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

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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°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°C at pH 6.0, while the conjugated enzyme was stable even at 70°C. In addition, the conjugated enzyme showed decreased K m values for d-amino acids. Because of these outstanding charcteristics, this new material is expected to be available for use as a liquid assay reagent.

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Authors and Affiliations

  1. Research and Development Division, Kikkoman Corporation, 399 Noda, 278-0037, Noda City, Chiba, Japan

    Mikio Bakke & Naoki Kajiyama

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  1. Mikio Bakke
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  2. Naoki Kajiyama
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Correspondence to Mikio Bakke.

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Bakke, M., Kajiyama, N. Improvement in thermal stability and substrate binding of pig kidney d-amino acid oxidase by chemical modification. Appl Biochem Biotechnol 112, 123–131 (2004). https://doi.org/10.1385/ABAB:112:3:123

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  • DOI: https://doi.org/10.1385/ABAB:112:3:123

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