Studies on the lipozyme-catalyzed synthesis of butyl laurate

✍ Scribed by Neena N. Gandhi; Sudhirprakash B. Sawant; Jyeshtharaj B. Joshi

• Book ID: 102772946
• Publisher: John Wiley and Sons
• Year: 1995
• Tongue: English
• Weight: 967 KB
• Volume: 46
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260460102

✦ Synopsis

The effects of temperature, speed of agitation, enzyme concentration, etc., on butyl laurate synthesis using Mu- cor rniehei lipase (Lipozyme'") have been studied. Although the soluble enzyme was quite thermostable in aqueous 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. rniehei lipase was found to be a function of the buSanol concentration in the aqueous phase, and rapid denaturation takes place at the concentration corresponding to its saturation at that temperature.