Heterologous expression and purification of Zea mays transglutaminase in Pichia pastoris

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• 作者：Hongbo Li (1)
  Yanhua Cui (1)
  Lanwei Zhang (1)
  Huaxi Yi (1)
  Xue Han (1)
  Yuehua Jiao (1)
  Ming Du (1)
  Rongbo Fan (1) (2)
  Shuang Zhang (1)
  
• 关键词：Zea mays transglutaminase ; Pichia pastoris GS115 ; protein expression ; purification ; polymerization effect
• 刊名：Food Science and Biotechnology
• 出版年：2014
• 出版时间：October 2014
• 年：2014
• 卷：23
• 期：5
• 页码：1507-1513
• 全文大小：444 KB
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• 作者单位：Hongbo Li (1)
  Yanhua Cui (1)
  Lanwei Zhang (1)
  Huaxi Yi (1)
  Xue Han (1)
  Yuehua Jiao (1)
  Ming Du (1)
  Rongbo Fan (1) (2)
  Shuang Zhang (1)
  
  1. School of Food Science and Engineering, Harbin Institute of Technology, Harbin, Heilongjiang, 150090, China
  2. College of Food Science & Engineering, Qingdao Agricultural University, Qingdao, Shandong, 266109, China
  
• ISSN：2092-6456

文摘

Transglutaminases (TGases) are a family of enzymes that catalyze the cross-linking of proteins and are widely used in the food industry to improve the texture of dairy, meat, and bread products. Zea mays transglutaminase (TGZ) is a new type of TGase with a wide potential. TGZ was expressed in the yeast Pichia pastoris under an alcohol oxidase promoter. Maximal expression of recombinant TGZ was achieved by inducing recombinant GS115 (pPIC9K-tgz) in BMMY medium using 1.5% methanol for 96 h. Secreted TGZ was initially separated using Superdex 200 resin and further purified on cation exchange resin. The activity of TGZ following purification was 0.32 U/mg of protein. The polymerization effect of TGZ on casein catalyzed by recombinant TGZ was slightly lower than the effect of microbial transglutaminase (MTG). TGZ is a new potential additive for the food industry.