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

文献类型： 外文期刊

作者： Qiu, Chaoying 1 ; Hu, Xiao 1 ; Li, Laihao 1 ; Yang, Xianqing 1 ; Zhao, Mouming 3 ; Ren, Jiaoyan 3 ;

作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Key Lab Aquat Prod Proc, Minist Agr, Guangzhou 510300, Guangdong, Peoples R China

2.Jinan Univ, Dept Food Sci & Engn, Guangzhou 510632, Guangdong, Peoples R China

3.South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Guangdong, Peoples R China

关键词： Arachin;Conarachin;TGase cross-linking;Structure;Emulsifying properties

期刊名称：EUROPEAN FOOD RESEARCH AND TECHNOLOGY （ 影响因子：2.998； 五年影响因子：3.005 ）

ISSN：

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收录情况： SCI

摘要： 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.

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