Identification of novel thermostable ω-transaminase and its application for enzymatic synthesis of chiral amines at high temperature. Issue 73 (21st July 2016)

• Record Type: Journal Article
• Authors: Mathew, Sam; Deepankumar, Kanagavel; Shin, Giyoung; Hong, Eun Young; Kim, Byung-Gee; Chung, Taeowan; Yun, Hyungdon
• Is Part Of: RSC advances. Volume 6:Issue 73(2016)
• Page Start: 69257
• Page End: 69260
• Publication Date: 2016-07-21
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c6ra15110h
• Languages: English
• ISSNs: 2046-2069

Abstract

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. 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.