Purification and characterization of cold active lipase from psychrotrophic Aeromonas sp. LPB 3

다국어 초록 (Multilingual Abstract)

A lipase from Aeromonas sp. LPB 4, a psychrotophile isolated from a sea sediment was purified and
characterized. The lipase was purified 53.5 fold to a homogeneous state by acetone precipitation and
QAE sephadex column chromatography and its molecular weight was determined to be 50 kDa by
SDS-PAGE. The enzyme exhibited maximum activity at 10oC and was stable at temperatures lower
than 50oC. This lipase favored substrates containing medium carbon chain of acyl group, while too low
and high carbon chain decreased its activity. The lipolytic activity of purified lipase was slightly
increased by the addition of 0.1% detergent, but decreased by 1% of detergent. Butanol severely
decreased the lipase activity while methanol increased the activity about 15%.