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Cholinesterase‐catalyzed resolution of D , L ‐carnitine
Author(s) -
Dropsy Eric P.,
Klibanov Alexander M.
Publication year - 1984
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260260815
Subject(s) - chemistry , carnitine , hydrolysis , acetylcholinesterase , butyrylcholinesterase , stereospecificity , enzyme , resolution (logic) , cholinesterase , chromatography , biochemistry , stereochemistry , catalysis , aché , biology , artificial intelligence , computer science , pharmacology
An enzymatic method for the preparative resolution of racemic carnitine (whose L ‐isomer and its acyl‐derivatives have numerous therapeutical applications) has been developed. It is based on our finding that electriceel acetylcholinesterase hydrolyzes the D ‐ but not the L ‐isomer of acetylcarnitine. (Another cholinesterase tested, horse serum butyrylcholinesterase, is also stereospecific and hydrolyzes only the L ‐isomer of butyrylcarnitine.) Acetylcholinesterase, covalently attached to alumina, was employed for the resolution of D , L ‐carnitine; the latter was first chemically acetylated, then stereoselectively hydrolyzed with the immobilized enzyme, and finally the acetyl‐ L ‐carnitine and D ‐carnitine produced were separated by ion‐exchange chromatography. Gram quantities of D , L ‐carnitine were thereby resolved.