Enzymatic Preparation, Identification by Transmembrane Channel-like 4 (TMC4) Protein, and Bioinformatics Analysis of New Salty Peptides from Soybean Protein Isolate.

To address the public health challenges posed by high-salt diets, this study utilized pepsin and flavourzyme for the continuous enzymatic hydrolysis of a soy protein isolate (SPI). The separation, purification, and identification of salt-containing peptides in SPI hydrolysate were conducted using ultrafiltration (UF), gel filtration chromatography (GFC), and Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (LC-MS/MS). Subsequently, a molecular docking model was constructed between salt receptor protein transmembrane channel 4 (TMC4) and the identified peptides. Basic bioinformatics screening was performed to obtain non-toxic, non-allergenic, and stable salt peptides. After the enzymatic hydrolysis, separation, and purification of SPI, a component with a sensory evaluation score of 7 and an electronic tongue score of 10.36 was obtained. LC-MS/MS sequencing identified a total of 1697 peptides in the above component, including 84 potential salt-containing peptides. A molecular docking analysis identified seven peptides (FPPP, GGPW, IPHF, IPKF, IPRR, LPRR, and LPHF) with a strong theoretical salty taste. Furthermore, residues Glu531, Asp491, Val495, Ala401, and Phe405 of the peptides bound to the TMC4 receptor through hydrogen bonds, hydrophobic interactions, and electrostatic interactions, thereby imparting a significant salty taste. A basic bioinformatics analysis further revealed that IPHF, LPHF, GGPW, and IPKF were non-toxic, non-allergenic, and stable salt-containing peptides. This study not only provides a new sodium reduction strategy for the food industry, but also opens up new avenues for improving the public's healthy eating habits.

Effects of Germination on the Structure, Functional Properties, and In Vitro Digestibility of a Black Bean (Glycine max (L.) Merr.) Protein Isolate.

The utilization of black beans as a protein-rich ingredient presents remarkable prospects in the protein food industry. The objective of this study was to assess the impact of germination treatment on the physicochemical, structural, and functional characteristics of a black bean protein isolate. The findings indicate that germination resulted in an increase in both the total and soluble protein contents of black beans, while SDS-PAGE demonstrated an increase in the proportion of 11S and 7S globulin subunits. After germination, the particle size of the black bean protein isolate decreased in the solution, while the absolute value of the zeta potential increased. The above results show that the stability of the solution was improved. The contents of ß-sheet and ß-turn gradually decreased, while the content of α-helix increased, and the fluorescence spectrum of the black bean protein isolate showed a red shift phenomenon, indicating that the structure of the protein isolate and its polypeptide chain were prolonged, and the foaming property, emulsification property and in vitro digestibility were significantly improved after germination. Therefore, germination not only improves functional properties, but also nutritional content.

Preparation, partial characterization and biological activity of exopolysaccharides produced from Lactobacillus fermentum S1.

A high slime-producing Lactobacillus fermentum strain (named as L. fermentum S1) was isolated from traditional fermented Fuyuan pickle, which was made of white turnip and collected from Fuyuan county, Yunnan province, China. We extracted and purified the exopolysaccharides from L. fermentum S1, and investigated their preliminary structure characteristics and biological activities. Three purified exopolysaccharide fractions, designated as EPS1, EPS2 and EPS3, were obtained from the culture supernatant of L. fermentum S1 by ethanol precipitation, anion exchange and gel filtration chromatography. The EPS2 and EPS3 were homogeneous with molecular weights of 4.45 × 106 and 2.82 × 106 Da, respectively. All the purified EPS fractions were composed of glucose, galactose, mannose and arabinose, but with different molar ratios. EPS1, EPS2 and EPS3 presented different surface morphologies and their degradation temperatures were 302.7°C, 316.3°C and 316.9°C, respectively. Bioactivity research showed that L. fermentum S1 EPS elicited free radical scavenging capacity and ferric reducing antioxidant power, and 1 mg/mL of EPS significantly improved the gastrointestinal transit tolerance of non EPS-producing strain L. fermentum LG1. Moreover, S1 EPS had a favorable anti-biofilm activity against Escherichia coli and Staphylococcus aureus. These results indicated that S1 EPS could be explored as a promising functional adjunct for application in foods.