Selecting optimal conditions for Alcalase CLEA-OM for synthesis of dipeptides in organic media

P. Vossenberg, H.H. Beeftink, T. Nuijens, M.A. Cohen Stuart, J. Tramper

Research output: Contribution to journalArticleAcademicpeer-review

15 Citations (Scopus)

Abstract

In protease-catalyzed peptide synthesis, the availability of water is essential, as a compromise must be made between on the one hand the overall enzymatic activity and, on the other hand, the rate of product synthesis. Water is essential for enzyme activity, but at the same time causes hydrolytic side reactions. We studied the coupling of the carbamoylmethyl ester of N-protected phenylalanine and phenylalanine amide in tetrahydrofuran catalyzed by Alcalase CLEA-OM at a range of water activity (aw) values, including the coupling in the presence of molecular sieves (i.e. at very low aw values). The hydrolytic side reaction (in the present system only the hydrolysis of substrate occurs) was found to dominate above an aw value of about 0.2. To prevent hydrolysis, the presence of molecular sieves was found to be necessary.
Original languageEnglish
Pages (from-to)43-49
JournalJournal of Molecular Catalysis. B, Enzymatic
Volume75
Issue number3
DOIs
Publication statusPublished - 2012

Keywords

  • industrial protease alcalase
  • controlled peptide-synthesis
  • controlled water activity
  • enzymatic-synthesis
  • support material
  • solvents
  • transesterification
  • acetonitrile
  • tripeptide
  • catalysis

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