Assessment of In Vitro Digestive Behavior of Lactic-Acid-Bacteria Fermented Soy Proteins: A Study Comparing Colloidal Solutions and Curds.

This study investigated the effect of lactic-acid-bacteria fermentation on the microstructure and gastrointestinal digestibility of soy proteins using a digestomics approach. Fermented soy protein isolates (FSPIs) under varied fermentation-terminal pH demonstrated a colloidal solution (FSPI-7.0/6.0) or yogurt-like curd (FSPI-5.0/4.0) state. Cryo-electron microscopy figures demonstrated the loosely stacked layer of FSPI-7.0/6.0 samples, whereas a denser gel network was observed for FSPI-5.0/4.0 samples. Molecular interactions shifted from dominant ionic bonds to hydrophobic forces and disulfide bonds. The gastric/intestinal digestion demonstrated that the curd samples afforded a significantly low particle size and high-soluble protein and peptide contents in the medium and late digestive phases. A peptidomics study showed that the FSPI-6.0 digestate at early intestinal digestion had a high peptidome abundance, whereas FSPI curd digestates (FSPI-5.0/4.0) elicited a postponed but more extensive promotion during medium and late digestion. Glycinin G2/G4 and ß-conglycinin α/α' subunits were the major subunits promoted by FSPI-curds. The spatial structures of glycinin G2 and ß-conglycinin α subunits demonstrated variations located in seven regions. Glycinin G2 region 6 (A349-K356) and ß-conglycinin α subunit region 7 (E556-E575), which were located at the interior of the 3D structure, were the key regions contributing to discrepancies at the late stage.

Assessment of arsenic distribution, bioaccessibility and speciation in rice utilizing continuous extraction and in vitro digestion.

Rice, a staple food for half the world's population, easily accumulates arsenic (As). Research on As distribution in rice protein and starch and its relationship with rice As bioaccessibility remains limited. This study investigated As distribution, chemical composition, As bioaccessibility and speciation in rice by continuous extraction and in vitro digestion. Of the total As, 87.5-94.5% was in rice protein and 5.0-9.8% in rice starch. The As amount in different protein fractions decreased as follows: glutelin > globulin > albumin > prolamin. As(V), As(III) and DMA in rice were more bioaccessible in the small intestinal phase than the gastric phase, and almost all As(V) dissolved in the small intestinal phase. Bioaccessible As in gastrointestinal digestive solution and As mass in protein fractions (albumin, globulin, and glutelin) were significantly positively correlated (p < 0.05). These results illuminate the bioaccessibility of As to humans consuming As-contaminated rice and avoid overassessment.

Improving surface functional properties of tofu whey-derived peptides by chemical modification with fatty acids.

Effect of acylation with saturated fatty acids on surface functional properties of tofu whey-derived peptides was investigated. Tofu whey (TW) and soy proteins (7S, 11S, and acid-precipitated soy protein [APP]) were hydrolyzed by Protease M 'Amano' G, and resulting peptide mixtures were acylated with esterified fatty acids of different chain length (6C to 18C) to form a covalent linkage between the carboxyl group of fatty acid and the free amino groups of peptide. Acylation significantly (P < 0.05) increased emulsifying properties of 7S, 11S, and APP peptides independent of fatty acid chain length. Acylation decreased water binding capacity although oil binding capacity of acylated tofu whey ultra filtered fraction (UFTW < 3 kDa), 7S- and 11S-peptides were improved compared to native peptides. 7S peptides acylated with long chain fatty acids had shown significant higher surface hydrophobicity as in contrast with acylated UFTW < 3 kDa and APP peptides. Fluorescence spectra studies revealed structural conformation of acylated soy peptides as compared to native peptides. This study shows that chemical modification with fatty acids can further affect functional properties of soy proteins.

A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and beta-conglycinin (7S).

Soybean glycinin (11S) and beta-conglycinin (7S) were subjected to select chemical treatments at various concentrations and resulting changes in protein structures were investigated by circular dichroism (CD) and fluorescence spectrometry. Fluorescence quenching results indicated that urea >/=3 M caused significant unfolding of 11S, but not that of 7S. GuHCl was more effective than urea in denaturation of 11S. A two-step transition in 11S structure was observed with a possible existence of a folding intermediate at 2.5 M GuHCl. Sodium dodecyl sulfate (SDS) measurably altered secondary and tertiary structures of 11S and 7S below SDS critical micellar concentration (CMC), possibly due to formation of mixed peptide-SDS micelles. SDS treatment increased alpha-helical and unordered structures of both proteins at the expense of beta-sheet structure. NaCl and CaCl 2 caused a significant decrease in fluorescence intensity without shifting emission lambda max. Exposure of 7S and 11S to NaSCN respectively at >/=0.3 and >/=0.6 M NaSCN caused a significant increase in fluorescence intensity measured at the corresponding lambda max of the protein. beta-Mercaptoethanol (beta-ME), N-ethylmaleimide (NEM), and phytic acid caused variable red shifts, 2.5-4 nm, in the emission lambda max.