Title Purification and Characterization of Cold Active Lipase from Psychrotrophic Aeromonas sp. LPB 4
Author Han-Ki Lee, Min-Jung Ahn, Sung-Ho Kwak, Won-Ho Song, and Byeong-Chul Jeong *
Address Department of Biological Science, Myong Ji University, Yongin, Kyonggi-do, 449-728, Korea (Received December 27, 2002 / Accepted February 10, 2003)
Bibliography Journal of Microbiology, 41(1),22-27, 2003,
DOI
Key Words psychrophile, Aeromonas sp. LPB 4, lipase
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 50℃. 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%.
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