Enantioselectivity of Candida rugosa lipase in the hydrolysis of 2-chloroproionic acid methyl ester

Biocatalytic synthesis of cyclopropanol from cyclopropyl methyl ketone using whole cells of Rhodococcus erythropolis

Solvent effect on lipase enantioselectivity. Evidence for the presence of two thermodynamic states.

Influence of lid conformation on lipase enantioselectivity.

Rational design of enantioselective biotransformations in organic media. Towards a comprehensive model for solvent-induced changes of lipase enantioselectivity.

Activity and enantioselectivity of modified lipases in organic solvents.

Lipase-catalyzed kinetic resolutions in organic solvents. Influence of process variables on enzyme enantioselectivity.

Optimization of Pseudomonas cepacia lipase preparations for catalysis in organic solvents

The temperature dependence of enzyme kinetic resolutions reveals the relative importance of enthalpy and entropy to enzyme enantioselectivity

Influence of process variables on the enantioselectivity of lipase-catalyzed kinetic resolutions in organic solvents

Organic cosolvents restore the inherently high enantiomeric ratio of lipase-B from candida-antarctica in hydrolytic resolution by relieving the enantiospecific inhibition of product alcohol.

Simple conformation space search protocols for the evaluation of enantioselectivity of lipases.

The Saccharomyces cerevisiae TGL2 gene encodes a protein with lipolytic activity and can complement an Escherichia coli diacylglycerol kinase disruptant.

Kluyver Institute for Biotechnology in The Netherlands - Unity in Biochemistry.

Biotechnology in The Netherlands.

Enthalpic and entropic contributions to lipase enantioselectivity.