Heterologous expression and characterization of Klebsiella oxytoca lysine decarboxylase.

Author: Naiqiang LI ¹ ; Lijun YU ² ; Yan XU ¹
Author Information

1. Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, Jiangsu, China.
2. Cathay Industrial Biotech Ltd., Shanghai 201203, China.
Publication Type:Journal Article
Keywords: Klebsiella oxytoca; cadaverine; heterologous expression; lysine decarboxylase; pH stability
MeSH: Bacterial Proteins; genetics; metabolism; Cadaverine; Carboxy-Lyases; genetics; metabolism; Escherichia coli; metabolism; Hydrogen-Ion Concentration; Klebsiella oxytoca; enzymology; genetics; Temperature
From: Chinese Journal of Biotechnology 2016;32(4):527-531
CountryChina
Language:Chinese
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.