title: Lipase-catalyzed condensation of p-methoxyphenethyl alcohol and carboxylic acids with different steric and electrical properties in acetonitrile.
abstract: The substrate selectivity of Candida antarctica lipase for various carboxylic acids was systematically investigated for their condensation with p-methoxyphenethyl alcohol in acetonitrile. The electron density of a carboxylic carbon and the projection area of an acid molecule were numerical indicators for evaluating the substrate selectivity. Both the electron density and projection area had an influence on the V/Km value, while only the projection area affected the Km value. The presence of conjugation with a carboxyl group in an acid and a branched structure in the non-carboxylic region independently lowered the V/Km value by an order of 1.
authors.affiliation: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Takashi
authors.initials: T
authors.lastname: Kobayashi
authors.forename: Shuji
authors.initials: S
authors.lastname: Adachi
authors.forename: Ryuichi
authors.initials: R
authors.lastname: Matsuno
mesh_terms: D000097:Acetonitriles / Q000737:chemistry*; D002264:Carboxylic Acids / Q000737:chemistry* / Q000145:classification; D002384:Catalysis; D004563:Electrochemistry / Q000379:methods*; D004789:Enzyme Activation; D005656:Fungal Proteins; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D000097:Acetonitriles; D002264:Carboxylic Acids; D005656:Fungal Proteins; D008049:Lipase; C431349:lipase B, Candida antarctica; C032159:acetonitrile