Purification and Properties of Laccase Produced from a White Rot Fungus (W-1)
CongBao Kang
Abstract
CongBao Kang
Abstract
The laccase was purified from a white rot fungus by ultrafiltration, Bio-gel P-100 and DEAE-Sephadex A-50 chromatography. The molecular weight of the purified laccase was determined as about 62^4 kD by SDS-PAGE. Its pI was determined to be 3.5 by IFE-PAGE. The optimum pH and temperature for laccase activity were 4.5 and 50℃, respectively. The laccase catalyzed the oxidation of 2,6-dimethoxyphenol with a Michaelis constant of 3.84×10 -5 mol/L. Various metal ions showed different effects on the activity. The activity was enhanced by K +, Mn 2+ and Ag +,and was strongly inhibited by Fe 2+, Fe 3+, Hg 2+, Co 2+ and Ba 2+. The laccase also had the ability to decolorize some dyes such as Remazol brilliant blue R and carmoisine.
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The laccase was purified from a white rot fungus by ultrafiltration, Bio-gel P-100 and DEAE-Sephadex A-50 chromatography. The molecular weight of the purified laccase was determined as about 62^4 kD by SDS-PAGE. Its pI was determined to be 3.5 by IFE-PAGE. The optimum pH and temperature for laccase activity were 4.5 and 50℃, respectively. The laccase catalyzed the oxidation of 2,6-dimethoxyphenol with a Michaelis constant of 3.84×10 -5 mol/L. Various metal ions showed different effects on the activity. The activity was enhanced by K +, Mn 2+ and Ag +,and was strongly inhibited by Fe 2+, Fe 3+, Hg 2+, Co 2+ and Ba 2+. The laccase also had the ability to decolorize some dyes such as Remazol brilliant blue R and carmoisine.
Key concepts: Laccase, Sephadex, Ultrafiltration (renal), Chemistry, Nuclear chemistry, Chromatography, Metal ions in aqueous solution, Metal