Purification and Characterization of Organic Solvent-Stable Lipase from Organic Solvent-Tolerant Pseudomonas aeruginosa LST-03

概要

論文の詳細を見る
An organic solvent-stable lipase(LST-03 lipase) secreted into the culture broth of the organic solvent-tolerant Pseudomonas aeruginosa LST-03 was purified by ion-exchange and hydrophobic interaction chromatography in the presence of 2-propanol. The purified enzyme was homogeneous as determined by SDS-PAGE. The molecular mass of the lipase was estimated to be 27.1 kDa by SDS-PAGE and 36 kDa by gel filtration. The optimum pH and temperature were 6.0 and 37℃. LST-03 lipase was stable at pH5-8 and below 40℃. Its hydrolytic activity was highest against tricaproin(C6), methyl octanoate(C8), and coconut oil respectively among the triacylglycerols, fatty acid methyl esters, and natural oils investigated. The enzyme cleaved not only the 1, 3-positioned ester bonds, but also the 2-positioned ester bond of triolein. It exhibited high levels of activity in the presence of n-decane, n-octane, DMSO, and DMF as well as in the absence of an organic solvent. In addition, LST-03 lipase was stabler in the presence of n-decane, ethyleneglycol, DMSO, n-octane, n-heptane, isooctane, and cyclohexane than in the absence of an organoc solvent.
社団法人日本生物工学会の論文
2000-05-25