| Literature DB >> 15907872 |
Raja Noor Zaliha R A Rahman1, Syarul Nataqain Baharum, Mahiran Basri, Abu Bakar Salleh.
Abstract
An organic solvent-tolerant S5 lipase was purified by affinity chromatography and anion exchange chromatography. The molecular mass of the lipase was estimated to be 60 kDa with 387 purification fold. The optimal temperature and pH were 45 degrees C and 9.0, respectively. The purified lipase was stable at 45 degrees C and pH 6-9. It exhibited the highest stability in the presence of various organic solvents such as n-dodecane, 1-pentanol, and toluene. Ca2+ and Mg2+ stimulated lipase activity, whereas EDTA had no effect on its activity. The S5 lipase exhibited the highest activity in the presence of palm oil as a natural oil and triolein as a synthetic triglyceride. It showed random positional specificity on the thin-layer chromatography.Entities:
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Year: 2005 PMID： 15907872 DOI： 10.1016/j.ab.2005.03.006
Source DB: PubMed Journal: Anal Biochem ISSN： 0003-2697 Impact factor: 3.365