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Received October 21, 2015
Accepted March 15, 2016
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This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits
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Alkaliphilic lysine decarboxylases for effective synthesis of cadaverine from L-lysine
Department of Chemical Engineering, Kwangwoon University, Seoul 01897, Korea 1R&D Center, Paik Kwang Industrial Co., Ltd., Korea
metalkim@kw.ac.kr
Korean Journal of Chemical Engineering, May 2016, 33(5), 1530-1533(4), 10.1007/s11814-016-0079-5
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Abstract
The enzymatic decarboxylation of L-lysine using lysine decarboxylase is a promising biological approach for producing cadaverine, a versatile platform chemical for bio-polyamides. However, due to the problem with elevated pH in the reaction solution during the enzymatic process, it is desirable to use lysine decarboxylases effectively active in alkaline conditions. In this study, the catalytic properties of three lysine decarboxylases from Selenomonas ruminantium (srLDC), Vibrio vulnificus (vvLDC), and Geobacillus thermodenitrificans (gtLDC) were characterized, and the applicability of the enzymes in alkaline conditions was investigated. Among the three enzymes, only vvLDC exhibited effective activity in alkaline pH conditions. The conversion rate of vvLDC was 1.5-fold higher than that of srLDC and 5.3-fold higher than that of gtLDC in pH 9.0. The results indicate that vvLDC is more advantageous than srLDC and gtLDC for the enzymatic conversion of L-lysine to cadaverine in alkaline conditions.
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