JOURNAL ARTICLE

Surface properties and structure characteristics of soybean protein isolate by limited hydrolysis

Abstract

The surface adsorption properties of soy protein isolated (SPI) were obviously improved after limited hydrolysis by trypsin. When the hydrolyzing degree (DH) of SPI was controlled from 2% to 6%, the surface tension behavior of modified SPI was decreased with the hydrolyzing degree increasing. Compared to the natural soy protein, the values of surface tension of modified SPI which DH was 4% decreased by 19.35% and the foamability increased by 22.03%. The variations of surface properties of modified SPI were related to its structural change, it presented better surface hydrophobic properties, lower electric surface charge, and the increased viscosity which was apt to adsorb at interface of two phase region as compared to the natural soy protein which had poor behaviors of foams and emulsions.

Keywords:
Soy protein Surface tension Adsorption Hydrolysis Viscosity Protein adsorption Chemical engineering Surface charge Chemistry Surface protein Phase (matter) Materials science Composite material Organic chemistry Food science Thermodynamics Physical chemistry

Metrics

1
Cited By
0.00
FWCI (Field Weighted Citation Impact)
15
Refs
0.20
Citation Normalized Percentile
Is in top 1%
Is in top 10%

Citation History

Topics

Proteins in Food Systems
Life Sciences →  Agricultural and Biological Sciences →  Food Science
Food Chemistry and Fat Analysis
Life Sciences →  Agricultural and Biological Sciences →  Food Science
Protein Hydrolysis and Bioactive Peptides
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology

Related Documents

JOURNAL ARTICLE

Hydrolysis of Isolate Soybean Protein Using Subcritical Water

Yun Hee HwangHyung-Yong ChoKo-Rae KimSeok‐Hoon LeeMi‐Jung ChoiJung-Kue Shin

Journal:   Korean Journal of Food Science and Technology Year: 2015 Vol: 47 (6)Pages: 772-778
© 2026 ScienceGate Book Chapters — All rights reserved.