28871-77-4Relevant academic research and scientific papers
Enzymatic optical resolution of norbornanecarboxylic esters using Pig Liver Esterase
Gastel, F. J. C. van,Klunder, A. J. H.,Zwanenburg, B.
, p. 175 - 184 (2007/10/02)
The hydrolysis of a series of norbornane-type carboxylic esters catalyzed by pig liver esterase (PLE) has been investigated.It was found that an exo-ester function (syn to the C7 methylene group) is hydrolyzed with high preference.Enantioselective hydrolysis can be accomplished when a vicinal carbonyl-containing function (ester, formyl, acetyl) is present in a trans position with respect to the exo ester.The regiospecifity of the enzymatic hydrolysis has been used for the separation of exo/endo mixtures of the cycloadducts derived from cyclopentadiene and alkene esters.The regiospecifity and enantioselectivity of the enzymatic hydrolysis of norbornane-type esters were analyzed in terms of Tamm's substrate model and also by Griengl's method.
