ArticleScientific reports2016
A novel cold-adapted and highly salt-tolerant esterase from Alkalibacterium sp. SL3 from the sediment of a soda lake.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 72 citations in OpenAlex.
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- Expression and characterization of a Clostridium Butyricum esterase from pit cellar of Chinese liquor and its potential in flavor ester synthesis.Archives of microbiology · 2025Article
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- X-ray crystallography of mutant GDSL esterase S12A of3 Biotech · 2023Article
- A novel salt- and organic solvent-tolerant phosphite dehydrogenase fromFrontiers in bioengineering and biotechnology · 2023Article
- An artificial self-assembling peptide with carboxylesterase activity and substrate specificity restricted to short-chain acid p-nitrophenyl esters.Frontiers in chemistry · 2022Article
- Cutin:cutin-acid endo-transacylase (CCT), a cuticle-remodelling enzyme activity in the plant epidermis.The Biochemical journal · 2021Article
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- Microbiota profiling and screening of the lipase active halotolerant yeasts of the olive brine.World journal of microbiology & biotechnology · 2021Article
- Characterization of a novel halotolerant esterase from3 Biotech · 2020Article
- Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis.European biophysics journal : EBJ · 2020Article
- Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine BacteriumJournal of microbiology and biotechnology · 2020Article
- Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases.Biotechnology for biofuels · 2020Article
- Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (Biotechnology for biofuels · 2020Article
- Molecular and Biochemical Characterization of Salt-Tolerant Trehalose-6-Phosphate Hydrolases Identified by Screening and Sequencing Salt-Tolerant Clones From the Metagenomic Library of the Gastrointestinal Tract.Frontiers in microbiology · 2020Article
- Recombinant production and characterization of a novel esterase from a hypersaline lake, Acıgöl, by metagenomic approach.Extremophiles : life under extreme conditions · 2019Article
- Identification and characterization of a novel alkalistable and salt-tolerant esterase from the deep-sea hydrothermal vent of the East Pacific Rise.MicrobiologyOpen · 2018Article
- Identification and characterization of a novel cold-tolerant extracellular protease from Planococcus sp. CGMCC 8088.Extremophiles : life under extreme conditions · 2018Article
- Degradation of phenol via ortho-pathway by Kocuria sp. strain TIBETAN4 isolated from the soils around Qinghai Lake in China.PloS one · 2018Article
- A Shinella β-N-acetylglucosaminidase of glycoside hydrolase family 20 displays novel biochemical and molecular characteristics.Extremophiles : life under extreme conditions · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A novel esterase gene (estSL3) was cloned from the Alkalibacterium sp. SL3, which was isolated from the sediment of soda lake Dabusu. The 636-bp full-length gene encodes a polypeptide of 211 amino acid residues that is closely related with putative GDSL family lipases from Alkalibacterium and Enterococcus. The gene was successfully expressed in E. coli, and the recombinant protein (rEstSL3) was purified to electrophoretic homogeneity and characterized. rEstSL3 exhibited the highest activity towards pNP-acetate and had no activity towards pNP-esters with acyl chains longer than C8. The enzyme was highly cold-adapted, showing an apparent temperature optimum of 30 °C and remaining approximately 70% of the activity at 0 °C. It was active and stable over the pH range from 7 to 10, and highly salt-tolerant up to 5 M NaCl. Moreover, rEstSL3 was strongly resistant to most tested metal ions, chemical reagents, detergents and organic solvents. Amino acid composition analysis indicated that EstSL3 had fewer proline residues, hydrogen bonds and salt bridges than mesophilic and thermophilic counterparts, but more acidic amino acids and less hydrophobic amino acids when compared with other salt-tolerant esterases. The cold active, salt-tolerant and chemical-resistant properties make it a promising enzyme for basic research and industrial applications.
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