Abstract
Two isoforms of laccase produced from the culture supernatant of Pycnoporus sanguineus were partially purified by phenyl-Sepharose chromatography. Molecular masses of the enzymes were 80 kDa (Lac I) and 68 kDa (Lac II). Optimum activity of Lac I was at pH 4.8 and 30 degrees C, and Lac II was at pH 4.2 and 50 degrees C over 5 min reaction. The Km values of enzymes toward syringaldazine were 10 microM: (Lac I) and 8 microM: (Lac II). Sodium azide inhibited Lac I (85%) and Lac II (75%) activities.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Biotechnology
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Chromatography, Agarose
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Enzyme Induction / drug effects
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Enzyme Stability
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Hydrazones / metabolism
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Hydrogen-Ion Concentration
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Isoenzymes / biosynthesis
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Isoenzymes / chemistry
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Isoenzymes / metabolism
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Kinetics
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Laccase / biosynthesis*
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Laccase / chemistry
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Laccase / metabolism
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Molecular Weight
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Polyporaceae / drug effects*
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Polyporaceae / enzymology*
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Substrate Specificity
Substances
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Hydrazones
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Isoenzymes
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syringaldazine
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Laccase