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KMID : 0545120060160111832
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Journal of Microbiology and Biotechnology
2006 Volume.16 No. 11 p.1832 ~ p.1836
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Screening and Purification of a Novel Transaminase Catalyzing the Transamination of Aryl β-Amino Acid from Mesorhizobium sp. LUK
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Kim Ju-Han
Kyung Do-Hyun
Yun Hyung-Don
Cho Byung-Kwan
Kim Byung-Gee
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Abstract
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Mesorhizobium sp. LUK, which utilizes 3-amino-3-phenylpropionic acid as the sole source of nitrogen with high enantioselectivity (E(S)>100), was isolated using enrichment culture. The enzyme involved in the utilization of (S)-3-amino-3-phenylpropionic acid was confirmed to be a transaminase and was purified by 235-folds with a specific activity of 0.72 U/mg. The molecular weight of the purified protein was ca. 47 kDa and the active enzyme was determined as a dimer on gel filtration chromatography. The N-terminal sequence was obtained from the purified protein. Spontaneous decarboxylation of produced acids was observed during the chiral resolution of 3-amino-3-phenylpropionic acid.
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KEYWORD
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Transaminase, β-amino acid, 3-amino-3-phenylpropionic acid, Mesorhizobium sp. LUK
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