79-4


Influence of gelling method on gelation ability of soy 7s and 11s globulins

X. Yang1, Y. Li1, F. ZHONG1, and Z. Wang2. (1) Food Science, Southern Yangtze University, 170# Huihe Road, Wuxi, 214036, China, (2) School of Food Science & Technology, Southern Yangtze University, 170 Huihe Rd., Wuxi, Jiangsu Province, 214036, China

Genetic modification of soybean cultivars to remove the allergenic subunits in 7S is one of the important research branches in the field of processing and utilization of soybean recently. As gelling, emulsifying and foaming properties of 7S and 11S are different, this modification would undoubtedly affect the physicochemical functions of soy protein. As soy protein is mainly used as gelling element in food, so the objective of this work is to compare the gelling ability of purified 7S and 11S under different gelling methods, and thus find the suitable coagulant or preheating condition for gelling soy protein from different genetically modified soy cultivars (with different 7S/11S ratio). Soy 7S and 11S components were purified from soy protein isolate and their purity were tested by SDS-PAGE. Gelation properties of soy were studied by dynamic viscoelastic test with rheometer. The results showed that heat-set gel from fully denatured 11S was stronger and more solid-like than that of 7S gel. Under the action of glucono-d-lactone (GDL), gelation speed of 11S was significantly higher than that of 7S, but the gel strength of each was about equal at the later stage. Transglutaminase (TGS) was more effective in gelating 11S; its storage modules was about two times higher than that of 7S gel. Proper papain concentration for inducing stronger gel for 11S was 3 times higher than that of 7S, and it was also true that the strength of 11S gel was higher than 7S gel when the concentration of papain was controlled to be at their each suitable level respectively. These results suggested that for the soy cultivars that had been genetically modified to reduce the 7S content, papain might be an excellent potential coagulator.

Session 79, Food Chemistry: Protein and enzyme chemistry
9:00 AM - 12:00 PM, Thursday AM Room N-120

2004 IFT Annual Meeting, July 12-16 - Las Vegas, NV