文献类型：期刊文献

英文题名：Enhancement of the thermal and alkaline pH stability of Escherichia coli lysine decarboxylase for efficient cadaverine production

作者：Kou, Fengyu[1];Zhao, Jing[1];Liu, Jiao[1];Sun, Cunmin[1];Guo, Yanmei[1];Tan, Zijian[1];Cheng, Feng[2];Li, Zhimin[3];Zheng, Ping[1];Sun, Jibin[1]

机构：[1]Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Key Lab Syst Microbial Biotechnol, Tianjin 300308, Peoples R China;[2]Zhejiang Univ Technol, Coll Biotechnol & Bioengn, Hangzhou 310014, Zhejiang, Peoples R China;[3]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2018

卷号：40

期号：4

起止页码：719

外文期刊名：BIOTECHNOLOGY LETTERS

收录：;EI(收录号：20180404676705);WOS:【SCI-EXPANDED(收录号:WOS:000428052600013)】；

基金：We are grateful for the financial support from the Tianjin Municipal City, the first "Special Support Plan for Talents Development" and "High-level Innovation and Entrepreneurship Team", National Natural Science Foundation of China (Nos. 21606251, 31370113, and 31370829), Science and Technology Foundation for Selected Overseas Chinese Scholar of Tianjin (2017), and Science and Technology Project of Tianjin (15PTCYSY00020).

语种：英文

外文关键词：Biotransformation; Cadaverine; Lysine decarboxylase; Multimeric interface; Stability

摘要：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. The mutant T88S was designed for improved structural stability by computational analysis. The optimal pH and temperature of T88S were 7.0 and 55 A degrees C (5.5 and 50 A degrees C for wild-type). T88S showed higher thermostability with a 2.9-fold increase in the half-life at 70 A degrees C (from 11 to 32 min) and increased melting temperature (from 76 to 78 A degrees C). Additionally, the specific activity and pH stability (residual activity after 10 h incubation) of T88S at pH 8.0 were increased to 164 U/mg and 78% (58 U/mg and 57% for wild-type). The productivity of cadaverine with T88S (284 g l-lysine L-1 and 5 g DCW L-1) was 40 g L-1 h(-1), in contrast to 28 g L-1 h(-1) with wild-type. The mutant T88S showed high thermostability, pH stability, and activity at alkaline pH, indicating that this mutant is a promising biocatalyst for industrial production of cadaverine.