Influence of Reaction Parameters on Synthesis of n-Butyl Oleate by ImmobilizedMucor miehei Lipase

✍ Scribed by Knez, Ž. ;Habulin, M.

• Publisher: John Wiley and Sons
• Year: 1993
• Weight: 351 KB
• Volume: 95
• Category: Article
• ISSN: 0931-5985
• DOI: 10.1002/lipi.19930950703

✦ Synopsis

Abstract

Enzymes lower the activation energy for reaction. Activation energy can be properly determined from Arrhenius plot, however the temperature range is quite limited. At temperatures, higher than the usual biological range, thermal deactivation occurs. In this paper some thermodynamic properties of immobilized Mucor miehei lipase activity, which catalyses the synthesis of n‐butyl oleate are presented. Esterification was performed batch‐wise in a stirred tank reactor with equimolar substrate ratio. Very low activation energy was determined (9.561 kJ/mol). At temperatures higher than 80 °C rapid thermal deactivation occurred. The constant of this process was found to be 0.898 and enthalpy was 25.877 kJ/mol.