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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 18, No. 6, 2015, pp. 451-458
Bioline Code: ej15076
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 18, No. 6, 2015, pp. 451-458

 en Molecular characterization of a novel thermostable laccase PPLCC2 from the brown rot fungus Postia placenta check for this species in other resources MAD-698-R
An, Hongde; Xiao, Tingting; Fan, Huan & Wei, Dongsheng

Abstract

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 check for this species in other resources 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 constant (kcat) was 1213 ± 18.3 s-1 for ABTS and 293.2 ± 21.9 s-1 for DMP. Km was 22.08 μM for ABTS and 11.62 μM for DMP. The optimal pH for the oxidation of ABTS and DMP was 3.5 and 5.0 respectively. The optimal temperature for the oxidation of ABTS and DMP was 60°C.
Conclusions: This is the first identified thermo activated and thermostable laccase in brown rot fungi. This investigation will contribute to understanding the roles played by laccases in brown rot fungi.

Keywords
Brown rot fungi; Pichia pastoris; Postia placenta; Thermostable laccase

 
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