Lipase regio- and stereoselectivities toward three enantiomeric pairs of didecanoyl-deoxyamino-O methyl glycerol: A kinetic study by the monomolecular film technique

A kinetic study was carried out on the regio‐ and stereoselectivities of 12 lipases of animal and microbial origin. For this purpose, monomolecular films consisting of three pairs of enantiomers (didecanoyl‐deoxyamino‐O methyl glycerol, DDG) containing a single hydrolyzable decanoyl ester bond and t...

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Bibliographic Details
Published in:Chirality (New York, N.Y.) N.Y.), 2003, Vol.15 (3), p.220-226
Main Authors: Douchet, Isabelle, de Haas, Gerard, Verger, Robert
Format: Article
Language:English
Subjects:
Animals
Candida
Diglycerides - chemistry
Fusarium
glyceride analogs
Guinea Pigs
Humans
Kinetics
Lipase - metabolism
lipases
Membranes, Artificial
monomolecular film technique
Penicillium
Pressure
Pseudomonas
regioselectivity
Rhizomucor
Stereoisomerism
stereoselectivity
Substrate Specificity
Surface Properties
Swine
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Summary:A kinetic study was carried out on the regio‐ and stereoselectivities of 12 lipases of animal and microbial origin. For this purpose, monomolecular films consisting of three pairs of enantiomers (didecanoyl‐deoxyamino‐O methyl glycerol, DDG) containing a single hydrolyzable decanoyl ester bond and two lipase‐resistant groups were spread at the air–water interface. Each of the lipases tested displayed a particular type of behavior, on the basis of which they were classified in two groups, depending on their ability to hydrolyze the sn‐2 position. From the qualitative point of view, the sn‐2 preference measured on triacylglycerides and DDG were in good agreement. The inductive chemical effect might explain why a greater level of hydrolytic activity was observed with the diglycerides than with DDG. With most of the lipases tested, it was observed that the enantiomeric pair having two distal acyl chains was more clearly differentiated stereochemically than the two homologous pairs with two adjacent acyl chains. This finding is consistent with the hypothesis that during the chiral recognition process two of the three attachment points may be the external (distal) hydrophobic chains, which is in line with the hypothesis of a tuning fork conformation of a triglyceride in the lipase active site. Chirality 15:220–226, 2003. © 2003 Wiley‐Liss, Inc.
ISSN:0899-0042
1520-636X
DOI:10.1002/chir.10183