title: Activity and enantioselectivity of the hydroxynitrile lyase MeHNL in dry organic solvents.
abstract: 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.
authors.affiliation: Gebouw voor Scheikunde, Afdeling Biotechnologie, Technische Universiteit Delft, Julianalaan 136, 2628 BL Delft, The Netherlands.
authors.forename: Monica
authors.initials: M
authors.lastname: Paravidino
authors.forename: Menno J
authors.initials: MJ
authors.lastname: Sorgedrager
authors.forename: Romano V A
authors.initials: RV
authors.lastname: Orru
authors.forename: Ulf
authors.initials: U
authors.lastname: Hanefeld
mesh_terms: 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*
chemical_list: D000097:Acetonitriles; D001547:Benzaldehydes; D004800:Enzymes, Immobilized; D012997:Solvents; D014867:Water; D000446:Aldehyde-Lyases