Improvement in thermal stability and substrate binding of pig kidney D-amino acid oxidase by chemical modification.

Abstract:

:Chemical modification was evaluated to stabilize pig kidney D-amino acid oxidase (pkDAAO), which is required for analytical determination of D-amino acids. Optimization of modification conditions was performed to obtain high recovery yield and stability, and chemical modification at 30 degrees C for 12 h with a highly concentrated enzyme solution gave dextran-conjugated pkDAAO with a 70% yield of activity. pkDAAO was stable at less than 55 degrees C at pH 6.0, while the conjugated enzyme was stable even at 70 degrees C. In addition, the conjugated enzyme showed decreased Km values for D-amino acids. Because of these outstanding characteristics, this new material is expected to be available for use as a liquid assay reagent.

authors

Bakke M,Kajiyama N

doi

10.1385/abab:112:3:123

subject

Has Abstract

pub_date

2004-03-01 00:00:00

pages

123-31

issue

3

eissn

0273-2289

issn

1559-0291

pii

ABAB:112:3:123

journal_volume

112

pub_type

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