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

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 Ente...