Purification and characterization of sulochrin oxidase from Penicillium frequentans.

…, K MIKAWA, I FUJII, Y EBIZUKA, U SANKAWA

Index: Huang, Ke-Xue; Yoshida, Yasunori; Mikawa, Kazunobu; Fujii, Isao; Ebizuka, Yutaka; Sankawa, Ushio Biological and Pharmaceutical Bulletin, 1996 , vol. 19, # 1 p. 42 - 46

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Citation Number: 8

Abstract

Sulochrin oxidase, an enzyme catalyzing regio-and stereospecific phenol oxidative coupling reaction to form (+)-bisdechlorogeodin from sulochrin, was isolated from Penicillium frequentans CMI 96659. By chromatographies on DEAE-cellulose, hydroxyapatite, Phenyl- Sepharose, Mono P, Mono Q, and HPLC gel filtration columns, sulochrin oxidase was purified to apparent homogeneity. The purified enzyme had a molecular weight of 230 K ...