Cloning and identification of a novel tyrosinase and its overexpression in Streptomyces kathirae SC-1 for enhancing melanin production

被引：24

作者：

Guo, Jing ^{[1
,2
]}

Rao, Zhiming ^{[1
,2
]}

Yang, Taowei ^{[1
,2
]}

Man, Zaiwei ^{[1
,2
]}

Xu, Meijuan ^{[1
,2
]}

Zhang, Xian ^{[1
,2
]}

Yang, Shang-Tian ^{[3
]}

机构：

[1] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China

[2] Jiangnan Univ, Sch Biotechnol, Key Lab Ind Biotechnol, Minist Educ, Wuxi 214122, Jiangsu, Peoples R China

[3] Ohio State Univ, Dept Chem & Biomol Engn, Columbus, OH 43210 USA

来源：

FEMS MICROBIOLOGY LETTERS | 2015年 / 362卷 / 08期

基金：

中国国家自然科学基金;

关键词：

Streptomyces kathirae; melanin production; tyrosinase; enzyme properties; gene cloning; gene expression; BACILLUS-THURINGIENSIS; PURIFICATION; GENE; BIOSYNTHESIS; EXPRESSION; COMPLEX; STRAIN;

D O I：

10.1093/femsle/fnv041

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A 30-kDa novel tyrosinase was purified to homogeneity. The K-m for L-Dopa and L-tyrosine were determined as 0.42 and 0.25mM. The 1231 bp (base pair) melC gene and its 167 bp promoter P-skmel were obtained by thermal asymmetric interlaced polymerase chain reaction based on the amino acids fragment obtained from MS results of the purified enzyme. The protein sequence of tyrosinase shows maximum identity (84%) to tyrosinase from Streptomyces galbus. The melC was introduced into S. kathirae. The melanin production and the transcriptional level of melC in recombinant S. kathirae [pIJP(skmel)melC] were about 2.1-fold and 2-fold higher than the wild-type strain, respectively. The melanin concentration was maximized at 28.8 g L-1.

引用

页数：7

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