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ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)

1 2013

Acta" v. 6, no. 1, 2013 10.15407/biotech6.01.009
Р. 9-21, Bibliography 65, Russian.
Universal Decimal classification: 577.152.311/547.8/548.73


E. A. Shesterenko, I. I. Romanovska O. V. Sevastyanov,S. A. Andronati

Bogatsky Physico-Сhemical Institute of National Academy of Sciences of Ukraine, Odesa

The classification, structure, and mechanism of catalytic action of carboxylesterase of  different origin are presented in the review.

The prospects of carboxylesterases application for metabolism and both several drugs and prodrugs activation investigation in vitro are shown. The enzyme usage as biocatalyst of stereoselective hydrolysis and synthesis of a wide range of acyclic, carbocyclic and heterocyclic compounds — esters are also urgent. It was established that enantiomers obtainable with the help of carboxylesterase are characterized by high chemical yields and optical purity; immobilization on different supports stabilizes the enzyme and allows the repeated usage of obtained biocatalysts. The own studies conducted and the enzymatic hydrolysis features of news 3-acylhydroxy-1,4-benzodiasepin-2-ones — potential anxiolytic and hypnotic means, with a help of pig liver microsomal fraction carboxylesterase have been established. For the first time the enantioselective hydrolysis of 3-acetoxy-7-bromo-1-methyl-5-phenyl-1,2-dihydro-3H-1,4-benzdiazepine-2-one was accomplished using free and immobilized in phyllophorine and alginate, stabilized by Ca2+ microsomal fraction. The S-enantiomer of substrate was isolated, which suggests the increased specificity of pig liver microsomal fraction carboxylesterase to its R-enantiomer.

Key words: carboxylesterase, pig liver microsomal fraction, stereoselective synthesis, 3-acylhydroxy-1,4-benzdiazepine-2-ones, immobi lization.

© Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, 2008