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Thermostabilization of porcine kidney D ‐amino acid oxidase by a single amino acid substitution
Author(s) -
Bakke Mikio,
Setoyama Chiaki,
Miura Retsu,
Kajiyama Naoki
Publication year - 2005
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20754
Subject(s) - d amino acid oxidase , amino acid , enzyme , biochemistry , chemistry , bioconversion , mutant , oxidase test , wild type , fermentation , gene
D ‐amino acid oxidase (DAO) is of considerable practical importance, such as bioconversion and enzymatic assay. In this study, we succeeded in obtaining a thermostable mutant DAO from porcine kidney by a single amino acid substitution. This mutant enzyme, F42C, was stable at 55°C, while the wild‐type enzyme was stable only up to 45°C. The K m values of F42C for D ‐amino acids was about half of those of the wild‐type enzyme. This mutant DAO with improved stability and affinity for its substrates is advantageous for the determination of D ‐amino acids. © 2005 Wiley Periodicals, inc.