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Characterization and homologous overexpression of an N-acetylglucosaminidase Nag1 from Trichoderma reesei.
Chen, Fei; Chen, Xiu-Zhen; Qin, Li-Na; Tao, Yong; Dong, Zhi-Yang.
Afiliación
  • Chen F; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No. 1 West Beichen Road, Chaoyang District, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
  • Chen XZ; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No. 1 West Beichen Road, Chaoyang District, Beijing 100101, China.
  • Qin LN; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No. 1 West Beichen Road, Chaoyang District, Beijing 100101, China.
  • Tao Y; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No. 1 West Beichen Road, Chaoyang District, Beijing 100101, China.
  • Dong ZY; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No. 1 West Beichen Road, Chaoyang District, Beijing 100101, China. Electronic address: dongzy@mail.im.ac.cn.
Biochem Biophys Res Commun ; 459(2): 184-188, 2015 Apr 03.
Article en En | MEDLINE | ID: mdl-25534854
Trichoderma reesei is thought to be a promising recombinant host for the production and secretion of complex proteins due to its ability to secrete large amounts of proteins. In this study we identified a functional N-acetyl-ß-glucosaminidase (NAGase) gene Nag1 in T. reesei. Nag1, a putative gene encoding a GH 20 family NAGase in T. reesei, was cloned and homologous overexpressed in the T. reesei RutC30ΔU3 with a strong cellobiohydrolase1 gene (cbh1) promoter. Nag1 was secreted in its active form and the highest expression level was around 499.85IU/ml. Nag1 has a molecular mass of 80kDa. The optimum pH and temperature were 4.0 and 60°C, respectively.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Acetilglucosaminidasa / Trichoderma / Proteínas Fúngicas Idioma: En Revista: Biochem Biophys Res Commun Año: 2015 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Acetilglucosaminidasa / Trichoderma / Proteínas Fúngicas Idioma: En Revista: Biochem Biophys Res Commun Año: 2015 Tipo del documento: Article País de afiliación: China