller peptide fragments. The < 3 kDa fraction exhibited a high proportion of hydrophobic amino acids and displayed superior inhibitory properties for both PL and CE. Five novel antiobesity peptides (LLGGLDSSLLPH, FDTGSSFYNKPAG, IWVGGSGMDM, YLQGFGKNIL, and IFNNDPNNHP) were identified as PL and CE inhibitors. Particularly, IFNNDPNNHP exhibited the most robust biological activity. These peptides exerted their inhibitory action on PL and CE by occupying catalytic or substrate-binding sites through hydrogen bonds, hydrophobic interactions, salt bridges, and π-π stacking.

Black bean (Phaseolus vulgaris L.) protein hydrolysates reduce acute postprandial glucose levels in adults with prediabetes and normal glucose tolerance

This study evaluated the acute effect of black bean protein hydrolysate (BPH) on postprandial glucose and insulin levels in adults with normal glucose tolerance (NGT) or prediabetes. First, an in silico predictive digestion was performed on twenty peptides identified in BPH. Then, 28 adults with NGT or prediabetes were randomized to a parallel double-blind, placebo-controlled trial. Following consent, participants were randomly assigned to one of two groups, placebo, or 5 g of BPH. To evaluate the acute effects of BPH, an oral glucose tolerance test was administered, and blood samples were collected at 60, 120, and 150 min. In the 5 g BPH group, the area under the curve for glucose, and glucose levels at 120 min were statistically lower compared to the placebo group (p = 0.04, p = 0.02). In this study, BPH had an acute glucose lowering effect after an oral glucose tolerance test in subjects with NGT or prediabetes.

Restoration and preservation effects of mung bean antioxidant peptides on H2O2-induced WRL-68 cells via Keap1-Nrf2 pathway.

Mung bean antioxidant peptides (MBAPs) were prepared from mung bean protein hydrolysate, and four peptide sequences including Ser-Asp-Arg-Thr-Gln-Ala-Pro-His (~953 Da), Ser-His-Pro-Gly-Asp-Phe-Thr-Pro-Val (~956 Da), Ser-Asp-Arg-Trp-Phe (~710 Da), and Leu-Asp-Arg-Gln-Leu (~644 Da) were identified. The effects of MBAPs on the oxidation-induced normal human liver cell line WRL-68 were analyzed to determine the mechanism protecting the oxidation-induced injury. The results showed that the cells were subjected to certain oxidative damage by H2O2 induction, as evidenced by decreased cell number and viability, overproduction of intracellular ROS, and decreased mitochondrial membrane potential. Compared with the H2O2-induced group, the MBAP-treated oxidation-induced group exhibited significantly higher cell number and viability, and the intracellular ROS was similar to that of the control group, suggesting that MBAP scavenges excessive intracellular free radicals after acting on the oxidation-induced cells. Combined with Western blotting results, it was concluded that the MBAP-treated oxidation-induced group also significantly promoted the expression of proteins related to the kelch-like ech-related protein 1 (Keap1)/ nuclear factor e2-related factor 2 (Nrf2) signaling pathway, which resulted in an approximately 2-fold increase in antioxidant enzymes, and a decrease in malondialdehyde content of approximately 55% compared to oxidatively-induced cells, leading to the recovery of both cell morphology and viability. These results suggest that MBAPs scavenge intracellular free radicals and improve oxidative stress in hepatocytes through the expression of Keap1/Nrf2 pathway-related protein, thereby reducing oxidative attack on the liver. Therefore, MBAP is applied as a nutritional ingredient in the functional food field, and this study provides a theoretical basis for the high utilization of mung bean proteins.

Effects of processing technologies on the antioxidant properties of common bean (Phaseolus vulgaris L.) and lentil (Lens culinaris) proteins and their hydrolysates

The effects of ultrasound (280 W, 5 min), heat treatment (75 °C and 90 °C for 10 min) and microfluidization (125 MPa, 4 cycles) as pre or post treatments and their combination with enzymatic hydrolysis on the antioxidant properties of common bean and lentil protein hydrolysates were investigated. In general, hydrolysis resulted in increases of antioxidant activity, both in the presence and absence of processing technologies. The increases reached maximum values of 158% (ABTS), 105% (DPPH), 279% (FRAP) and 107% (TAC) for the bean protein hydrolysates submitted to post-treatment with ultrasound (ABTS, FRAP and TAC) and pre-treatment with microfluidization (DPPH), compared to their respective controls (untreated samples). For lentil proteins, the increases reached 197% (ABTS), 170% (DPPH), 690% (FRAP) and 213% (TAC) for samples submitted to ultrasound post-treatment (ABTS), microfluidization pre-treatment (DPPH) and post-treatment (FRAP), and 75 °C pre-treatment (TAC) compared to their respective controls. Surface hydrophobicity and molecular weight profile by SEC-HPLC analysis indicated modifications in the structures of proteins in function of the different processing technologies. For both proteins, electrophoresis indicated a similar profile for all hydrolysates, regardless of the process applied as pre or post treatment. Solubility of bean and lentil protein concentrates was also improved. These results indicated that different processing technologies can be successfully used in association with enzymatic hydrolysis to improve the antioxidant properties of lentil and bean proteins.

Kidney bean protein hydrolysate as a fish meal replacer: Effects on growth, digestive enzymes, metabolic functions, immune-antioxidant parameters and their related gene expression, intestinal and muscular gene expression

A feeding trial for 70 days was designated on Nile tilapia, Oreochromis niloticus (O. niloticus). A total of 200 fish (34.38 ± 0.05 g) were assigned into five groups, four replicates for each (10 fish/replicate; 40 fish/group) and received five isonitrogenous and isocaloric diets with five replacement levels of fishmeal (FM) with kidney bean (Phaseolus vulgaris L) protein hydrolysate (KBH) (0, 25, 50, 75, 100%). The findings demonstrated a significant increase in the performance metrics (final body weight, total weight gain, average daily weight gain, protein efficiency ratio, and specific growth rate) with a considerable improvement in the feed conversion ratio across all replacement levels, with the greatest value obtained in the KBH75 and KBH100 groups. Regarding the broken line regression analysis, the optimum FM replacement level with KBH was 76%. By replacing FM with KBH, the growth hormone and digestive enzymes (amylase and protease) levels were significantly increased, whilst the glucose and leptin hormone levels significantly declined. The amino acid transporters (solute carrier family 15 member 2 and solute carrier family 26 member 6), insulin growth factor-1, the immune-associated genes (interleukin-8, toll-like receptors-7, and cc-chemokine), and the antioxidant-associated genes (glutathione peroxidase, superoxide dismutase, and Glutathione synthetase) expression was substantially boosted in all replacement levels, where the KBH50 group recorded the highest expression. As well as the mRNA expression of myostatin was down-turned in all replacement levels relative to the KBH0 group. Improving the immune functions (lysozyme, complement 3, nitric oxide, phagocytic %, and phagocytic index) was noticed by FM replacement with KBH. The cumulative mortality as a result of challenging with Aeromonas sobria at the end of the feeding trial was decreased by increasing the replacement level (80, 40, 37, 30, and 25% for KBH0, KBH25, KBH50, KBH75, and KBH100, respectively). From the economic point of view, the feed costs and feed cost/ kg gain declined in the KBH75 and KBH100 diets. From the aforementioned outcomes, KBH could replace the FM up to 100% with improving the growth and their related genes expression, digestive enzymes activity, and immune/antioxidant parameters and their encoding gene expression, and the optimal replacement level was 76%. The replacement of FM with KBH was economically efficient.

Assessment of the DPP‐IV inhibitory potential of mung bean and adzuki bean protein hydrolysates using enzymatic hydrolysis process: specificity of peptidases and novel peptides

SummaryMung bean and adzuki bean protein concentrates were hydrolysed to the same degree of hydrolysis by two peptidases: Flavourzyme and Alcalase. Peptide fractions were analysed using MALDI‐TOF MS to investigate the differences in enzyme cleavage specificity and the inhibition activity of Dipeptidyl peptidase‐IV (DPP‐IV), using bioinformatics tools. It was shown that each peptidase showed specific selectivity in cleaving the designated substrate at a specific site. Alcalase main cutting sites on mung bean and adzuki bean proteins were identified as hydrophobic amino acid residues, particularly between Leu‐X (X‐Leu) or Phe‐X (X‐Phe) while Flavourzyme cleavage occurred between peptide bonds between Gln‐X (X‐Gln) or Pro‐X (X‐Pro). The findings demonstrated that Flavourzyme had a higher capacity for generating active peptides from both mung bean and adzuki bean protein concentrates with higher levels of DPP‐IV inhibitory activity. Proteomics and bioinformatics methodologies provided the essential knowledge required to explore novel peptides with DPP‐IV inhibitor potential from mung bean and adzuki bean hydrolysates.

Comparative study on structural, biological and functional activities of hydrolysates from Adzuki bean (Vigna angularis) and mung bean (Vigna radiata) protein concentrates using Alcalase and Flavourzyme

The physicochemical features of mung bean protein (MBP) and adzuki bean protein (ABP) hydrolysates derived from Alcalase (MBPHA, ABPHA) and Flavourzyme (MBPHF, ABPHF) were assessed using FTIR, hydrophobicity, emulsion activity, zeta potential, and health-promoting activities. The results proved that the choice of peptidase and substrate both have a significant effect on the hydrolysates in different physicochemical, structural and functional properties. Size exclusion-HPLC was used to fractionate the MBP and ABP hydrolysates. The results demonstrated that Alcalase hydrolysates included smaller peptides than Flavourzyme hydrolysates, and the chromatogram patterns of the two peptidases were similar. The peptides with the most potent antioxidant and ACE-inhibitory properties were identified using MALDI-TOF-MS. The fraction (F4) of MBPHA exhibited the highest levels of metal chelating activity. The Flavourzyme hydrolysates fraction (F2) and the ABPHA fraction (F2) showed the highest ABTS radical scavenging activity and ACE-inhibitory activity, respectively. Pro-Pro was identified in peptide sequences with ABTS radical scavenging activity as an active component while Pro-Gln was identified in peptide sequences with ACE-inhibitory activity. As a result, Pro-Pro and Pro-Gln, respectively, are likely-one of the characteristics of antioxidant and ACE-inhibitory peptides from MBP and ABP. Compared to mung bean and adzuki bean protein as substrate, Alcalase and Flavourzyme as peptidases significant impacted the development of distinct functionalities and biological activities.

The Preservative Action of Protein Hydrolysates from Legume Seed Waste on Fresh Meat Steak at 4 °C: Limiting Unwanted Microbial and Chemical Fluctuations.

Valorizing agricultural wastes to preserve food or to produce functional food is a general trend regarding the global food shortage. Therefore, natural preservatives were developed from the seed waste of the cluster bean and the common bean to extend the shelf life of fresh buffalo meat steak and boost its quality via immersion in high-solubility peptides, cluster bean protein hydrolysate (CBH), and kidney bean protein hydrolysate (RCH). The CBH and the RCH were successfully obtained after 60 min of pepsin hydrolysis with a hydrolysis degree of 27–30%. The SDS-PAGE electropherogram showed that at 60 min of pepsin hydrolysis, the CBH bands disappeared, and RCH (11–48 kD bands) nearly disappeared, assuring the high solubility of the obtained hydrolysates. The CBH and the RCH have considerable antioxidant activity compared to ascorbic acid, antimicrobial activity against tested microorganisms compared to antibiotics, and significant functional properties. The CBH and the RCH (500 µg/mL) successfully scavenged 93 or 89% of DPPH radicals. During the 30-day cold storage (4 °C), the quality of treated and untreated fresh meat steaks was monitored. Protein hydrolysates (500 g/g) inhibited lipid oxidation by 130–153% compared to the control and nisin and eliminated 31–55% of the bacterial load. The CBH and the RCH (500 µg/g) significantly enhanced meat redness (a* values). The protein maintained 80–90% of the steak’s flavor and color (p < 0.05). In addition, it increased the juiciness of the steak. CBH and RCH are ways to valorize wastes that can be safely incorporated into novel foods.

Exploring the Antioxidant and Structural Properties of Black Bean Protein Hydrolysate and Its Peptide Fractions.

A great deal of attention has been paid to charactering the protein hydrolysates prepared by enzymatic hydrolysis, while the influence of molecular weight (MW) distributions on the resultant hydrolysates remains unclear. This study aimed to explore the physicochemical and antioxidant characteristics of protein hydrolysate and its peptide fractions. Bromelain has been commonly used to hydrolyze black bean protein via response surface methodology (RSM). The optimal hydrolysis parameters were observed at 52°C, pH 7, E/S ratio of 2.2 (ratio of enzyme to substrate), and 4 h. Under these parameters, the hydrolysate (BPH) presented DPPH radical scavenging activity and Fe2+ chelating activity with IC50 values of 100.08 ± 2.42 and 71.49 ± 0.81 μg/mL, respectively. This might be attributed to structural characteristics, varying with different molecular weight distributions. Interestingly, among BPH and its peptide fractions, peptides smaller than 3 kDa were noted to exhibit the strongest DPPH and ABTS radical scavenging activity. More intriguingly, this peptide fraction (<3 kDa) could predominantly prolong the induction period of sunflower oil, which was, respectively increased to 1.31 folds. This may be due to high proportions of hydrophobic amino acids. Unexpectedly, the optimal Fe2+ chelating activity was observed in the peptide fraction measuring at 3–10 kDa, showing highly positive correlations with histidine and arginine. These identified peptide fractions derived from black bean protein can therefore be employed for food fortification acting as natural antioxidant alternatives.

Anti-inflammatory effects of mung bean protein hydrolysate on the lipopolysaccharide- induced RAW264.7 macrophages.

The anti-inflammatory effects of mung bean protein hydrolysate (MBPH) on the lipopolysaccharide (LPS)-induced macrophages were investigated herein. MBPH was shown to affect the cell morphology, proliferation, cell cycle, cytokine levels at different culture times, and the expression level of nuclear factor-kappa B (NF-κB). The obtained results revealed that different fractions of MBPH promote cell proliferation, alter the cell cycle by decreasing the proportion of cells in the S stage and increasing the proportion of cells in the G2 stage, increase the expression of cytokines, included IL-6, IL-1β, and TNF-α, and negatively affect the LPS-induced inflammatory cytokines. Based on the analysis of cytokine expression at different points in time, it is concluded that cytokine secretion of MBPH-treated group reaches a peak at 24h, the result was significantly different compared to other treatment groups (P < 0.05). It can be observed that the inflammatory response induced by LPS in the MBPH-III treatment group is reduced compared with other fractions (P < 0.05). In addition, MBPH inhibits the activation of NF-κB signaling pathway by inhibiting the nuclear transcription of p65 and phosphorylation of IκBα in macrophages induced by LPS. Our results demonstrated that lower molecular weight MBPH exerted stronger anti-inflammatory effects than other molecular fractions. Thus, MBPH could be utilized as a functional food ingredient to prevent inflammation in chronic diseases.

Fractionation of foam-mat dried rice bean hydrolysates using membrane filtration and solid phase extraction: Peptide- and phenolic-based fractions with bioactive potential

Flavourzyme was used to hydrolyze the germinated rice bean, and the hydrolysates were separated using membrane ultrafiltration with a molecular weight (MW) cut-off of 3 kDa. The ultrafiltration permeate fraction (UFP), non-fractionated hydrolysate (RH), and ultrafiltration retentate fraction (UFR) were foam-mat dried at two temperatures, 60 and 70 °C. The content of each phenolic composition in dried RH samples decreased with increasing drying temperature particularly gallic acid, p-coumaric acid, vanillin, rutin, and, quercetin dropped by 27, 24, 21, 35 and 33%, however the kind of phenolic compositions identified in dried samples was unaffected by drying temperature. Dried UFR and dried UFP had different chromatograms. When the dried UFP and dried UFR chromatograms were examined, it was discovered that the intensity of the peaks in the dried UFR chromatogram was much lower. The majority of phenolics can pass through ultrafiltration membranes with a molecular weight cut-off of 3 kDa, according to this finding. Individual phenolic compound levels in dried UFP samples were similar to RH, implying that the majority of phenolic components in dried rice bean protein hydrolysate were smaller than 3 kDa. With increasing drying temperature, gallic acid, p-coumaric acid, catechol, epicatechin and naringenin levels in dried UFP samples were decreased. The antioxidant capacity of dried rice bean hydrolysate was discovered to be due to phenolic components (gallic acid, epicatechin, catechol, ferulic acid, and rutin), which were found to be more prevalent than peptide fractions. As a result, rice bean hydrolysates could bring novel health advantages, which could lead to the development of nutraceuticals and food products.

Influence of ultrasound treatment on the physicochemical and antioxidant properties of mung bean protein hydrolysate

This study aimed to investigate influence of ultrasonic treatment on physicochemical and antioxidant properties of mung bean protein hydrolysate (MPH). Physicochemical properties of MPH were evaluated by Tricine-SDS-PAGE, particle size distribution, fourier transform infrared spectroscopy (FTIR) and fluorescence spectroscopy, among others. Radicals scavenging activities of ABTS, hydroxyl, superoxide anion, Fe2+ chelating ability and reducing power characterized antioxidant activities of MPH. MPH contained four bands of 25.6, 12.8, 10.6 and 4.9 kDa, in which 4.9 kDa was the most abundant. Ultrasonic treatment increased the contents of aromatic and hydrophobic amino acids in MPH. Ultrasonic treatment decreased the content of α-helix of MPH and increased β-sheet and β-turn compared to MPH. MPH-546 W (ultrasonic treatment 546 W, 20 min) had the lowest average particle size (290.13 nm), zeta potential (-36.37 mV) and surface hydrophobicity (367.95 A.U.). Antioxidant activities of ultrasonicated-MPH increased with the ultrasonic power, achieving the lowest IC50 (mg/mL) of 0.1087 (ABTS), 1.796 (hydroxyl), 1.003 (superoxide anion) and 0.185 (Fe2+ chelating ability) in 546 W power. These results indicated ultrasonic treatment would be a promising method to improve the antioxidant properties of MPH, which would broaden the application scope of MPH as bioactive components in the food industry.

Heat-Treated Adzuki Bean Protein Hydrolysates Reduce Obesity in Mice Fed a High-Fat Diet via Remodeling Gut Microbiota and Improving Metabolic Function.

Heat-treated adzuki bean protein hydrolysates (APH) reduce cholesterol in vitro. However, it is unclear if APH have anti-obesity effects in vivo and, if so, the relationship between the effects and the improvement of gut microbiota composition and metabolic function. Four groups of mice are fed either a normal control diet (NCD) or a high-fat diet (HFD) with or without APH for 12 weeks. In HFD-fed mice, APH supplementation significantly alleviate fat accumulation, dyslipidemia, insulin resistance, hepatic steatosis, and inflammation. In addition, APH supplementation regulate gut microbiota composition, reduce the abundance of harmful bacteria (Clostridium_sensu_stricto_1, Romboutsia, Blautia, Mucispirillum, Bilophila, and Peptococcus), enrich Lactobacillus and SCFA-producing bacteria (Lactobacillaceae, Eisenbergiella, Alistipes, Parabacteroides, Tannerellaceae, Eubacterium_nodatum_group, Acetatifactor, Rikenellaceae, and Odoribacter), and increase fecal SCFAs concentration. Importantly, APH supplementation significantly regulate the levels of serum metabolites, especially Lactobacillus-derived metabolites and tryptophan derivatives, which help to alleviate obesity and its complications. APH improve gut microbiota composition and metabolic function in mice and may help to prevent and treat obesity and related complications.

Sensory and Biological Potential of Encapsulated Common Bean Protein Hydrolysates Incorporated in a Greek-Style Yogurt Matrix.

The work aimed to develop a gel as a protective barrier of common bean protein hydrolysates to be incorporated into a Greek-style yogurt and evaluate the sensory perception and biological potential. The gel was formed by complex coacervation and induced heat at a pH 3.5 and 3:1 biopolymer ratio (whey protein and gum arabic). The gel presented a 39.33% yield, low syneresis (0.37%), and a gel strength of 100 gf. The rheological properties showed an elastic behavior (G′ > G″). The gel with the most stable characteristics favored the incorporation of 2.3 g of hydrolysates to be added into the Greek-style yogurt. Nutritionally, the Greek-style yogurt with the encapsulated hydrolysates presented 9.96% protein, 2.27% fat, and 1.76% carbohydrate. Syneresis (4.64%), titratable acidity (1.39%), and viscoelastic behavior presented similar characteristics to the Greek-style control yogurt. The bitterness and astringency in yogurt with encapsulated hydrolysates decreased 44% and 52%, respectively, compared to the yogurt control with the unencapsulated hydrolysates. The Greek-style yogurt with the encapsulated hydrolysates showed the ability to inhibit enzymes related to carbohydrate metabolism (α-amylase (92.47%) and dipeptidyl peptidase-4 (75.24%) after simulated gastrointestinal digestion). The use of gels could be an alternative to transporting, delivering, and masking off-flavors of common bean protein hydrolysates in food matrices to decrease glucose absorption for type 2 diabetes patients.

Structure and in vitro bioactive properties of O/W emulsions generated with fava bean protein hydrolysates

The use of plant-derived proteins in the generation of food products is gaining popularity as an alternative to proteins of animal origin. This study described the emulsifying and bioactive properties of fava bean protein hydrolysates (FBH) generated at low and high degree of hydrolysis (DH), i.e., FBH8 (low DH: 8.4 ± 0.3) and FBH210 (high DH: 15.6 ± 0.7) when adjusted to three different pHs (3.0, 5.0 and 8.0). Overall, FBH8, had more favourable emulsifying properties compared to the FBH210. The emulsion generated with FBH8 at pH 8.0 also had the highest antioxidant activity when measured by the oxygen radical absorbance capacity (ORAC) and ferric reducing antioxidant power (FRAP) assays with values of 1108.6 ± 3.8 and 1159.9 ± 20.5 μmol Trolox Eq·g−1 emulsion, respectively. The antioxidant activity of the emulsions, in most cases, remained unchanged following in vitro simulated gastrointestinal digestion. Both the FBH8 and FBH210 emulsions following in vitro simulated gastrointestinal digestion were able to inhibit the activities of dipeptidyl peptidase-IV (DPP-IV) and angiotensin converting enzyme (ACE) with ∼45% and 65% inhibition, respectively. These results indicated that hydrolysates from fava bean may find use for the generation of bioactive emulsions.

Evaluation of quality parameters and antioxidant properties of protein concentrates and hydrolysates of hyacinth bean (Lablab purpureus)

AbstractThe hyacinth bean protein hydrolysates (HPHs) were derived from hyacinth bean protein concentrate (HPC) by enzymatic hydrolysis following isoelectric method using pepsin enzyme. The HPH displayed strong antioxidant activities than hyacinth flour and HPC, where released amino acids were the major contributors to enhanced antioxidant activities. The IC50 values for HPH and ascorbic acid (AA) were 0.052 and 0.020 mg/ml correspondingly. The total phenolic content (TPC) of HPH and HPC were 35.1 and 22.03 mg GAE/g, respectively. The antioxidant potential of both HPC and HPH was assessed by adding those components to apple juice at a rate of 3 g/L and kept at ambient temperature for 6 days. Both HPC and HPH delayed the development of oxidizing products during 6‐day storage where HPH exhibited significantly higher antioxidant activity to that of HPC. The HPH reduced the oxidizing substances by 79.58%, 65.1%, and 62.03% at Days 0, 1, and 6, respectively, compared with control. These findings demonstrate that the hyacinth hydrolysates offer a good potential for use in the food industry as natural antioxidants.