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).
(Less)
- author
- Clapés, Pere
; Valencia, Gregorio
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 1992-01-01
- type
- Contribution to journal
- 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
-
- scopus:0026899249
- pmid:1368428
- 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
- 2024-04-02 09:34:51
@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}},
keywords = {{bioorganic synthesis; chymotrypsin; Enzymatic peptide synthesis; organic media; water activity}},
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}},
}