Parameters affecting the synthesis of geranyl butyrate by esterase 30,000 from Mucor miehei

The factors affecting the synthesis of geranyl butyrate by esterase 30,000 of Mucor miehei were studied in a solvent-free system. The effects of substrate molar ratio, temperature, agitation speed, and initial addition of water were investigated. The equimolar ratio was most interesting for ester production in batch. There were no diffusion limitations, and the reaction could be realized at low agitation. The catalytic activity of the enzyme was irreversibly deactivated at 60 degrees C, and the initial addition of water decreased the rare of conversion after 75 h of reaction. The enzyme activity increased with increased linear chainlength of the acid and was also affected by the alcohol structure. Esterase 30,000 gave the highest conversion of butyric acid with hexanol and terpenic alcohols (citronellol, nerol) and the lowest with the secondary alcohol (2-hexanol). Finally, five other industrial enzymatic preparations were investigated for their ability to synthesize geranyl butyrate and to hydrolyze olive oil. We observed, for the lipase from Rhizopus javanicua, that there is no relationship between hydrolytic and synthetic activities; this example shows that the hydrolytic lipase activity data cannot predict the capability of lipases in esterification reactions.