Cloning and characterization of CotA laccase from Bacillus subtilis WD23 decoloring dyes

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• 作者：Chunlei Wang ; Daizong Cui ; Lei Lu ; Ning Zhang ; Hongyi Yang…
• 关键词：Bacillus subtilis ; CotA Laccase ; Dye decolorization ; Expression ; Mediator
• 刊名：Annals of Microbiology
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：66
• 期：1
• 页码：461-467
• 全文大小：551 KB
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• 作者单位：Chunlei Wang (1) (2)
  Daizong Cui (1)
  Lei Lu (1)
  Ning Zhang (3)
  Hongyi Yang (1)
  Min Zhao (1)
  Shaojun Dai (2)
  
  1. College of Life Sciences, Northeast Forestry University, Harbin, 150040, China
  2. Key Laboratory of Saline-Alkali Vegetation Ecology Restoration in Oil Field, Alkali Soil Natural Environmental Science Center, Northeast Forestry University, Harbin, 150040, China
  3. Heilongjiang Dairy Industry Technology Development Center, Harbin, 150028, China
  
• 刊物主题：Microbiology; Microbial Genetics and Genomics; Microbial Ecology; Fungus Genetics; Medical Microbiology; Applied Microbiology;
• 出版者：Springer Berlin Heidelberg
• ISSN：1869-2044

文摘

CotA protein is a component of the endospore coat of Bacillus subtilis and it exhibits the activities of laccase. CotA protein is known as CotA laccase. A CotA laccase gene from B. subtilis WD23 was cloned and expressed in Escherichia coli. The expressed CotA laccase was observed in an active form. The molecular weight of CotA laccase was estimated to be 67.5 kDa. Optimal laccase activity was detected at pH 7.2 and 45 °C with syringaldazine as substrate. The half-life of the laccase was 1.5 h at 80 °C at the optimum pH. Half of the laccase activity was lost after 8 h at 45 °C and pH 9.0. The CotA laccase exhibited high tolerance to acetone, petroleum ether, ethyl acetate and chloroform, like spore laccase. Purified CotA laccase was activated 157 % by Cu2+ and remained stable to Fe2+. The purified CotA laccase could decolorize 87 % of Remazol Brilliant Blue R (RBBR) and 81 % of Congo Red in 6 h in absence of any mediator. Keywords Bacillus subtilis CotA Laccase Dye decolorization Expression Mediator