title: Properties of a thermostable and solvent stable extracellular lipase from a Pseudomonas sp. AG-8.
abstract: An extracellular lipase isolated from Pseudomonas sp. AG-8, had an optimal activity at 45 degrees C and pH 8.0-8.5. It retained more than 80% of its initial activity after keeping for 1 h at 65 degrees C. The enzyme was stable in 5 M NaCl and 6 M urea. Triton X-100 increased the lipase activity by 2.4 fold. Ca2+ ions activated the enzyme, while Zn2+, Fe2+, Fe3+ strongly inhibited its activity. Ethanol, methanol and acetone at 20% (v/v) enhanced the lipase activity by 2.9, 3.6 and 4.5 fold respectively. Dimethylsulphoxide at 90% (v/v) enhanced the enzyme activity up to 5.7 fold.
authors.affiliation: Department of Microbiology, Panjab University, Chandigarh-160 014, India.
authors.forename: A K
authors.initials: AK
authors.lastname: Sharma
authors.forename: R P
authors.initials: RP
authors.lastname: Tiwari
authors.forename: G S
authors.initials: GS
authors.lastname: Hoondal
mesh_terms: D004795:Enzyme Stability; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D012997:Solvents / Q000494:pharmacology; D013696:Temperature
chemical_list: D012997:Solvents; D008049:Lipase