Engineering Transaminase for Stability Enhancement and Site-Specific Immobilization through Multiple Noncanonical Amino Acids Incorporation

Title
Engineering Transaminase for Stability Enhancement and Site-Specific Immobilization through Multiple Noncanonical Amino Acids Incorporation
Author(s)
카나가벨디판쿠마Saravanan Prabhu Nadarajan[Saravanan Prabhu Nadarajan]샘매튜이선구[이선구]유태현[유태현]홍은영[홍은영]김병기[김병기]윤형돈[윤형돈]
Keywords
GREEN FLUORESCENT PROTEIN; OMEGA-TRANSAMINASE; ESCHERICHIA-COLI; GENETIC-CODE; BIOPHYSICAL PROPERTIES; ENZYME MICROREACTOR; POLYSTYRENE BEADS; SYNTHETIC BIOLOGY; ORGANIC-SOLVENT; E. COLI
Issue Date
201502
Publisher
WILEY-V C H VERLAG GMBH
Citation
CHEMCATCHEM, v.7, no.3, pp.417 - 421
Abstract
In general, conventional enzyme engineering utilizes 20 canonical amino acids to alter and improve the functional properties of proteins such as stability, and activity. In this study, we utilized the noncanonical amino acid incorporation technique to enhance the functional properties of -transaminase (-TA). Herein, we enhanced the stability of -TA by residue-specific incorporation of (4R)-fluoroproline [(4R)-FP] and successfully immobilized onto chitosan or polystyrene (PS) beads with site-specifically incorporated L-3,4-dihydroxyphenylalanine (DOPA) moiety. The immobilization of -TAdopa and -TAdp[(4R)-FP] onto PS beads showed excellent reusability for 10 cycles in the kinetic resolution of chiral amines. Compared to the -TAdopa, the -TAdp[(4R)-FP] immobilized onto PS beads exerted more stability that can serve as suitable biocatalyst for the asymmetric synthesis of chiral amines.
URI
http://hdl.handle.net/YU.REPOSITORY/33528http://dx.doi.org/10.1002/cctc.201402882
ISSN
1867-3880
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생명공학부 > 생명공학부 > Articles
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