Study on mechanism of cross-linking of peanut protein isolate modified with transglutaminase

被引：5

作者：

Sun, Qingjie ^{[1
]}

Xiong, Liu ^{[1
]}

Bu, Xianghui ^{[1
]}

Liu, Yan ^{[1
]}

机构：

[1] Qingdao Agr Univ, Sch Food Sci & Engn, Qingdao 266109, Peoples R China

来源：

ADVANCES IN CHEMICAL ENGINEERING II, PTS 1-4 | 2012年 / 550-553卷

关键词：

Cross-linking; Transglutaminase; Arachin; Conarachin; Peanut Protein Isolate (PPI); CONFORMATION; SPECTROSCOPY;

D O I：

10.4028/www.scientific.net/AMR.550-553.1304

中图分类号：

TQ [化学工业];

学科分类号：

0817 ;

摘要：

The mechanism of cross-linking of peanut protein isolate (PPI) modified with transglutaminase was investigated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier Transformation Infrared (FT-IR) spectra. SDS-PAGE banding patterns indicated that the contents of arachin and conarachin after transglutaminase (TGase) modification were decreased and high molecular weight polymers were formed. SDS-PAGE banding patterns also suggested that cross-linking effects were accomplished in the presence of transglutaminase and the main component participating in cross-linking was arachin. The representative FT-IR spectra of arachin, conarachin modified with TGase treatment appeared the sharp peak at 1680 similar to 1630cm(-1) region, which showed that intramolecular cross-linking was occurred, respectively. Compared with FT-IR spectra of arachin, conarachin modified with TGase treatment, the spectra of PPI modified with TGase treatment appeared two characteristic absorption at 1546.29cm(-1) and 1330.75cm(-1), suggesting that cross-linking was occurred between arachin and conarachin and the epsilon-(gamma-glutamyl) isopeptide bond generated.

引用

页码：1304 / 1308

页数：5

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