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KMID : 0545120020120060972
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Journal of Microbiology and Biotechnology
2002 Volume.12 No. 6 p.972 ~ p.978
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Purification and Characterization of 2,4-Dichlorophenol Oxidizing Peroxidase from Streptomyces sp. AD001
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JEON, JEONG-HO
HAN, YUN-JON/KANG, TAE-GU/KIM, EUNG-SOO/HONG, SOON-KWANG/JEONG, BYEONG-CHUL
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Abstract
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Streptomyces sp. AD001 is a Gram-positive soil actinomycetes secreting an uncharacterized 2,4-dichlorophenol (DCP) ixidizing enzyme, whose activity is similar to the previously known Actinomycetes lignin-peroxidase (ALiP). This extracelluar peroxidase was purified from Streptomyces sp. AD110 as a single protein band on an SDS-PAGE by ammonium sulfate fractionaion, Q-sepharose, concanavalin A, and Bio-Gel HTP column chromatographies. The molecular mass of the purified peroxidase was determined by SDS-PAGE to be 45.2kDa, and 49.7 kDa with MALDI-TOF-MS, respectively. The highest level of peroxidase activity was observed at pH 7.5 and 30℃. The amino terminal sequence of the purified peroxidase (G-E-P-E-E-G-N-V-D-G-T-L) significant homologies to any known proteins, suggesting that Streptomyces sp. AD001 may secrete a novel kind of bacterial peroxidase. Inditial rate kinetic data of the 2,4-DCP oxidation were best modeled with a random-binding bireactant system.
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