Process design for enzymatic peptide synthesis in near-anhydrous organic media

P. Vossenberg, H.H. Beeftink, M.A.C. Stuart, J. Tramper

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)

Abstract

This work is a case study on a process design for enzymatic peptide synthesis, which is based on and inspired by previously established data about the Alcalase-catalyzed coupling of an amino acid amide and a chemically synthesized activated N-protected amino acid carbamoylmethyl ester in near-anhydrous tetrahydrofuran. The choices with regard to Alcalase formulation, the type of reactor, method of controlling the water content, and whether or not to recycle the enzyme, are discussed. In addition, an estimate is given for the reactor size, volumes of solvent, amount of substrate, enzyme and molecular sieves, needed in order to meet a specific demand for peptides. We believe that this case study gives a good indication of the various choices that have to be made when designing a process for enzymatic peptide synthesis and the implications of these choices.
Original languageEnglish
Pages (from-to)255-268
JournalBiocatalysis and Biotransformation
Volume31
Issue number5
DOIs
Publication statusPublished - 2013

Keywords

  • catalyzed dipeptide synthesis
  • water activity control
  • industrial protease alcalase
  • immobilized lipases
  • precursor dipeptide
  • support material
  • 2-phase systems
  • solvents
  • biocatalysis
  • esterification

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