Natural flavour ester production by immobilized Candida cylindracea lipase in organic solvent
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Production of natural flavour esters by lipase was studied. Lipase can catalyze ester formation when an organic solvent, capable of extracting the ester, is used as a bulk phase solvent. Candida cylindracea lipase, which shows broad substrate specificity and pH stability, was immobilized by adsorption to silica gel. Synthesis of ethyl butyrate was studied as a model. The immobilized lipase was shaken in n-heptane containing ethanol and butyric acid. Ester production rate was optimal around: pH 4, decreasing at higher pH values; 30°C, decreasing at higher temperatures; substrate concentration of 0.4 M ethanol and 0.25 M butyric acid. Enzyme hydration was found necessary for stable activity in repeated use. A variety of flavour esters was produced. Ethyl butyrate production was also evaluated in a packed column of immobilized lipase through which a solution of hexane containing substrate was recycled. With a solution volume to packed bed ratio of 3:1, a space velocity of 20h-1 was found to maximize ethyl butyrate production.
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Copyright © 1987 the author(s). Theses may be used for non-commercial research, educational, or related academic purposes only. Such uses include personal study, research, scholarship, and teaching. Theses may only be shared by linking to Carleton University Institutional Repository and no part may be used without proper attribution to the author. No part may be used for commercial purposes directly or indirectly via a for-profit platform; no adaptation or derivative works are permitted without consent from the copyright owner.
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- 1987
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