Directed evolution. After 3 rounds the mutant enzyme from S. cerevisiae displayed a 20-fold increase in the specific activity when compared to the wild-type enzyme.
Isomerization/epimerization of hexoses, pentoses and tetroses
pH-activity profile
Protein engineering through directed evolution. The turnover number on D-glucose in some mutants was increased by 30%–40% when compared to the wild type at pH 7.3. Enhanced activities are maintained between pH 6.0 and 7.5.
Protein engineering through site-directed mutagenesis. The resulting mutant displayed a 3-fold increase in catalytic efficiency with L-arabinose as substrate.