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Enhancement of the thermal and alkaline pH stability of Escherichia coli lysine decarboxylase for efficient cadaverine production.

Biotechnology letters - 1 Apr 2018

Kou Fengyu, Zhao Jing, Liu Jiao, Sun Cunmin, Guo Yanmei, Tan Zijian, Cheng Feng, Li Zhimin, Zheng Ping, Sun Jibin

Abstract excerpt

OBJECTIVE: To enhance the thermal and alkaline pH stability of the lysine decarboxylase from Escherichia coli (CadA) by engineering the decameric interface and explore its potential for industrial applications. RESULTS: The mutant T88S was designed for improved structural stability by computational analysis. The optimal pH and temperature of T88S were 7.0 and 55 °C (5.5 and 50 °C for wild-type). T88S showed...

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PMID: 29349625
DOI: 10.1007/s10529-018-2514-7

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