Chain-length selectivity of various lipases during hydrolysis, esterification and alcoholysis in biphasic aqueous medium
Chain-length selectivity profiles of seven lipases (EC 3.1.1.3) have been determined by multiple substrate competition for three reactions at 30 and 50°C: hydrolysis and synthesis of fatty acid methyl esters and acyl transfer between fatty acid ethyl esters and methyl esters. All acyl chains were even-numbered and saturated. Chain-length specificity profiles depended on the enzyme and the reaction considered, due to the combined influence of enzyme and substrate properties. Changing temperature had a significant influence on substrate specificity for esterification only. The results led to the selection of Candida deformans lipase for the selective hydrolysis of short-chain (C8, C10) esters in an equimolar mixture of C8-C18 methyl esters in the presence of various methanol concentrations. The reaction resulted in a long-chain-enriched methyl ester and a short-chain-enriched fatty acid fractions, respectively, consisting of 96% C12-C18 and 68% C8-C10 in a given example.
| Main Authors: | , , , |
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| Format: | article biblioteca |
| Language: | eng |
| Subjects: | Q60 - Traitement des produits agricoles non alimentaires, triacylglycérol lipase, hydrolyse, estérification, bioconversion, activité enzymatique, acide gras, http://aims.fao.org/aos/agrovoc/c_24095, http://aims.fao.org/aos/agrovoc/c_24940, http://aims.fao.org/aos/agrovoc/c_28361, http://aims.fao.org/aos/agrovoc/c_27463, http://aims.fao.org/aos/agrovoc/c_2604, http://aims.fao.org/aos/agrovoc/c_2818, |
| Online Access: | http://agritrop.cirad.fr/509619/ http://agritrop.cirad.fr/509619/1/509619.pdf |
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