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Effect of transglutaminase cross-linking on the conformational and emulsifying properties of peanut arachin and conarachin fractions

Qiu, Chaoying, Hu, Xiao, Li, Laihao, Yang, Xianqing, Zhao, Mouming, Ren, Jiaoyan
European food research & technology 2017 v.243 no.6 pp. 913-920
chemical elements, crosslinking, emulsifying properties, gel chromatography, hydrophobicity, peanut protein, peanuts, polyacrylamide gel electrophoresis, polymers, protein solubility, protein-glutamine gamma-glutamyltransferase, variance
Peanut protein is widely consumed in many countries of the world. The effects of transglutaminase (TGase)-induced cross-linking on the functional properties of peanut protein fractions of arachin and conarachin were investigated. TGase promoted protein cross-linking and caused lower protein solubility. SDS-PAGE and high-performance size exclusion chromatography displayed that larger polymers or aggregates were formed during TGase treatment and the conarachin fraction was more susceptible to cross-linking than arachin. Conarachin has higher surface hydrophobicity (H ₀) and emulsifying properties than arachin. TGase incubation led to decrease in total free SH content and increase in exposed SH and H ₀ before 90 min treatment, suggesting unfolding of the protein molecules. The emulsifying properties for conarachin were also progressively improved by TGase treatment before 90 min, which was consistent with the change of H ₀. This study presented the variance in structure and emulsifying properties changes between arachin and conarachin fractions and their functional properties change caused by TGase cross-linking.