Selectivity of Rhizomucor miehei lipase as affected by choice of cosubstrate system in ester modification reactions in organic media
✍ Scribed by Jad Arsan; Kirk L. Parkin
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 96 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
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 npropanol 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.