Purification and characterization of lipase from Aeromonas sobria LP004

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. so...

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Veröffentlicht in:Journal of biotechnology 1997-04, Vol.54 (2), p.113-120
Hauptverfasser: Lotrakul, Pongtharin, Dharmsthiti, Saovanee
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0168-1656
1873-4863
DOI:10.1016/S0168-1656(97)01696-9