Production of chiral beta-amino acids using omega-transaminase from Burkholderia graminis

Title
Production of chiral beta-amino acids using omega-transaminase from Burkholderia graminis
Author(s)
정태완샘매튜윤형돈[윤형돈]배한섭[배한섭]Nadarajan[Nadarajan]
Keywords
ORGANIC-SOLVENTS; AMINOTRANSFERASE; CLONING
Issue Date
201502
Publisher
ELSEVIER SCIENCE BV
Citation
JOURNAL OF BIOTECHNOLOGY, v.196, pp.1 - 8
Abstract
Optically pure beta-amino acids are of high pharmacological significance since they are used as key ingredients in many physiologically active compounds. Despite a number of enzymatic routes to these compounds, an efficient synthesis of beta-amino acids continues to pose a major challenge for researchers. omega-Transaminase has emerged as an important class of enzymes for generating amine compounds. However, only a few omega-transaminases have been reported so far which show activity towards aromatic beta-amino acids. In this study, (S)-omega-transaminase from Burkholderia graminis C4D1M has been functionally characterized and used for the production of chiral aromatic beta-amino acids via kinetic resolution. The enzyme showed a specific activity of 3.1 U/mg towards rac-beta-phenylalanine at 37 degrees C. The K-m and K-cat values of this enzyme towards rac-beta-phenylalanine with pyruvate as the amino acceptor were 2.88 mM and 91.57 min(-1) respectively. Using this enzyme, racemic beta-amino acids were kinetically resolved to produce (R)-beta-amino acids with an excellent enantiomeric excess (> 99%) and similar to 50% conversion. Additionally, kinetic resolution of aromatic beta-amino acids was performed using benzaldehyde as a cheapamino acceptor. (C)2015 Elsevier B.V. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/33444http://dx.doi.org/10.1016/j.jbiotec.2015.01.011
ISSN
0168-1656
Appears in Collections:
이과대학 > 화학생화학부 > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE