title: Purification and characterization of an organic solvent-tolerant alkaline cellulase from a halophilic isolate of Thalassobacillus.
abstract: An extracellular cellulase from Thalassobacillus sp. LY18 was purified 4.5-fold with a recovery of 21 % and a specific activity of 52.4 U mg(-1) protein. Its molecular mass was 61 kDa estimated by SDS-PAGE. It was an endoglucanase for soluble cellulose with optimal activity was at 60 °C and pH 8 with 10 % (w/v) NaCl. It was stable from 30 to 80 °C and from pH 7 to 11 with NaCl from 5 to 17.5 % (w/v). EDTA inhibited activity indicating it was a metalloenzyme. Inhibition by diethyl pyrocarbonate and β-mercaptoethanol suggested that histidine residues and disulfide bonds may play important roles in its catalytic function. The cellulase was highly active in non-ionic surfactants and was stable in water-insoluble organic solvents with log P (ow) ≥ 2.13.
authors.affiliation: Life Science College, Yuncheng University, Yuncheng, 044000, China. lixin-eva@163.com
authors.forename: Xin
authors.initials: X
authors.lastname: Li
authors.forename: Hui-Lu
authors.initials: HL
authors.lastname: Wang
authors.forename: Tang
authors.initials: T
authors.lastname: Li
authors.forename: Hui-Ying
authors.initials: HY
authors.lastname: Yu
mesh_terms: D001406:Bacillaceae / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D009930:Organic Chemicals / Q000737:chemistry; D012965:Sodium Chloride; D012997:Solvents / Q000737:chemistry; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D009930:Organic Chemicals; D012997:Solvents; D012965:Sodium Chloride; D002480:Cellulase