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Native subtilisin Karlsberg and modified subtilisin 72 as effective catalysts 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 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 P 1 and P 1 (Glu, Arg, and Asp) containing unprotected side ionogenic groups.

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sodium dodecyl sulfate


benzyloxycarbonyl. All amino acids belong to the L series


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Correspondence to I. Yu. Filippova.

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Original Russian Text © O.M. Anikina, T.A. Semashko, E.S. Oksenoit, E.N. Lysogorskaya, I.Yu. Filippova, 2006, published in Bioorganicheskaya Khimiya, 2006, Vol. 32, No. 2, pp. 130–136.

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Anikina, O.M., Semashko, T.A., Oksenoit, E.S. et al. Native subtilisin Karlsberg and modified subtilisin 72 as effective catalysts of peptide bond formation in organic media. Russ J Bioorg Chem 32, 116–121 (2006).

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Key words

  • enzymatic peptide synthesis
  • organic solvents
  • SDS-subtilisin Karlsberg comple