Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 66, Issue 11, Pages 2347-2355Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.66.2347
Keywords
cholesterol esterase; cholesteryl ester; Pseudomonas aeruginosa; contact lens cleaner
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With the aim of developing a new cholesterol esterase for eliminating lipids on used contact lenses, microorganisms were screened for the enzyme activity. A Pseudomonas aeruginosa isolated from soil was found to produce a desirable enzyme. The enzyme had an isoelectric point of 3.2, and molecular mass of 58 kDa. The optimal temperature was around 53degreesC at pH 7.0, and the optimal pH was from 5.5 to 9.5. The enzyme was stable between pH 5 and 10 for 19 h at 25degreesC, and retained its activity up to 53degreesC on 30 min of incubation at pH 7.0. The rates of hydrolysis of cholesteryl esters of different fatty acids were in the following order: linoleate > oleate > stearate > palmitate > caprylate > myristate > laurate, caprate > caproate > butyrate, acetate. Addition of (tauro)cholate to a final concentration of 100 mm markedly promoted the hydrolysis of triglycerides of short-, medium-, and long-chain fatty acids. When used with taurocholate, the enzyme acted as an effective cleaner for contact lenses stained with lipids consisting of cholesteryl oleate, tripalmitin, and stearyl stearate.
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