Abstract
Thermodynamic studies of free Candida antartica lipase B in kinetic resolution of acebutolol have been carried out to characterize the temperature effects towards enzyme stability and activity. A decreased in reaction rate was observed in temperature above 40oC. Thermodynamic studies on lipase deactivation exhibited a first-order kinetic pattern. The activation and deactivation energies were 39.63 kJ/mol and 54.90 kJ/mol, respectively. The enthalpy and entropy of the lipase deactivation were found to be 52.12 kJ/mol and -0.18 kJ/mol, respectively.
Highlights
Chiral drugs including beta blockers are available as racemic mixture consists of (S) and (R)-enantiomers
A large number of studies have been done with various strategies and routes to produce pure enantiomer of beta blocker such as asymmetric synthesis, biotransformation and chromatography methods as well as kinetic resolution
The kinetic resolution of racemic acebutolol through enantioselective transesterification was conducted in a 250 ml Erlenmeyer flask
Summary
Chiral drugs including beta blockers are available as racemic mixture consists of (S) and (R)-enantiomers. Acebutolol pure enantiomers have been synthesized through hydrolytic kinetic resolution (HKR), condensation and followed by reaction with propyl amine, obtained overall yield and optical purity of 47.3 and >98%, respectively [9]. Both techniques involved various intermediate product couple with multi step and lengthy reaction. Preparation of pure enantiomer of propranolol [14] and atenolol [15] have been carried out In both studies, the effects of reaction parameters on the reaction rate and enantiopreference of immobilized Candida antartica lipase B (CALB), as well as the effects of different immobilization protocol has been investigated. Temperature effect on enzymatic reaction can be determined by understanding the thermodynamic properties such as entropy, free energy change and enthalpy change
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More From: IOP Conference Series: Earth and Environmental Science
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