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[产酸克雷伯菌赖氨酸脱羧酶的异源表达及特性研究]

[Heterologous expression and characterization of Klebsiella oxytoca lysine decarboxylase].

作者信息

Li Naiqiang, Yu Lijun, Xu Yan

机构信息

Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, Jiangsu, China.

Cathay Industrial Biotech Ltd., Shanghai 201203, China.

出版信息

Sheng Wu Gong Cheng Xue Bao. 2016 Apr 25;32(4):527-531. doi: 10.13345/j.cjb.150380.

DOI:10.13345/j.cjb.150380
PMID:28853274
Abstract

Cadaverine is a biogenic amine that has the potential to become an important platform chemical for the production of industrial polymers, such as polyamides and polyurethanes. We reported here a lysine decarboxylase from Klebsiella oxytoca. The lysine decarboxylase from Klebsiella oxytoca was cloned to Escherichia coli to get the strain LN18. The specific activity of the crude protein from LN18 reached 30 000 U. The molecular weight was about 80 kDa. The optimum temperature and pH of the crude protein were 55 ℃ and 5.5 respectively. The specific activity could keep over 30% at pH 8.0 compared the one at pH 5.5, much difference from Escherichia coli lysine decarboxylase CadA. Mg²⁺ was positive to the specific activity, whereas Fe²⁺, Zn²⁺ and Ca²⁺ were negative.

摘要

尸胺是一种生物胺,有潜力成为生产工业聚合物(如聚酰胺和聚氨酯)的重要平台化学品。我们在此报道了一株来自产酸克雷伯菌的赖氨酸脱羧酶。将产酸克雷伯菌的赖氨酸脱羧酶克隆到大肠杆菌中,得到菌株LN18。LN18粗蛋白的比活性达到30000 U。分子量约为80 kDa。粗蛋白的最适温度和pH分别为55℃和5.5。与pH 5.5时相比,在pH 8.0时比活性可保持在30%以上,这与大肠杆菌赖氨酸脱羧酶CadA有很大差异。Mg²⁺对比活性有促进作用,而Fe²⁺、Zn²⁺和Ca²⁺则有抑制作用。

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