Studies on the lipozyme-catalyzed synthesis of butyl laurate

Gandhi, Neena N. ; Sawant, Sudhirprakash B. ; Joshi, Jyeshtharaj B. (1995) Studies on the lipozyme-catalyzed synthesis of butyl laurate Biotechnology and Bioengineering, 46 (1). pp. 1-12. ISSN 0006-3592

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The effects of temperature, speed of agitation, enzyme concentration, etc., on butyl laurate synthessis using Mucor miehei lipase (Lipozyme™) have been studied. Although the soluble enzyme was quite thermcstable in aqeous solution, it deactivated rapidly at and above 40°C in the presence of butanol. This enzyme immobilized on an anion-exchange resin (Lipozyme™) showed enhanced stability (as compared to the soluble form) to denaturation by butanol under the same conditions. The denaturation of M. miehei lipase was found to be a function of the butanol concentration in the aqueous phase, and rapid denaturation takes place at the concentration corresponding to its saturation at that temperature.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Lipozyme; Esterification; Immobilization; Butanol; Lauric Acid
ID Code:61151
Deposited On:13 Sep 2011 10:56
Last Modified:13 Sep 2011 10:56

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