title: Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media.
abstract: Fatty acid (FA) selectivity of immobilized Rhizomucor miehei lipase was determined for various cosubstrate systems for ester modification involving competing n-acyl-donor substrates of even-chain length (C4-C16; FA or their methyl esters, FAME) and either n-propanol or propyl acetate in hexane. Acyl-chain-length optima were observed for C8 and C14/16 in all cases. Upon changing between cosubstrate systems of [FA + propanol] to [FAME + propanol] to [FAME + propyl acetate], there was a general shift in selectivity toward shorter-chain-length FA (C4-C8). The greatest degree of reaction selectivity (based on ratios of selectivity constants) among the FA substrates was 3.1 for the [FA + propanol], 2.5 for the [FAME + propanol], and 1.4 for the [FAME + propyl acetate] cosubstrate systems. For esterification reactions between C6 FA and reactive members of a series of aliphatic and aromatic alcohols, the greatest degree of selectivity observed was 3.6.
authors.affiliation: Department of Food Science, University of Wisconsin, Babcock Hall, 1605 Linden Drive, Madison, Wisconsin 53706, USA.
authors.forename: J
authors.initials: J
authors.lastname: Arsan
authors.forename: K L
authors.initials: KL
authors.lastname: Parkin
mesh_terms: D000433:1-Propanol / Q000378:metabolism; D019840:2-Propanol / Q000378:metabolism; D000085:Acetates / Q000378:metabolism; D000438:Alcohols / Q000378:metabolism; D001709:Biotechnology; D004800:Enzymes, Immobilized; D005227:Fatty Acids / Q000737:chemistry / Q000378:metabolism; D008049:Lipase / Q000378:metabolism*; D020103:Rhizomucor / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000085:Acetates; D000438:Alcohols; D004800:Enzymes, Immobilized; D005227:Fatty Acids; C069372:isopropyl acetate; C026498:propyl acetate; D000433:1-Propanol; D008049:Lipase; D019840:2-Propanol