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Influence of solvent and water activity on kinetically controlled peptide synthesis

Clapés, Pere ; Valencia, Gregorio and Adlercreutz, Patrick LU (1992) In Enzyme and Microbial Technology 14(7). p.575-580
Abstract

α-Chymotrypsin deposited on Celite was used to catalyse peptide synthesis reactions between N-protected amino acid esters and leucine amide in organic media with low water content. The influence of the solvent and the thermodynamic water activity on the reaction kinetics was studied. The substrate specificity in the reactions was shown to be a combination of the substrate specificity of the enzyme in aqueous media and the influence of the solvents. The magnitude of the solvent effects differed greatly depending on the substrates used. In hydrophobic solvents high reaction rates were observed and the competing hydrolysis of the ester substrate occurred to only a minor extent. Reactions occurred at water activities as low as 0.11, but the... (More)

α-Chymotrypsin deposited on Celite was used to catalyse peptide synthesis reactions between N-protected amino acid esters and leucine amide in organic media with low water content. The influence of the solvent and the thermodynamic water activity on the reaction kinetics was studied. The substrate specificity in the reactions was shown to be a combination of the substrate specificity of the enzyme in aqueous media and the influence of the solvents. The magnitude of the solvent effects differed greatly depending on the substrates used. In hydrophobic solvents high reaction rates were observed and the competing hydrolysis of the ester substrate occurred to only a minor extent. Reactions occurred at water activities as low as 0.11, but the rate constants increased with increasing water activity and were about two orders of magnitude higher at the highest water activity tested (0.97).

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author
; and
organization
publishing date
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publication status
published
subject
keywords
bioorganic synthesis, chymotrypsin, Enzymatic peptide synthesis, organic media, water activity
in
Enzyme and Microbial Technology
volume
14
issue
7
pages
6 pages
publisher
Elsevier
external identifiers
  • pmid:1368428
  • scopus:0026899249
ISSN
0141-0229
DOI
10.1016/0141-0229(92)90129-C
language
English
LU publication?
yes
id
85ecf33a-bfff-4674-9e79-b1bf79f941c6
date added to LUP
2019-06-22 09:26:45
date last changed
2020-01-13 02:05:10
@article{85ecf33a-bfff-4674-9e79-b1bf79f941c6,
  abstract     = {<p>α-Chymotrypsin deposited on Celite was used to catalyse peptide synthesis reactions between N-protected amino acid esters and leucine amide in organic media with low water content. The influence of the solvent and the thermodynamic water activity on the reaction kinetics was studied. The substrate specificity in the reactions was shown to be a combination of the substrate specificity of the enzyme in aqueous media and the influence of the solvents. The magnitude of the solvent effects differed greatly depending on the substrates used. In hydrophobic solvents high reaction rates were observed and the competing hydrolysis of the ester substrate occurred to only a minor extent. Reactions occurred at water activities as low as 0.11, but the rate constants increased with increasing water activity and were about two orders of magnitude higher at the highest water activity tested (0.97).</p>},
  author       = {Clapés, Pere and Valencia, Gregorio and Adlercreutz, Patrick},
  issn         = {0141-0229},
  language     = {eng},
  month        = {01},
  number       = {7},
  pages        = {575--580},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Influence of solvent and water activity on kinetically controlled peptide synthesis},
  url          = {http://dx.doi.org/10.1016/0141-0229(92)90129-C},
  doi          = {10.1016/0141-0229(92)90129-C},
  volume       = {14},
  year         = {1992},
}