title: Expression and characterization of LacMP, a novel fungal laccase of Moniliophthora perniciosa FA553.
abstract: OBJECTIVE
  To characterize a putative laccase gene, LacMP, of Moniliophthora perniciosa FA553 that had been screened using a genome mining approach, then cloned and expressed in Pichia pastoris.
  
  
  RESULTS
  The purified recombinant LacMP was ~57 kDa with a maximum laccase activity of 232 U/l. The optimal pH for oxidation reactions with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), syringaldazine, guaiacol and 2,6-dimethoxyphenol, were 6, 7.5, 6.5, and 6.5, respectively. The laccase activity was optimal at 60, 45, 45, and 55 °C for the four respective substrates. LacMP was stable at pH 6-8 and <30 °C. Li(+), K(+), Co(2+), Ni(2+), Mn(2+), and Mg(2+) at 1 mM had no obvious effect on its activity.
  
  
  CONCLUSIONS
  Given that LacMP has optimal activity under neutral and alkaline oxidation reaction conditions, it could be a potential candidate for industrial biocatalytic applications.
authors.affiliation: School of Bioscience and Bioengineering, South China University of Technology, Guangzhou, 510006, Guangdong, China, hping.liu@foxmail.com.
authors.forename: Huiping
authors.initials: H
authors.lastname: Liu
authors.forename: Chaofan
authors.initials: C
authors.lastname: Tong
authors.forename: Bing
authors.initials: B
authors.lastname: Du
authors.forename: Shuli
authors.initials: S
authors.lastname: Liang
authors.forename: Ying
authors.initials: Y
authors.lastname: Lin
mesh_terms: D000363:Agaricales / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D042845:Laccase / Q000235:genetics* / Q000378:metabolism*; D010843:Pichia / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D011994:Recombinant Proteins; D042845:Laccase