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Enzymes in organic synthesis, 25 . Lipase‐catalyzed sequential esterification of (±)‐2‐methylbutanedioic anhydride — a biocatalytical access to an enantiomerically pure 1‐monoester of ( S )‐2‐methylbutanedioic acid
Author(s) -
Ozegowski Rüdiger,
Kunath Annamarie,
Schick Hans
Publication year - 1995
Publication title -
liebigs annalen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0947-3440
DOI - 10.1002/jlac.1995199509237
Subject(s) - lipase , chemistry , catalysis , organic chemistry , candida antarctica , enantioselective synthesis , enantiomer , yield (engineering) , transesterification , enantiomeric excess , enzyme , triacylglycerol lipase , acylation , materials science , metallurgy
The preparation of enantiomerically pure 1‐(2‐methylpropyl) 4‐hydrogen ( S )‐2‐methylbutanedioate ( ent ‐ 3 ) by an enzyme‐catalyzed sequential esterification of (±)‐2‐methylbutanedioic anhydride ( rac ‐ 1 ) demands two different enzymes. Lipozyme, a lipase from Mucor miehei , was used for the alcoholysis of rac ‐ 1 to a mixture of the isomeric monoesters 2 / ent ‐ 2 and 3 / ent ‐ 3 , whereas Novozym 435, a lipase from Candida antarctica , was required for the enantioselective conversion of a mixture of 3 and ent ‐ 3 into the easily separable neutral diester 4 and the acidic monoester ent ‐ 3 , which thus was obtained in a yield of 26% with an enantiomeric excess of 99%. ent ‐ 3 was reduced by LiBH 4 to ( S )‐3‐methylbutan‐4‐olide ( ent ‐ 10 ), a versatile chiral intermediate.