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Improved cadaverine production from mutant Klebsiella oxytoca lysine decarboxylase
Authors:Naiqiang Li  Howard Chou  Yan Xu
Affiliation:1. Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, P. R. China;2. Cathay Industrial Biotech Ltd, Shanghai, P. R. China
Abstract:Cadaverine has the potential to become an important platform chemical for the production of nylon. Previously, a system that overexpresses the Klebsiella oxytoca lysine decarboxylase in Escherichia coli was engineered. The system was optimized by codon optimization, and tuning the expression level of the gene by testing various promoters and inducer concentrations. Here, we further improved the system by optimizing the sequence located in the region of the ribosome‐binding site in order to enhance translation efficiency. We also identified mutant lysine decarboxylase enzymes that demonstrated enhanced cadaverine‐production ability. Together, these modifications increased cadaverine production in the system by 50%, and the system has a yield of 80% from lysine‐HCl under the conditions we tested. This is the first time that a system to produce cadaverine using the lysine decarboxylase from K. oxytoca performed at a level that is competitive with the traditional systems using the E. coli lysine decarboxylases in both lab‐scale and batch fermentation conditions.
Keywords:Cadaverine  Diamine  Error‐prone PCR mutagenesis  Lysine decarboxylase  Ribosome‐binding site
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