This project involves elucidation of amino acid residues exerting control of catalytic specificity in glycosidases, by use of molecular biology techniques combined with in depth structure-function analysis. Three stable, differently folded model enzymes originating from glycoside hydrolase family 1, 3 and 12, are studied, with the aim to promote development specific carbohydrate engineering tools. 

Detailed structure-function analysis (in collaboration with D Logan, Dept. Mol Biophysics) allows rational selection of residues/regions for mutagenesis, and improved understanding of the structural requirements for the different acceptor molecule structures important for catalytic selectivity of the enzymes. Evaluation of their efficiency in the selected biocatalytic target reaction will confirm improvements. Use of carbohydrate containing rawmaterials from biomass as substrates offers environmentally friendly production alternatives, and this work will evaluate the possibility to develop new biocatalysts for selective biocatalytic processes.

Contact:     Eva Nordberg Karlsson
Collaboration:    Dr Derek Logan (Dept. Molecular Biophysics, LU)