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Lipase regio‐ and stereoselectivities toward three enantiomeric pairs of didecanoyl‐deoxyamino‐O methyl glycerol: A kinetic study by the monomolecular film technique
Author(s) -
Douchet Isabelle,
de Haas Gerard,
Verger Robert
Publication year - 2003
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.10183
Subject(s) - chemistry , lipase , enantiomer , kinetic resolution , hydrolysis , stereochemistry , regioselectivity , glycerol , candida antarctica , triacylglycerol lipase , chirality (physics) , organic chemistry , enzyme , enantioselective synthesis , catalysis , nambu–jona lasinio model , chiral symmetry breaking , physics , quantum mechanics , quark
Abstract 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.