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Heterologous Expression and Purification of Zea mays Transglutaminase in Pichia pastoris
Hongbo Li,Yanhua Cui,Lanwei Zhang,Huaxi Yi,Xue Han,Yuehua Jiao,Ming Du,Rongbo Fan,Shuang Zhang 한국식품과학회 2014 Food Science and Biotechnology Vol.23 No.5
Transglutaminases (TGases) are a family ofenzymes that catalyze the cross-linking of proteins and arewidely used in the food industry to improve the texture ofdairy, meat, and bread products. Zea mays transglutaminase(TGZ) is a new type of TGase with a wide potential. TGZwas expressed in the yeast Pichia pastoris under an alcoholoxidase promoter. Maximal expression of recombinantTGZ was achieved by inducing recombinant GS115(pPIC9K-tgz) in BMMY medium using 1.5% methanol for96 h. Secreted TGZ was initially separated using Superdex200 resin and further purified on cation exchange resin. The activity of TGZ following purification was 0.32 U/mgof protein. The polymerization effect of TGZ on caseincatalyzed by recombinant TGZ was slightly lower than theeffect of microbial transglutaminase (MTG). TGZ is a newpotential additive for the food industry.