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  • 标题:Molecular Characterization and Directed Evolution of a Metagenome-Derived l-Cysteine Sulfinate Decarboxylase
  • 本地全文:下载
  • 作者:Deng, Jie ; Wu, Qiaofen ; Gao, Hua
  • 期刊名称:Food Technology and Biotechnology
  • 印刷版ISSN:1330-9862
  • 电子版ISSN:1334-2606
  • 出版年度:2018
  • 卷号:56
  • 期号:1
  • 页码:117-123
  • DOI:10.17113/ftb.56.01.18.5415
  • 语种:English
  • 出版社:Sveuciliste u Zagrebu - Faculty of Food
  • 摘要:L-Cysteine sulfinate decarboxylase (CSD, EC 4.1.1.29), the rate-limiting enzyme in taurine synthesis pathway, catalyzes L-cysteine sulfinic acid to form hypotaurine. Identification of the novel CSD that could improve the biosynthetic efficiency of taurine is important. An unexplored decarboxylase gene named undec1A was identified in a previous work through sequence-based screening of uncultured soil microorganisms. Random mutagenesis through sequential error-prone polymerase chain reaction was used in Undec1A. A mutant Undec1A-1180, which was obtained from mutagenesis library, had 5.62-fold higher specific activity than Undec1A at 35 °C and pH=7.0. Molecular docking results indicated that amino acid residues Ala235, Val237, Asp239, Ile267, Ala268, and Lys298 in the Undec1A-1180 protein helped recognize and catalyze the substrate molecules of L-cysteine sulfinic acid. These results could serve as a basis for elucidating the characteristics of the Undec1A-1180. Directed evolution technology is a convenient way to improve the biotechnological applications of metagenome-derived genes.
  • 关键词:taurine; L-cysteine sulfinate decarboxylase; metagenomic library; sequential error-prone PCR
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