Alcohol inhibition and specificity studies of lipase B fromCandida antarctica in organic solvents

Abstract

Alcohol inhibition of the lipase B from Candida antarctica has been studied through two different approaches: using the same inhibitor (1‐butanol) in different organic solvents and using different inhibitors (differing in chain length) in the same solvent. The competitive inhibition constant values obtained in each case correlate with the calculated activity coefficients of the substrate, suggesting that desolvation of the alcohol is the major force changed. Data dispersion observed using the second approach has been interpreted to come from contributions of enzyme–inhibitor interactions to the binding energy. On the other hand, deacylation has been found to be much less influenced by the solvent variation than the acylation step, despite of the fact that solvation of the substrate involved in this step (the alcohol) is expected to change more than for the ester. Concerning the specificity behavior of the enzyme, a bimodal pattern was observed for the deacylation rate dependence on the alcohol chain length, with the highest values for hexanol (C6) and decanol (C10). With regard to the ester specificity, ethyl caproate (C6) is the preferred one. These results have been confronted with those reported for the lipase from Candida rugosa. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59: 163–170, 1998.

Factors Affecting Enantioselectivity: Allosteric Effects

“…Kinetic studies of the inhibitory effect of 1 -butanol in different solvents on CALB have been performed and the competitive inhibition constant K i values obtained correlated with the calculated activity coeffi cients of the substrate, suggesting that desolvation of the alcohol was the changing condition [35] .…”

Magnetic MOF microreactors for recyclable size-selective biocatalysis

“…17 In the present case, given the intact nature of the capsules and demonstrable heterogeneous nature of the catalysis, we attribute the modest decrease in conversion to the cumulative effects of enzyme denaturing by the 1-butanol substrate. 30 …”

Kinetics and mechanism of regioselective monoacetylation of 3-aryloxy-1,2-propandiols using immobilized Candida antarctica lipase

“…The substrate inhibition of enzyme by excess substrate 258 may result from an interaction of substrate at a secondary binding 259 site on the enzyme which induces a conformational change at the 260 active site resulting the reduced enzyme activity [58,59].…”