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Abstract
AbstractFA 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 cosubstrate, 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.
Published Version
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