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Purification and characterization of an extracellular laccase from the anthracene-degrading fungus Fusarium solani MAS2

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Title: Purification and characterization of an extracellular laccase from the anthracene-degrading fungus Fusarium solani MAS2
Authors: Wu, Yi-Rui1 oxwyr@tom.com, Luo, Zhu-Hua1,2, Kwok-Kei Chow, R.1, Vrijmoed, L.L.P.1 bhlilian@cityu.edu.hk
Source: Bioresource Technology. Dec2010, Vol. 101 Issue 24, p9772-9777. 6p.
Subjects: Polycyclic aromatic hydrocarbons, Mangrove plants, Sedimentation & deposition, Acetone, Heavy metals, Biotechnology, Molecular weights, Endoglycosidases
Abstract: Abstract: An extracellular laccase was purified from the culture medium of the non-white rot, anthracene-degrading fungal strain Fusarium solani MAS2. Both native PAGE and SDS–PAGE revealed one single band corresponding to a molecular weight of about 72kDa. Treatment with endoglycosidase H reduced the molecular weight by 12%. The purified laccase maintained stable at pH 3–11 and up to 50°C. The highest activity was detected at pH 3.0 and at 70°C. The enzyme retained 46.2–97.2% of it activity in the presence of 20mM Pb2+, Ni2+, Cr3+, and its activity was enhanced in the presence of 20mM Hg2+. The laccase retained more than 50% of its activity in the presence of 5% acetone, acetonitrile, dimethyl sulphoxide (DMSO), ethanol and methanol. The kinetic constants (K m and k cat) showed that 2,6-dimethoxyphenol (DMOP) and 2,2′-azino-bis-(3-ethylbenzthiazoline-6-sulphonic acid) diammonium salt (ABTS) were the more effective substrates rather than catechol and guaiacol. The novel properties of this laccase suggest its potential for biotechnological and environmental applications. [ABSTRACT FROM AUTHOR]
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Abstract:Abstract: An extracellular laccase was purified from the culture medium of the non-white rot, anthracene-degrading fungal strain Fusarium solani MAS2. Both native PAGE and SDS–PAGE revealed one single band corresponding to a molecular weight of about 72kDa. Treatment with endoglycosidase H reduced the molecular weight by 12%. The purified laccase maintained stable at pH 3–11 and up to 50°C. The highest activity was detected at pH 3.0 and at 70°C. The enzyme retained 46.2–97.2% of it activity in the presence of 20mM Pb2+, Ni2+, Cr3+, and its activity was enhanced in the presence of 20mM Hg2+. The laccase retained more than 50% of its activity in the presence of 5% acetone, acetonitrile, dimethyl sulphoxide (DMSO), ethanol and methanol. The kinetic constants (K m and k cat) showed that 2,6-dimethoxyphenol (DMOP) and 2,2′-azino-bis-(3-ethylbenzthiazoline-6-sulphonic acid) diammonium salt (ABTS) were the more effective substrates rather than catechol and guaiacol. The novel properties of this laccase suggest its potential for biotechnological and environmental applications. [ABSTRACT FROM AUTHOR]
ISSN:09608524
DOI:10.1016/j.biortech.2010.07.091