• Microbiology and Biotechnology Letters
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• v.30 no.3
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• pp.287-292
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• 2002

Lignin-peroxidase (LiP) has been considered as one of the most important industrial enzymes for biodegradation of various recalcitrant toxic compounds such as chlorinated aromatic hydrocarbons and azo-dyes. Recently, several soil actinomycetes have been reported to secrete a functionally-similar lignin-peroxidase called actinomycetes lig-nin-peroxidase (ALiP). In this manuscript, we isolated over 100 morphologically distinct actinomycetes from the contaminated soils around 10 different gas stations located nearby the Kyung-An river. Among these actinomycetes screened based on the congo-red dye-decolorization activities, one newly-isolated actinomycetes named SMA-2 showed the most significant dye-decoloring activity on the congo-red plate as well as a significant ALiP activity in a yeast-extract-malt-extract liquid media supplemented with starch. The optimum SMA-2 culture condition fur ALiP production was determined and the kinetic parameters fur the SMA-2 AkIP activity were characterized. The optimally-cultured SMA-2 also exhibited the oxidation activities toward various recalcitrant aromatic compounds including phenol, 2- chlorophenol, 4- chlorophenol, 2,4- dichlorophenol ,2,6- dichlorophenol, and 2,4, f-trichlorophe - not, suggesting a potential application of SMA-2 for contaminated soil bioremediation.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.877-880
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• 1999

Over 50 morphologically distinctive soil Streptomyces were isolated from various Jocations in the Yongin area in Korea and visually screened for dye-decoloring activities on an agar plate. Two Streptomyces species (AD001 and ND002) showed strong dye-decoloring activities on the plate containing congo-red and new-fuchin dyes, respectively. Also, the liquid culture supernatants of these species showed 2,4-dicholophenol (DCP) oxidation activities only in the presence of hydrogen peroxide, a characteristic of Actinomycetes lignin-peroxidase (ALiP)-P3 isoform found in dye-degrading S. viridosporus T7A and S. badius 252. Based on their dye-decoloring capabilities and the 2,4-DCP oxidation kinetic data, it is suggested that these Streptomyces secrete not-yet-characterized extracelluar enzyme(s), whose activities are very similar to the ALiP-P3 enzyme.

• Journal of Microbiology and Biotechnology
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• v.12 no.6
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• pp.972-978
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• 2002

Streptomyces sp. AD001 is a Gram-positive soil actinomycetes secreting an uncharacterized 2,4-dichlorophenol (DCP) oxidizing enzyme, whose activity is similar to the previously known Actinomycetes lignin-peroxidase (ALiP). This extracellular peroxidase was purified from Streptomyces sp. AD001 as a single protein band on an SDS-PACE by ammonium sulfate fractionation, Q-sepharose, concanavalin A, and Bio-Gel HTP column chromatographies. The molecular mass of the purified peroxidase was determined by SDS-PAGE to be 45.2 kDa, and 49.7 kDa with MALDI-TOF-MS, respectively. The highest level of peroxidase activity was observed at pH 7.5 and $30^{\circ}C$. The amino terminal sequence of the purified peroxidase (G-E-P-E-E-G-N-V-D-G-T-L) showed no significant homologies to my known proteins, suggesting that Streptomyces sp. AD001 may secrete a novel kind of bacterial peroxidase Initial rate kinetic data of the 2,4-DCP oxidation were best modeled with a random-binding bireactant system.