Purification and characterization of a novel laccase from the mushroom Pleurotus nebrodensis

• Autorzy: Tian G.-T. , Zhang G.-Q. , Wang H.-X. , Ng T. B.
• Języki publikacji: EN

Abstrakty

EN

 A novel laccase with a molecular mass of 64 kDa and the N-terminal sequence AIGPDDTINF was isolated from fresh fruiting bodies of the mushroom Pleurotus nebrodensis. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose, but not on CM-cellulose. It demonstrated an optimal temperature of 70°C. The enzyme activity increased steadily over the temperature range 20°C-70°C. There was only a slight reduction in activity at 80°C. However, all activity disappeared following exposure to 100°C for 10 minutes. The enzyme activity changed only slightly over the pH range 3-5, with the optimum at pH 5, but underwent a precipitous decline when the pH was elevated to 6, and was undetectable at pH 8 and pH 9.

Słowa kluczowe

EN

purification; novel laccase; laccase; mushroom; Pleurotus nebrodensis; enzyme activity

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2012
• Tom: 59
• Numer: 3
• Opis fizyczny: p.407-412,fig.,ref.

Twórcy

autor

Tian G.-T.

• Institute of Biotechnology and Germplasmic Resource, Yunnan Academy of Agricultural Science, Kunming, China

autor

Zhang G.-Q.

autor

Wang H.-X.

autor

Ng T. B.

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