Modeling the performance of immobilized α-chymotrypsin catalyzed peptide synthesis in acetonitrile medium

Raúl J. Barros, Ernst Wehtje, Patrick Adlercreutz

Research output: Contribution to journalArticlepeer-review

6 Citations (SciVal)

Abstract

A model was developed which describes simultaneous reaction and internal diffusion for kinetically controlled, immobilized α-chymotrypsin-catalyzed, oligopeptide synthesis in acetonitrile medium. The model combines the equations that describe the intrinsic kinetics of four different reactions and the physical characteristics of three different support materials, as determined experimentally, to predict the apparent initial activity and nucleophile selectivity of the immobilized biocatalyst. The model is able to predict reasonably well the experimentally observed initial rate and nucleophile selectivity vs. enzyme loading profiles. The reduction in observed initial rate with enzyme loading when fast reactions are carried out with α-chymotrypsin immobilized on celite, and the larger influence of mass transfer limitations on the initial reaction rates than on nucleophile selectivities are correctly predicted by the numerical calculations. The model is general in terms of its application to other systems - enzymes, reactions, support materials and/or kinetic schemes - as long as the intrinsic kinetics and the characteristics of the enzyme and support material are known.

Original languageEnglish
Pages (from-to)841-850
Number of pages10
JournalJournal of Molecular Catalysis - B Enzymatic
Volume11
Issue number4-6
DOIs
Publication statusPublished - 2001 Jan 22

Subject classification (UKÄ)

  • Biocatalysis and Enzyme Technology

Keywords

  • Initial rate
  • Internal diffusion and reaction
  • Kinetically controlled peptide synthesis
  • Nucleophile selectivity
  • Numerical model

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