Pongtharin LotrakulSaovanee DharmsthitiFac. S.Mahidol University2018-07-042018-07-041997-04-25Journal of Biotechnology. Vol.54, No.2 (1997), 113-120016816562-s2.0-0030911253https://repository.li.mahidol.ac.th/handle/123456789/17897Lipase 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyImmunology and MicrobiologyArticleSCOPUS10.1016/S0168-1656(97)01696-9