Separation and characterization of two extracelluar H2O2‐dependent oxidases from ligninolytic cultures of Phanerochaete chrysosporium

FEBS Letters

Glenn, Jeffrey K.¹  Morgan, Meredith A.¹  Kuwahara, Masaaki¹  Gold, Michael H.¹ 

[1] Department of Chemistry and Biochemical Sciences, Oregon Graduate Center, 19600 N.W. Walker Road, Beaverton, OR 97006, USA

关键词: Oxidase;    Lignin degradation;    Basidiomycete;    Diarylpropane;    Hydrogen peroxide;    Ethylene;    KTBA;    2-keto-4-thiomethylbutyric acid;    TMS;    trimethylsilyl;   

DOI  :  10.1016/0014-5793(84)80327-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two H₂O₂-dependent oxidases found in the extracellular medium of the white rot fungus Phanerochaete chrysosporium were separated by chromatography on blue agarose. The first enzyme fraction to elute from the column generated ethylene from 2-keto-4-thiomethylbutyric acid (KTBA) in the presence of veratryl alcohol, and catalyzed the α,β cleavage of the diarylpropane 1-(3,4-diethoxyphenyl)1,3-dihdyroxy-(4-methoxyphenyl)propane (I). During the diarylpropane cleavage, ¹⁸O from ¹⁸O₂ was incorporated specifically into the α-position of the product 1-(4-methoxyphenyl)1,2-dihdyroxyethane (III), suggesting that this enzyme is an H₂O₂-dependent oxygenase. The second enzyme which binds to blue agarose is an Mn²⁺-dependent, lactate-activated peroxidase. The enzyme catalyzed the oxidation of phenol red, o-dianisidine, Poly R, and a variety of other dyes. It was also capable of decarboxylating vanillic acid.

【 授权许可】

Unknown