Native and modified subtilisin Karlsberg as an effective catalyst of peptide bond formation in organic media

The activity and stability of native subtilisin Karlsberg and subtilisin 72 and their complexes with sodium dodecyl sulfate (SDS) in organic solvents were studied. The kinetic constants of the hydrolysis of specific chromogenic peptide substrates Z- ALA-Ala-Leu-pNA and Glp-Ala-Ala-Leu-pNA by the sub...

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Bibliographic Details
Published in:	Bioorganicheskaia khimiia Vol. 32; no. 2; p. 130
Main Authors:	Anikina, O M, Semashko, T A, Oksenoĭt, E S, Lysogorskaia, E N, Filippova, I Iu
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-03-2006
Subjects:	Chromogenic Compounds - chemistry Enzyme Stability Hydrolysis Kinetics Oligopeptides - chemical synthesis Oligopeptides - chemistry Sodium Dodecyl Sulfate - chemistry Solvents Subtilisins - chemistry
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Summary:	The activity and stability of native subtilisin Karlsberg and subtilisin 72 and their complexes with sodium dodecyl sulfate (SDS) in organic solvents were studied. The kinetic constants of the hydrolysis of specific chromogenic peptide substrates Z- ALA-Ala-Leu-pNA and Glp-Ala-Ala-Leu-pNA by the subtilisins were determined. It was found that the subtilisin Karlsberg complex with SDS in anhydrous organic solvents is an effective catalyst of peptide synthesis with multifunctional amino acids in positions P1 and P'1 (Glu, Arg, and Asp) containing unprotected side ionogenic groups.
ISSN:	0132-3423