Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media.
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.
Arsan
J
J
Department of Food Science, University of Wisconsin, Babcock Hall, 1605 Linden Drive, Madison, Wisconsin 53706, USA.
Parkin
K L
KL
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
D000085:Acetates; D000438:Alcohols; D004800:Enzymes, Immobilized; D005227:Fatty Acids; C069372:isopropyl acetate; C026498:propyl acetate; D000433:1-Propanol; D008049:Lipase; D019840:2-Propanol