Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature-Reference-Cited by-同舟云学术

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

Published:2016 Issue:73 Volume:6 Page:69257-69260
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Mathew Sam¹²³⁴,Deepankumar Kanagavel⁵⁶⁷⁸,Shin Giyoung⁹¹⁰¹¹¹²,Hong Eun Young¹³¹⁴³⁴,Kim Byung-Gee¹³¹⁴³⁴,Chung Taeowan¹⁵¹⁶¹⁷⁴,Yun Hyungdon¹²³⁴

Affiliation:

1. Department of Bioscience & Biotechnology

2. Konkuk University

3. Seoul

4. South Korea

5. School of Materials Science and Engineering

6. Biological & Biomimetic Material Laboratory

7. Nanyang Technological University

8. Singapore

9. School of Interdisciplinary Bioscience and Bioengineering

10. Pohang University of Science and Technology

11. Pohang

12. Republic of Korea

13. School of Chemical and Biological Engineering

14. Seoul National University

15. School of Biotechnology

16. Yeungnam University

17. Gyeongsan

Abstract

A novel thermostable ω-transaminase from Thermomicrobium roseum showing broad substrate specificity and high enantioselectivity was identified, expressed and biochemically characterized and it could produce chiral amines at high temperature.

Funder

National Research Foundation of Korea

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/RA/C6RA15110H

Reference24 articles.

1. Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications

2. Biocatalytic Approaches to the Synthesis of Enantiomerically Pure Chiral Amines

3. Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis

4. Features and technical applications of ω-transaminases

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