A novel cold-adapted and highly salt-tolerant esterase from Alkalibacterium sp. SL3 from the sediment of a soda lake

• Published in: Scientific reports Vol. 6; no. 1; p. 19494
• Main Authors: Wang, Guozeng, Wang, Qiaohuang, Lin, Xianju, Bun Ng, Tzi, Yan, Renxiang, Lin, Juan, Ye, Xiuyun
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.02.2016; Nature Publishing Group
• Subjects: 631/45; 631/535; 82/81; Acetic acid; Adaptation, Physiological; Amino acid composition; Amino acids; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Carnobacteriaceae - enzymology; Cloning, Molecular; Cold Temperature; Detergents; Detergents - chemistry; E coli; Enzyme Stability; Enzymes; Esterase; Esterases - chemistry; Esterases - genetics; Esterases - metabolism; Esters; Humanities and Social Sciences; Hydrogen bonding; Hydrogen-Ion Concentration; Hydrophobicity; Industrial applications; Lakes; Lakes - microbiology; Metals - chemistry; multidisciplinary; Organic solvents; pH effects; Phylogeny; Proline; Reagents; Salinity tolerance; Salts; Science; Sequence Analysis, Protein; Sodium chloride; Sodium Chloride - chemistry; Solvents; Substrate Specificity; Temperature effects
• DOI: 10.1038/srep19494
• ISSN: 2045-2322

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 p NP-acetate and had no activity towards p NP-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.