Properties of Biopolymers from Cross‐linking Whey Protein Isolate and Soybean 11S Globulin
Authors:
- 1 November 1996
- journal article
- Published by Wiley in Journal of Food Science
- Vol. 61 (6) , 1129-1132
Abstract
Biopolymers were prepared by cross‐linking whey protein isolate (WPI) and soybean 11S using transglutaminase. Electrophoretic pattern, solubility, emulsification, hydrophobicity and foaming properties of the biopolymers were determined. SDS‐PAGE showed bands corresponding to high‐molecular‐weight components (MW>200 kDa). Biopolymer solubility was > 90% at pH 3 and below, and at pH 7 and above. Emulsifying properties of biopolymers were lower than those of WPI. The foaming capacity of the biopolymers (23.6 mL) and WPI/11S mixture (22.7 mL) were similar to that of egg albumin (20.3 mL). The foaming stability of the biopolymers (122 min) was higher than that of WPI/11S mixture (33.7 min), and was similar to that of egg albumin (132 min).Keywords
This publication has 15 references indexed in Scilit:
- Modification Reactions and Protein Structure1994
- Crosslinking of Whey Protein by TransglutaminaseJournal of Dairy Science, 1990
- Interfaces, Protein Films, and Foams1990
- Solubility, Emulsifying, and Foaming Properties of Rice Bran Protein ConcentratesJournal of Food Science, 1989
- Gelation of casein and soybean globulins by transglutaminase.Agricultural and Biological Chemistry, 1985
- Functional properties of food proteins polymerized by transglutaminase.Agricultural and Biological Chemistry, 1984
- Functional properties of proteins: Possible relationships between structure and function in foamsFood Chemistry, 1981
- Emulsifying properties of proteins: evaluation of a turbidimetric techniqueJournal of Agricultural and Food Chemistry, 1978
- Major proteins of soybean seeds. A straightforward fractionation and their characterizationJournal of Agricultural and Food Chemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970