Related Experiment Video
Updated: Aug 19, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Creation of a synthetically useful lipase with higher than wild-type enantioselectivity and maintained catalytic
1Department of Biotechnology, Royal Institute of Technology, SE-100 44 Stockholm, Sweden. mats.holmquist@biochem.kth.se
Abstract:
[reaction: see text] We have found that two Geotrichum candidum lipase isozymes have remarkably different abilities to differentiate between enantiomers of ethyl 2-methyldecanoate. By rational recombination of selected portions of the two isozymes, we have created a novel lipase with an enantioselectivity superior to that of the best wild-type parent isozyme. Site-directed mutagenesis identified two key amino acid residues responsible for the improved enantioselectivity without compromised total activity of the reengineered enzyme.
Related Concept Videos
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
Catalytically Perfect Enzymes

