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Comparison of the aggregation behavior of soy and bovine whey protein hydrolysates

Paper ID Volume ID Publish Year Pages File Format Full-Text
14562 1229 2007 5 PDF Available
Title
Comparison of the aggregation behavior of soy and bovine whey protein hydrolysates
Abstract

Soy-derived proteins (soy protein isolate, glycinin, and β-conglycinin) and bovine whey-derived proteins (whey protein isolate, α-lactalbumin, β-lactoglobulin) were hydrolyzed using subtilisin Carlsberg, chymotrypsin, trypsin, bromelain, and papain. The (in)solubility of the hydrolysates obtained was studied as a function of pH. At neutral pH, all soy-derived protein hydrolysates, particularly those from glycinin, obtained by hydrolysis with subtilisin Carlsberg, chymotrypsin, bromelain, and papain showed a stronger aggregation compared to the non-hydrolyzed ones. This increase in aggregation was not observed upon hydrolysis by trypsin. None of the whey-derived protein hydrolysates exhibited an increase in aggregation at neutral pH. The high abundance of theoretical cleavage sites in the hydrophobic regions of glycinin probably explains the stronger exposure of hydrophobic groups than for the other proteins, which is suggested to be the driving force in the aggregate formation.

Keywords
Aggregation; Peptides; Soy protein; Whey protein
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Comparison of the aggregation behavior of soy and bovine whey protein hydrolysates
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biotechnology Advances - Volume 25, Issue 6, November–December 2007, Pages 606–610
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
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