文献类型：期刊文献

英文题名：Purification and Characterization of an Organic Solvent-Tolerant Lipase from Pseudomonas aeruginosa CS-2

作者：Peng, Ren[1,2];Lin, Jinping[1];Wei, Dongzhi[1]

机构：[1]E China Univ Chem Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Jiangxi Normal Univ, Coll Life Sci, Nanchang 330022, Peoples R China

年份：2010

卷号：162

期号：3

起止页码：733

外文期刊名：APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY

收录：;EI(收录号：20103013097531);WOS:【SCI-EXPANDED(收录号:WOS:000278178500011)】；

基金：The financial support from the Ministry of Science and Technology of the People's Republic of China is thankfully acknowledged (Project ID: 2006AA020203).

语种：英文

外文关键词：Organic solvent-tolerant lipase; Pseudomonas aeruginosa CS-2

摘要：An extracellular lipase secreted by Pseudomonas aeruginosa CS-2 was purified to homogeneity about 25.5-fold with an overall yield of 45.5%. The molecular mass of the lipase was estimated to be 33.9 kDa by SDS-PAGE and 36 kDa by gel filtration. The optimum temperature and pH were 50 A degrees C and 8.0. The lipase was found to be stable at pH 4-10 and below 50 A degrees C. Its hydrolytic activity was highest against p-nitrophenyl palmitate (p-NPP) among p-nitrophenyl esters of fatty acids with various chain lengths. The lipase was activated in the presence of Ca2+, while it was inactivated by other metal ions more or less. EDTA significantly reduced the lipase activity, indicating the lipase was a metalloenzyme. Gum Arabic and polyvinyl alcohol 124 enhanced lipase activity but Tween-20, Tween-80, and hexadecyltrimethyl ammonium bromide strongly inhibited the lipase. It exhibited stability in some organic solvents. The lipase was activated in the presence of acetonitrile. Conversely, it was drastically inactivated by methanol and ethanol.