AI 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.
Article Abstract
The activity and stability of native subtilisin 72, its complex with poly(acrylic acid), and subtilisin covalently attached to poly(vinyl alcohol) cryogel were studied in aqueous and organic media by hydrolysis of specific chromogenic peptide substrates. Kinetic parameters of the hydrolysis of Glp-Ala-Ala-Leu-pNA by native subtilisin and its complex with poly(acrylic acid) were determined. Based on the comparative study of stability of native and modified subtilisins in media of various compositions, it was established that covalent immobilization of subtilisin on poly(vinyl alcohol) cryogel is the most effective approach to improve enzyme stability in water as well as in mixtures with low water content.
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| http://dx.doi.org/10.1023/b:biry.0000009142.88974.85 | DOI Listing |
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