Issue 73, 2016, Issue in Progress
From the journal:

RSC Advances

Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature†

Sam Mathew,a   Kanagavel Deepankumar,b   Giyoung Shin,c   Eun Young Hong,d   Byung-Gee Kim,d   Taeowan Chunge  and  Hyungdon Yun*a  

* Corresponding authors

a Department of Bioscience & Biotechnology, Konkuk University, Seoul, South Korea
E-mail: hyungdon@konkuk.ac.kr

b School of Materials Science and Engineering, Biological & Biomimetic Material Laboratory, Nanyang Technological University, Singapore

c School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang, Gyeongbuk, Republic of Korea

d School of Chemical and Biological Engineering, Seoul National University, Seoul, South Korea

e School of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk, South Korea

Abstract

A novel thermostable ω-transaminase from Thermomicrobium roseum which showed broad substrate specificity and high enantioselectivity was identified, expressed and biochemically characterized. The advantage of this enzyme to remove volatile inhibitory by-products was demonstrated by performing asymmetric synthesis and kinetic resolution at high temperature.

Graphical abstract: Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature

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Article information

DOI
https://doi.org/10.1039/C6RA15110H
Article type
Communication
Submitted
10 Jun 2016
Accepted
13 Jul 2016
First published
13 Jul 2016

RSC Adv., 2016,6, 69257-69260

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Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature

S. Mathew, K. Deepankumar, G. Shin, E. Y. Hong, B. Kim, T. Chung and H. Yun, RSC Adv., 2016, 6, 69257 DOI: 10.1039/C6RA15110H

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