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  • Title: Improvement in thermal stability and substrate binding of pig kidney D-amino acid oxidase by chemical modification.
    Author: Bakke M, Kajiyama N.
    Journal: Appl Biochem Biotechnol; 2004 Mar; 112(3):123-31. PubMed ID: 15007180.
    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.
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