TGase-Catalyzed Glycosylation of Zein

doi:10.7506/spkx1002-6630-201424003

Abstract

Abstract:

In the present work, transglutaminase (TGase) was used to catalyze covalent cross-linking reaction between
zein and glucosamine hydrochloride (GAH). The cross-linking reaction was identified by SDS-PAGE. The reaction
conditions were optimized based on the amount of GAH conjugated onto zein. Meanwhile, the solubility of zein modified
by glycosylation was characterized. The results showed that the optimized reaction conditions for TGase/zein concentration,
zein ratio molar ratio of acyl donor to acceptor, initial reaction pH, temperature and reaction time were 5 g/100 mL, 50 U/g,
1:6, 8.0, 44 ℃ and 7 h respectively. Under these conditions, the amount of GAH conjugated onto zein was (11.34 ± 0.21)
mg/g zein. Compared with intact zein, the solubility of both cross-linked zein and glycosylated zein was improved, and
glycosylation resulted in the highest solubility.

Key words: zein, transglutaminase (TGase), glycosylation, protein modification

CLC Number:

Q814.9

ZHOU Li-min, LIU Xiao-lan, LIU Yue, ZHENG Xi-qun*. TGase-Catalyzed Glycosylation of Zein[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201424003.

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TGase-Catalyzed Glycosylation of Zein

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