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Candida antarctica Lipase B in a Chemoenzymatic Route to Cyclic α‐Quaternary α‐Amino Acid Enantiomers
Author(s) -
Li XiangGuo,
Rantapaju Maria,
Kanerva Liisa T.
Publication year - 2011
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201001575
Subject(s) - candida antarctica , chemistry , kinetic resolution , enantiomer , lipase , enantioselective synthesis , amino acid , stereochemistry , enzyme , organic chemistry , biochemistry , catalysis
Abstract Kinetic resolution of three cyclic quaternary ethyl 1‐amino‐2,3‐dihydro‐1 H ‐indene‐1‐carboxylates and both 1‐ and 2‐amino‐1,2,3,4‐tetrahydronaphthalene analogues have been studied. Interesterification with butyl butanoate and Candida antarctica lipase B accomplished the task. The enantiomers of all 1‐amino analogues reacted with excellent enantioselectivity (enantiomeric ratio er greater than 200), whereas the 2‐amino analogue was not enantioselective ( er = 4). Amino acid enantiomers were finally obtained as their respective hydrochlorides with almost maximum theoretical yields. For the first time, a lipase enzyme was effectively used in the kinetic resolution of cyclic α‐quaternary α‐amino esters.