3,053
Views
14
CrossRef citations to date
0
Altmetric
Research Paper

Enhanced catalytic efficiency of CotA-laccase by DNA shuffling

&
Pages 182-189 | Received 21 Aug 2018, Accepted 14 May 2019, Published online: 29 May 2019

References

  • Giardina P, Faraco V, Pezzella C, et al. Laccases: a never-ending story. Cell Mol Life Sci. 2010;67:369–385.
  • Claus H. Laccases and their occurrence in prokaryotes. Arch Microbiol. 2003;179:145–150.
  • Baldrian P. Fungal laccases – occurrence and properties. FEMS Microbiol Rev. 2006;30:215–242.
  • Lončar N, Božić N, Lopez-Santin J, et al. Bacillus amyloliquefaciens laccase – from soil bacteria to recombinant enzyme for wastewater decolorization. Bioresour Technol. 2013;147:177–183.
  • Guan ZB, Shui Y, Song CM, et al. Efficient secretory production of CotA-laccase and its application in the decolorization and detoxification of industrial textile wastewater. Environ Sci Pollut Res Int. 2015;22:9515–9523.
  • Brissos V, Pereira L, Munteanu FD, et al. Expression system of CotA-laccase for directed evolution and high-throughput screenings for the oxidation of high-redox potential dyes. Biotechnol J. 2009;4:558–563.
  • Samak NA, Hu J, Wang K, et al. Development of a novel micro-aerobic cultivation strategy for high potential CotA laccase production. Waste Biomass Valorization. 2017;9:369–377.
  • Martins LO, Soares CM, Pereira MM, et al. Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J Biol Chem. 2002;277:18849–18859.
  • Chen Y, Luo Q, Zhou W, et al. Improving the catalytic efficiency of Bacillus pumilus CotA-laccase by site-directed mutagenesis. Appl Microbiol Biotechnol. 2017;101:1935–1944.
  • Koschorreck K, Schmid RD, Urlacher VB. Improving the functional expression of a Bacillus licheniformis laccase by random and site-directed mutagenesis. BMC Biotechnol. 2009;9:12.
  • Brander S, Mikkelsen JD, Kepp KP. Characterization of an alkali- and halide-resistant laccase expressed in E. coli: CotA from Bacillus clausii. PLoS One. 2014;9:e99402.
  • Chong Z, Diao H, Lu F, et al. Degradation of triphenylmethane dyes using a temperature and pH stable spore laccase from a novel strain of Bacillus vallismortis. Bioresour Technol. 2012;126:80–86.
  • Claus H, Filip Z. The evidence of a laccase-like enzyme activity in a Bacillus sphaericus strain. Microbiol Res. 1997;152:209–216.
  • Mohammadian M, Fathi-Roudsari M, Mollania N, et al. Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization. J Ind Microbiol Biotechnol. 2010;37:863–869.
  • Stemmer WP. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc Natl Acad Sci U S A. 1994;91:10747–10751.
  • Fan L, Zhao M, Wang Y. Expression of CotA laccase in Pichia pastoris and its electrocatalytic sensing application for hydrogen peroxide. Appl Microbiol Biotechnol. 2015;99:9483–9493.
  • Chen Y, Luo Q, Zhou W, et al. Improving the catalytic efficiency of Bacillus pumilus CotA-laccase by site-directed mutagenesis. Appl Microbiol Biotechnol. 2017;101:1935.
  • Yup LS, Jong Hyun C, Zhaohui X. Microbial cell-surface display. Trends Biotechnol. 2003;21:45–52.
  • Sheng S, Jia H, Topiol S, et al. Engineering CotA laccase for acidic pH stability using Bacillus subtilis spore display. J Microbiol Biotechnol. 2017;27:507–513.
  • Festa G, Autore F, Fraternali F, et al. Development of new laccases by directed evolution: functional and computational analyses. Proteins. 2008;72:25–34.
  • Koschorreck K, Richter SM, Ene AB, et al. Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids. Appl Microbiol Biotechnol. 2008;79:217–224.
  • Mollania N, Khajeh K, Ranjbar B, et al. Enhancement of a bacterial laccase thermostability through directed mutagenesis of a surface loop. Enzyme Microb Technol. 2011;49:446–452.
  • Guan ZB, Song CM, Zhang N, et al. Overexpression, characterization, and dye-decolorizing ability of a thermostable, pH-stable, and organic solvent-tolerant laccase from Bacillus pumilus W3. J Mol Catal B Enzym. 2014;101:1–6.
  • Spassov VZ, Karshikoff AD, Ladenstein R. The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions. Protein Sci. 1995;4:1516.
  • Lu L, Zhao M, Wang TN, et al. Characterization and dye decolorization ability of an alkaline resistant and organic solvents tolerant laccase from Bacillus licheniformis LS04. Bioresour Technol. 2012;115:35–40.