Native and modified subtilisin 72 as a catalyst for peptide synthesis in media with a low water content

Bacheva, A.; OV, B.; AV, B.; EN, L.; ES, O.; VI, L.; IY, F.

Авторы: Bacheva AV, Baibak OV, Belyaeva AV, Lysogorskaya EN, Oksenoit ES, Lozinskii VI, Filippova IY
Журнал: Russian Journal of Bioorganic Chemistry
Том: 29
Номер: 5
Год издания: 2003
Издательство: Maik Nauka/Interperiodica Publishing
Местоположение издательства: Russian Federation
Первая страница: 502
Последняя страница: 508
DOI: 10.1023/A:1026013912147
Аннотация: 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. A series of tetrapeptide p-nitroanilides of the general formula Z-Ala- Ala-Xaa-Yaa-pNA (where Xaa is Leu, Lys, or Glu and Yaa is Phe or Asp) was obtained in the presence of immobilized enzyme in yields of 70-98% in DMF-MeCN without any activation of the carboxyl component and without protection of side ionogenic groups of polyfunctional amino acids. #protease, #enzymatic #peptide #synthesis, #nonaqueous #media, #immobilized #subtilisin,#low-water
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