Activity and enantioselectivity of the hydroxynitrile lyase MeHNL in dry organic solvents.
Water concentration affects both the enantioselectivity and activity of enzymes in dry organic media. Its influence has been investigated using the hydrocyanation of benzaldehyde catalyzed by hydroxynitrile lyase cross-linked enzyme aggregate (MeHNL-CLEA) as a model reaction. The enzyme displayed higher enantioselectivity at higher water concentration, thus suggesting a positive effect of enzyme flexibility on selectivity. The activity increased on reducing the solvent water content, but drastic dehydration of the enzyme resulted in a reversible loss of activity.
Paravidino
Monica
M
Gebouw voor Scheikunde, Afdeling Biotechnologie, Technische Universiteit Delft, Julianalaan 136, 2628 BL Delft, The Netherlands.
Sorgedrager
Menno J
MJ
Orru
Romano V A
RV
Hanefeld
Ulf
U
D000097:Acetonitriles / Q000737:chemistry* / Q000378:metabolism; D000327:Adsorption; D000446:Aldehyde-Lyases / Q000737:chemistry* / Q000378:metabolism; D001547:Benzaldehydes / Q000737:chemistry*; D002384:Catalysis; D003890:Desiccation; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D015394:Molecular Structure; D012997:Solvents / Q000737:chemistry*; D013237:Stereoisomerism; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D000097:Acetonitriles; D001547:Benzaldehydes; D004800:Enzymes, Immobilized; D012997:Solvents; D014867:Water; D000446:Aldehyde-Lyases