Improved Bile Acid-binding Ability of Soybean Glycinin A1a Polypeptide by the Introduction of a Bile Acid-binding Peptide (VAWWMY)

Evidence for the Existence of a Soybean Resistant Protein That Captures Bile Acid and Stimulates Its Fecal Excretion

“…In fact, peptides prepared by the in vitro digestion of soybean protein had bile acid-binding activity and stimulated fecal steroid excretion. [3][4][5][6] A similar effect has also been observed in proteins other than soy protein such as the peptide preparations obtained from papain-hydrolyzed pork meat 7) and alactoglobulin tryptic hydrolysate. 8) Sugano and his coworkers digested a soy protein isolate in vitro by microbial proteases and prepared soluble and residual fractions, these being referred to as the low-molecular fraction (LMF) and high-molecular fraction (HMF), respectively.…”

Rice Endosperm Protein Administration to Juvenile Mice Regulates Gut Microbiota and Suppresses the Development of High-Fat Diet-Induced Obesity and Related Disorders in Adulthood

“…Moreover, the excretion of lipids, fatty acids, and bile acids in the feces of mice fed REP, especially during adulthood, was higher than in mice fed a casein-based diet. It has been reported that REP can bind to fatty acids and bile acids and interfere with their absorption in the lower intestine and thereby may have a specific ability to increase their fecal excretion [18], as reported for soybean peptides [50]. The mechanism of action of cholestyramine, a basic anion-exchange resin used to improve lipid metabolism, involves its binding to bile acids and increasing their excretion in feces in humans [51] and in animal models [52].…”

Effective screening for hypolipidemic bile acid - binding peptides by hierarchical clustering - based catalog array

“…A total of 544 amino acid indices (Table SI) registered in the database (version 9.1, as of January 2008) were found to comprise 21 clusters, with high correlation ( Figure S1). To represent the remaining 13 independent clusters covering the majority of indices, 13 indices were selected (schematic illustration in Figure 1A; detailed list in Table SII): [1] Isoelectric point [31], [2] Normalized van der Waals volume [32], [3] Alpha-helix indices for beta-proteins [33], [4] Beta-strand indices for betaproteins [33], [5] Side-chain contribution to protein stability [34], [6] The stability scale from the knowledge-based atom-atom potential [35], [7] Hydropathy index [36], [8] Normalized frequency of turn [37], [9] Free energy in beta-strand region [38], [10] Free energy in alpha-helical region [38], [11] Polarity [31], [12] Side chain interaction parameter [39], and [13] Amino acid distribution [40], Each amino acid of each sequenced peptide sequenced was numbered from the N to C-terminus using each of the 13 indices. Therefore, each amino acid index profile for each sequence included 39 parameters (3 positions × 13 indices).…”

“…Previously, Choi et al reported that a hydrophobic peptide derived from the soy protein glycinin binds strongly to bile acid in vitro [11,12]. Nagaoka S. et al found for the first time that VAWWMY (soystatin) derive from soybean glycinin acted as an inhibitor of cholesterol absorption in vivo [13].…”