Purification and Characterization of a Nylon-Degrading Enzyme
作者： Tetsuya Deguchi , Yoshihisa Kitaoka , Masaaki Kakezawa , Tomoaki Nishida
DOI: 10.1128/AEM.64.4.1366-1371.1998
关键词:
摘要: A nylon-degrading enzyme found in the extracellular medium of a ligninolytic culture white rot fungus strain IZU-154 was purified by ion-exchange chromatography, gel filtration and hydrophobic chromatography. The characteristics protein (i.e., molecular weight, absorption spectrum, requirements for 2,6-dimethoxyphenol oxidation) were identical to those manganese peroxidase, which previously characterized as key systems many fungi, this result led us conclude that nylon degradation is catalyzed peroxidase. However, reaction mechanism differed significantly from reported activity did not depend on exogenous H 2 O but nevertheless inhibited catalase, superoxide dismutase strongly. These features are peroxidase-oxidase horseradish In addition, α-hydroxy acids known accelerate peroxidase Degradation nylon-6 fiber also investigated. Drastic regular erosion surface observed, suggesting degraded soluble oligomers selectively.
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