Simultaneous purification and reversible immobilization of D-amino acid oxidase from Trigonopsis variabilis on a hydrophobic support.

Abstract

Purification and reversible immobilization of D-amino acid oxidase from Trigonopsis variabilis could be simultaneously accomplished by hydrophobic interaction on Phenyl Sepharose CL-4B in the presence of 50 mM pyrophosphate buffer (pH 8.5). The presence of a high salt concentration of 2 M, which is generally required for the hydrophobic interactions, was… (More)

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