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- W2185068700 abstract "The extracellular lipase produced by B subtilis Pa2 was purified by acetone precipitation and ion exchange chromatography. The molecular weight of the pure protein was estimated to be 19.4 & 19.2 kDa by SDS-PAGE. The lipase formed high molecular weight aggregates (>100,000 kDa). The enzyme was most active in the pH range of 7 to 9 with maximum activity at pH 8, whereas it was most stable in the pH range of 5 to 10, retaining more than 70% activity. The present lipase was most active in temperature between 30 and 50 °C. Mg 2+ was found to stimulate lipase activity." @default.
- W2185068700 created "2016-06-24" @default.
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- W2185068700 date "2011-01-01" @default.
- W2185068700 modified "2023-09-27" @default.
- W2185068700 title "Purification and characterization of lipase from Bacillus subtilis Pa2" @default.
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