Characterization of a novel halotolerant esterase from Chromohalobacter canadensis isolated from salt well mine

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...

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Published in3 Biotech Vol. 10; no. 10; p. 430
Main Authors Wang, Mou, Ai, Li, Zhang, Mengping, Wang, Fengqing, Wang, Chuan
Format Journal Article
LanguageEnglish
Published Cham Springer International Publishing 01.10.2020
Springer Nature B.V
Subjects
Agriculture
Association analysis
Benzene
Bioinformatics
Biomaterials
Biotechnology
Calcium
Calcium ions
Cancer Research
Chemistry
Chemistry and Materials Science
Esterase
Industrial applications
Lipase
Magnesium
Metal ions
Molecular weight
Original
Original Article
pH effects
Phylogeny
Salinity tolerance
Sequence analysis
Serine
Sodium chloride
Stem Cells
Substrates
Toluene
Esterase
Characteristics
Halotolerant
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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 + , Ca 2+  , Mg 2+  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.
AbstractList 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 + , Ca 2+  , Mg 2+  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.
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.
ArticleNumber 430
Author Wang, Fengqing
Wang, Mou
Wang, Chuan
Ai, Li
Zhang, Mengping
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  organization: Sichuan Technology Business College, Sichuan Province
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  fullname: Zhang, Mengping
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  givenname: Fengqing
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  surname: Wang
  fullname: Wang, Chuan
  email: watpc57944@163.com
  organization: College of Biotechnology, Sichuan University of Science and Engineering, Sichuan Province, Liquor Making Biological Technology and Application of Key Laboratory of Sichuan Province
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Snippet A esterase gene was characterized from a halophilic bacterium Chromohalobacter canadensis which was originally isolated from a salt well mine. Sequence...
A esterase gene was characterized from a halophilic bacterium Chromohalobacter canadensis which was originally isolated from a salt well mine. Sequence...
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SubjectTerms Agriculture
Association analysis
Benzene
Bioinformatics
Biomaterials
Biotechnology
Calcium
Calcium ions
Cancer Research
Chemistry
Chemistry and Materials Science
Esterase
Industrial applications
Lipase
Magnesium
Metal ions
Molecular weight
Original
Original Article
pH effects
Phylogeny
Salinity tolerance
Sequence analysis
Serine
Sodium chloride
Stem Cells
Substrates
Toluene
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Title Characterization of a novel halotolerant esterase from Chromohalobacter canadensis isolated from salt well mine
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https://www.proquest.com/docview/2442611851
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https://pubmed.ncbi.nlm.nih.gov/PMC7490289
Volume 10
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