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Screening catalytic lipase activities with an analytical supercritical fluid extractor
Author(s) -
Frykman Hans B.,
Snyder Janet M.,
King Jerry W.
Publication year - 1998
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-998-0257-7
Subject(s) - lipase , supercritical fluid , hydrolysis , chemistry , triacylglycerol lipase , chromatography , substrate (aquarium) , organic chemistry , enzyme , biology , ecology
Two different screenings of several commercial lipases were performed to find a lipase with superior performance for the conversion of lipid moieties to their fatty acid methyl ester (FAME) derivatives under supercritical conditions. The first screening was done under hydrolytic conditions in a buffer. The second screening was done under supercritical conditions with CO 2 , utilizing some of the same lipases for the methanolysis of different lipids. For the substrates studied, there was a significant difference in lipase activity under the two above conditions. Significant hydrolytic activity was demonstrated for three different lipid types (triglycerides, sterols, and phospholipids) with Lipase PS30, but when the same lipase was immobilized on an Accurel carrier (polypropylene), the activity decreased considerably. The opposite was found for Lipase G, which showed strong activity when immobilized and under supercritical conditions. Furthermore, Chirozyme L‐1 was superior under supercritical conditions. The altered substrate specificity that some of these lipases show in supercritical CO 2 suggests several interesting synthetic options and applications under these conditions.