Work

Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment

Year: 2014

Type: article

Abstract: This study investigated relationship between secondary structure and surface hydrophobicity of soy protein isolate (SPI) subjected to a thermal treatment at 70~90°C. Heat denaturation increased the surface hydrophobicity and surface hydrophobicity decreased as aggregate formed. Heat caused an increase in the relative amount of α -helix structures and an overall decrease in the amount of β -sheet structures when compared with nontreated SPI. The relative amounts of secondary structures varied with time, temperature, and intensity of heat treatment applied. The β -sheet structure was most important for its significant role in denaturation of 7S globulin and following formed aggregates and even in denaturation of 11S globulin. The amount of β -sheet structure in SPI had an inverse correlation with the surface hydrophobicity when the temperature was kept below 90°C. Besides, β -turn structure increased as β -7S/B-11S aggregate formated.

Source: Journal of Chemistry

DOI: 10.1155/2014/475389

Authors: Zhongjiang Wang, Yang Li, Lianzhou Jiang, Baokun Qi, Linyi Zhou

Institution: Northeast Agricultural University

Language: English

Topic: Proteins in Food Systems

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $2,160

Funders: National Natural Science Foundation of China, Northeast Agricultural University