Publications by authors named "O V Baĭbak"
Activity and stability of native and modified subtilisins in various media.
Biochemistry (Mosc)
November 2003
Article Synopsis
- The study examined the activity and stability of native subtilisin 72 and its complexes with poly(acrylic acid) and poly(vinyl alcohol) cryogel using specific peptide substrates.
- Kinetic parameters for the hydrolysis reaction of a particular substrate were measured for both native subtilisin and its complex with poly(acrylic acid).
- The findings revealed that covalent attachment of subtilisin to poly(vinyl alcohol) cryogel significantly enhances the enzyme's stability in various environments, particularly in low water content mixtures.
The catalytic efficiencies of native subtilisin, its noncovalent complex with polyacrylic acid, and the subtilisin covalently immobilized in a cryogel of polyvinyl alcohol were studied in the reaction of peptide coupling in mixtures of organic solvents with a low water content in dependence on the medium composition, reaction time, and biocatalyst concentration. It was established that, in media with a DMF content > 80%, the synthase activity of modified subtilisins is higher than that of the native subtilisin. The use of N-acylpeptides with a free carboxyl group was found to be possible in organic solvents during the enzymatic synthesis catalyzed by both native and immobilized subtilisin.
View Article and Find Full Text PDF