Premium
Properties of a thermostable and solvent stable extracellular lipase from a Pseudomonas sp. AG‐8
Author(s) -
Sharma Anil K.,
Tiwari Ram P.,
Hoondal Gurinder S.
Publication year - 2001
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/1521-4028(200112)41:6<363::aid-jobm363>3.0.co;2-c
Subject(s) - lipase , acetone , chemistry , enzyme , extracellular , enzyme assay , specific activity , urea , methanol , ethanol , solvent , triacylglycerol lipase , pseudomonas , nuclear chemistry , chromatography , biochemistry , organic chemistry , biology , bacteria , genetics
An extracellular lipase isolated from Pseudomonas sp. AG‐8, had an optimal activity at 45 °C and pH 8.0–8.5. It retained more than 80% of its initial activity after keeping for 1 h at 65 °C. The enzyme was stable in 5 M NaCl and 6 M urea. Triton X‐100 increased the lipase activity by 2.4 fold. Ca 2+ ions activated the enzyme, while Zn 2+ , Fe 2+ , Fe 3+ 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.