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Kinetic Resolution of 3-Fluoroalanine Using a Fusion Protein ofD-Amino Acid Oxidase withVitroscillaHemoglobin
Author(s) -
Young-Man Seo,
YongHo Khang,
Hyungdon Yun
Publication year - 2011
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.110122
Subject(s) - oxidase test , d amino acid oxidase , fusion protein , chemistry , escherichia coli , fusion , biochemistry , amino acid , recombinant dna , enzyme , gene , linguistics , philosophy
In this study, a fusion protein (VHb-DAAO) of D-amino acid oxidase (DAAO) with Vitreoscilla hemoglobin (VHb) was functionally expressed in Escherichia coli and purified. The k(cat) value VHb-DAAO (47.1 s⁻¹) towards rac-3-flouroalanine was about 2-fold higher than that of DAAO (21.9 s⁻¹). rac-3-Flouroalanine (500 mM) was kinetically resolved into (R)-3-fluoroalanine with high enatiomeric excess (>99%) by VHb-DAAO with about 52% conversion.

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