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Stereospecificity of different lipases
Author(s) -
Akesson B.,
Gronowitz S.,
Herslöf B.,
Michelsen P.,
Olivecrona T.
Publication year - 1983
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02534708
Subject(s) - stereospecificity , lipase , rhizopus arrhizus , glycerol , chemistry , enantiomer , substrate (aquarium) , glyceride , organic chemistry , acylation , alkyl , stereochemistry , enzyme , catalysis , biology , fatty acid , ecology
The stereospecificity of 4 lipases towards enantiomeric alkyldiacylglycerols and alkylmonoacylglycerols was investigated. No stereospecific breakdown of the former substrate was observed for lipases from pancreas, Rhizopus arrhizus, Pseudomonas fluorescens , or bile salt‐stimulated lipase from human milk. All lipases degraded 2‐oleoyl‐3‐tetradecyl‐ sn ‐glycerol faster than 1‐tetradecyl‐2‐oleoyl‐ sn ‐glycerol. Among X‐1‐acyl‐3‐alkylglycerol isomers, 1‐acyl‐3‐alkyl‐ sn ‐glycerol was preferentially attacked by the 3 first mentioned lipases. Possible mechanisms and metabolic implications for these stereospecificities are discussed.