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Molecular characterization of a novel thermostable laccase PPLCC2 from the brown rot fungus Postia placenta MAD-698-R Electron. J. Biotechnol.
An,Hongde; Xiao,Tingting; Fan,Huan; Wei,Dongsheng.
Background Laccase has been considered important for the degradation of lignocellulose by wood rot fungi. The properties and functions of laccase in white rot fungi have been investigated extensively, but those from brown rot fungi remain largely unknown. In this paper, a laccase isoform Pplcc2 from the brown rot fungus Postia placenta MAD-698-R was expressed heterologously in Pichia pastoris GS115, purified and the properties of the enzyme were determined. Results The molecular weight of the protein was determined to be 67 kDa using SDS-PAGE. It cannot oxidize syringaldazine (SGZ), but it can oxidize 2,2'-azino-di-(3-ethylbenzothialozin-6-Sulfonic acid) (ABTS) and 2,6-dimethoxyphenol (DMP). Specific activity for ABTS was 1960 ± 19 Unit/mg. The catalytic...
Tipo: Journal article Palavras-chave: Brown rot fungi; Pichia pastoris; Postia placenta; Thermostable laccase.
Ano: 2015 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000600011
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