Cloning and expression of thermo-alkali-stable laccase of Bacillus licheniformis in Pichia pastoris and its characterization Article

Lu, L, Wang, TN, Xu, TF et al. (2013). Cloning and expression of thermo-alkali-stable laccase of Bacillus licheniformis in Pichia pastoris and its characterization . 134 81-86. 10.1016/j.biortech.2013.02.015



cited authors

  • Lu, L; Wang, TN; Xu, TF; Wang, JY; Wang, CL; Zhao, M

fiu authors

abstract

  • A thermo-alkali-stable laccase gene from Bacillus licheniformis was cloned and expressed in Pichia pastoris. The recombinant laccase was secreted into the culture medium with a maximum activity of 227.9. U/L. The purified laccase is a monomeric glycoprotein, and its molecular weight was estimated to be 65. kDa on SDS-PAGE after deglycosylation. Optimal enzyme activity was observed at pH 6.2 and 70. °C with syringaldazine as substrate. The recombinant laccase was highly stable in the pH range 7-9 after 10. days at 30. °C. The enzyme displayed remarkable thermostability at 50-70. °C, with a half-life of inactivation at 70. °C of 6.9. h. It also exhibited high tolerance to NaCl and organic solvents like the native spore laccase. The purified laccase could rapidly decolorize reactive blue 19, reactive black 5 and indigo carmine in the presence of acetosyringone. More than 93% of the tested dyes were decolorized in 4. h at pH 9.0. © 2013 Elsevier Ltd.

publication date

  • January 1, 2013

Digital Object Identifier (DOI)

start page

  • 81

end page

  • 86

volume

  • 134