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Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media
Author(s) -
Arsan Jad,
Parkin Kirk L.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(20000720)69:2<222::aid-bit11>3.0.co;2-8
Subject(s) - selectivity , chemistry , rhizomucor miehei , lipase , cofactor , hexane , triacylglycerol lipase , organic chemistry , enzyme , catalysis
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. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 69: 222–226, 2000.