Publication: Purification and characterization of lipase from Aeromonas sobria LP004
Issued Date
1997-04-25
Resource Type
ISSN
01681656
Other identifier(s)
2-s2.0-0030911253
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Journal of Biotechnology. Vol.54, No.2 (1997), 113-120
Suggested Citation
Pongtharin Lotrakul, Saovanee Dharmsthiti Purification and characterization of lipase from Aeromonas sobria LP004. Journal of Biotechnology. Vol.54, No.2 (1997), 113-120. doi:10.1016/S0168-1656(97)01696-9 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/17897
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Purification and characterization of lipase from Aeromonas sobria LP004
Author(s)
Other Contributor(s)
Abstract
Lipase from Aeromonas sobria LP004, isolated from raw milk, was purified and characterized. The lipase was purified 10.29 fold to a homogeneous state by ultrafiltration and column chromatography on phenyl sepharose. The molecular weight of the lipase determined by SDS-PAGE was 97 kDa. Purified A. sobria LP004 lipase exhibited the maximum activity at pH 6.0 and 45°C and was stable under alkaline conditions (pH 6.5-10.0) and at temperatures lower than 40°C. This lipase could be classified as a 1.3-position specific enzyme and its catalytic activity was calcium dependent. PMSF, a serine enzyme inhibitor and 2-mercaptoethanol, a reducing agent, did not affect the enzyme activity.