Characterization of a novel halotolerant esterase from Chromohalobacter canadensis isolated from salt well mine
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ORIGINAL ARTICLE
Characterization of a novel halotolerant esterase from Chromohalobacter canadensis isolated from salt well mine Mou Wang1 · Li Ai3 · Mengping Zhang1 · Fengqing Wang1 · Chuan Wang1,2 Received: 30 April 2020 / Accepted: 31 August 2020 / Published online: 14 September 2020 © King Abdulaziz City for Science and Technology 2020
Abstract A esterase gene was characterized from a halophilic bacterium Chromohalobacter canadensis which was originally isolated from a salt well mine. Sequence analysis showed that the esterase, named as EstSHJ2, contained active site serine encompassed by a conserved pentapeptide motif (GSSMG). The EstSHJ2 was classified into a new lipase/esterase family by phylogenetic association analysis. Molecular weight of EstSHJ2 was 26 kDa and the preferred substrate was p-NP butyrate. The EstSHJ2 exhibited a maximum activity at 2.5 M NaCl concentration. Intriguingly, the optimum temperature, pH and stability of EstSHJ2 were related to NaCl concentration. At 2.5 M NaCl concentration, the optimum temperature and pH of EstSHJ2 were 65 ℃ and pH 9.0, and enzyme remained 81% active after 80 ℃ treatment for 2 h. Additionally, the EstSHJ2 showed strong tolerance to metal ions and organic solvents. Among these, 10 mM K+, Ca2+ , Mg2+ and 30% hexane, benzene, toluene has significantly improved activity of EstSHJ2. The EstSHJ2 was the first reported esterase from Chromohalobacter canadensis, and may carry considerable potential for industrial applications under extreme conditions. Keywords Chromohalobacter canadensis · Esterase · Halotolerant · Characteristics
Introduction Lipolytic enzymes, including esterases and lipases, mainly catalyze the hydrolysis and synthesize ester bonds. Lipolytic enzymes carry a conserved motif (Gly-X-Ser-X-Gly) and catalytic active site serine. Based on the specific amino * Chuan Wang [email protected] Mou Wang [email protected] Li Ai [email protected] Mengping Zhang [email protected] Fengqing Wang [email protected] 1
College of Biotechnology, Sichuan University of Science and Engineering, Sichuan Province, No. 180 College Street, Zigong City 643000, China
2
Liquor Making Biological Technology and Application of Key Laboratory of Sichuan Province, Zigong, China
3
Sichuan Technology Business College, Sichuan Province, Chengdu, China
acid sequences and fundamental biological properties, these enzymes can be divided into eight families (Arpigny et al. 1999). Lipolytic enzymes exist in all organisms, and primarily commercial-grade lipidolytic enzymes are acquired from microorganisms. Microbial lipolytic enzymes are the third largest industrial biocatalyst after amylase and protease (Kapoor et al. 2012; Schreck et al. 2014). Owing to their versatile catalytic properties, microbial esterases are used in industries as diverse as pharmaceuticals, cosmetics, food detergents, leather, textiles, paper and biodiesel (Gupta et al. 2004; Hasan et al. 2006). Among the microbial esterases, halotolerant esterases from halophilic microorganisms are of highest va
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