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ARS Home » Research » Publications at this Location » Publication #101329
Title: STEROL ESTER PRODUCTION BY LIPASE-CATALYZED REACTIONS IN SUPERCRITICAL CARBON DIOXIDE

Author
item Snyder, Janet
item FRYKMAN, HANS - FORMER ARS EMPLOYEE
item KING, JERRY
item Neese, Angela

Submitted to: Annual Meeting and Expo of the American Oil Chemists' Society
Publication Type: Abstract Only
Publication Acceptance Date: 5/10/1999
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Previously we have reported the application of various enzymes to facilitate lipid reactions in supercritical carbon dioxide (SC-CO2). In this study, several enzymes were studied to determine the optimum catalyst required for the reaction of various fatty acids with sterol compounds in SC-CO2. Using an analytical scale extractor and experimental conditions, the lipase from Burkholderia cepacia, Chirazyme L-1, was determined to be the most selective for these reactions. The sterols used in the study were cholesterol and sitostanol, reacting with fatty acids that included caprylic, capric, lauric, palmitic, and oleic acid. Pressure (3000-4500 psi), temperature (40-60 deg C), flow rate (0.5-2 mL/min), and static extraction hold time (0-15 min) were varied to determine the best conditions for the lipase/catalyzed reaction. The yield of the cholesterol ester, measured by supercritical fluid chromatography, ranged from 90% for caprylic acid to 99% for palmitic acid. The ester yield from the reaction of sitostanol and the fatty acids ranged from 92% for caprylic acid to 99% for palmitic acid.