Soybean glycinin subunits: Characterization of physicochemical and adhesion properties

被引:64
作者
Mo, Xiaoqun
Zhong, Zhikai
Wang, Donghai
Sun, Xiuzhi [1 ]
机构
[1] Kansas State Univ, Biomat & Technol Lab, BIVAP, Dept Grain Sci & Ind, Manhattan, KS 66506 USA
[2] Kansas State Univ, Dept Biol & Agr Engn, Manhattan, KS 66506 USA
关键词
soybean protein; adhesion strength; pH; thermal properties; hydrophobic amino acids;
D O I
10.1021/jf060780g
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Soybean proteins have shown great potential for applications as renewable and environmentally friendly adhesives. The objective of this work was to study physicochemical and adhesion properties of soy glycinin subunits. Soybean glycinin was extracted from soybean flour and then fractionated into acidic and basic subunits with an estimated purity of 90 and 85%, respectively. Amino acid composition of glycinin subunits was determined. The high hydrophobic amino acid content is a major contributor to the solubility behavior and water resistance of the basic subunits. Acidic subunits and glycinin had similar solubility profiles, showing more than 80% solubility at pH 2.0-4.0 or 6.5-12.0, whereas basic subunits had considerably lower solubility with the minimum at pH 4.5-8.0. Thermal analysis using a differential scanning calorimeter suggested that basic subunits form new oligomeric structures with higher thermal stability than glycinin but no highly ordered structures present in isolated acidic subunits. The wet strength of basic subunits was 160% more than that of acidic subunits prepared at their respective isoelectric points (pI) and cured at 130 degrees C. Both pH and the curing temperature significantly affected adhesive performance. High-adhesion water resistance was usually observed for adhesives from protein prepared at their pI values and cured at elevated temperatures. Basic subunits are responsible for the water resistance of glycinin and are a good starting material for the development of water-resistant adhesives.
引用
收藏
页码:7589 / 7593
页数:5
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