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Selectivity of potato tuber lipid acyl hydrolase toward long-chain unsaturated FA in esterification reactions with glycerol analogs in organic media
Author(s)
Parkin, Kirk L.
Date Issued
January 1, 2003
Type
Article
Abstract
FA selectivity of a Celite-immobilized potato lipid acyl hydrolase (LAH) in esterification reactions with long-chain FA, including stearic acid (18:0), oleic acid (18:1), linoleic acid (18:2), α-linolenic acid (18:3), EPA (20:5), and DHA (22:6), and alcohol co-substrates (n-propanol, isopropanol, 1,3-propanediol, and glycerol) was studied in isooctane. Immobilized LAH was selective for FA of greater degrees of unsaturation (18:3 > 18:2 > 18:1 > 18:0) for all alcohol acceptors evaluated. Selectivity of LAH toward unsaturated C18 FA increased with an increase in water activity (aw) from 0.19 to 0.90 for n-propanol, isopropanol, and 1,3-propanediol as alcohol co-substrates. In contrast, with glycerol as the alcohol co-substrate, selectivity of LAH toward these unsaturated C18 FA increased with a decrease in aw from 0.90 to 0.19. In addition, immobilized LAH strongly discriminated against EPA and DHA for both 1,3-propanediol and glycerol as alcohol co-substrates.
Citation
JAOCS Journal of the American Oil Chemists Society, 80(4), 335-340, 2003