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

Barros, Raúl J. LU ; Wehtje, Ernst LU and Adlercreutz, Patrick LU (2001) In Journal of Molecular Catalysis - B Enzymatic 11(4-6). p.841-850
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... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Initial rate, Internal diffusion and reaction, Kinetically controlled peptide synthesis, Nucleophile selectivity, Numerical model
in
Journal of Molecular Catalysis - B Enzymatic
volume
11
issue
4-6
pages
10 pages
publisher
Elsevier
external identifiers
  • scopus:0035931365
ISSN
1381-1177
DOI
10.1016/S1381-1177(00)00030-8
language
English
LU publication?
yes
id
67c7614f-4636-4325-b5b2-e31ca8881c8b
date added to LUP
2019-06-20 15:47:35
date last changed
2020-01-13 02:04:09
@article{67c7614f-4636-4325-b5b2-e31ca8881c8b,
  abstract     = {<p>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.</p>},
  author       = {Barros, Raúl J. and Wehtje, Ernst and Adlercreutz, Patrick},
  issn         = {1381-1177},
  language     = {eng},
  month        = {01},
  number       = {4-6},
  pages        = {841--850},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Catalysis - B Enzymatic},
  title        = {Modeling the performance of immobilized α-chymotrypsin catalyzed peptide synthesis in acetonitrile medium},
  url          = {http://dx.doi.org/10.1016/S1381-1177(00)00030-8},
  doi          = {10.1016/S1381-1177(00)00030-8},
  volume       = {11},
  year         = {2001},
}