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Useful methods in enzymatic synthesis of peptides : A comparative study focussing on kinetically controlled synthesis of Ac-Phe-Ala-NH2 catalyzed by α-chymotrypsin

Björup, Peter ; Adlercreutz, Patrick LU orcid and Clapés, Pere (1999) In Biocatalysis and Biotransformation 17(5). p.319-345
Abstract

The usefulness of different reaction systems for enzymatic peptide synthesis was evaluated by studying the formation of a dipeptide from equimolar amounts of acyl-donor and acyl-acceptor. α-Chymotrypsin (EC 3.4.21.1.), dissolved or deposited on celite,was used for the synthesis of Ac-Phe-Ala-NH2 from Ac-Phe-OEt and H-Ala-NH2. Reactions were carried out at room temperature (≃ 25°C), if not otherwise stated, in aqueous solutions (≤ 21% yield), frozen solutions at -30°C (≤ 60% yield), suspensions in aqueous media with and without 0.5% (v/v) of Triton X-100 (≤ 82% yield), suspensions in hydrophobic organic media with Na2CO3 . 10H2O as water source (≤ 90% yield), eutectic... (More)

The usefulness of different reaction systems for enzymatic peptide synthesis was evaluated by studying the formation of a dipeptide from equimolar amounts of acyl-donor and acyl-acceptor. α-Chymotrypsin (EC 3.4.21.1.), dissolved or deposited on celite,was used for the synthesis of Ac-Phe-Ala-NH2 from Ac-Phe-OEt and H-Ala-NH2. Reactions were carried out at room temperature (≃ 25°C), if not otherwise stated, in aqueous solutions (≤ 21% yield), frozen solutions at -30°C (≤ 60% yield), suspensions in aqueous media with and without 0.5% (v/v) of Triton X-100 (≤ 82% yield), suspensions in hydrophobic organic media with Na2CO3 . 10H2O as water source (≤ 90% yield), eutectic mixtures at 37°C (≤ 97% yield), and acetonitrile containing 1-5% (v/v) of aqueous buffer (≤ 99% yield). Initial rates of synthesis were in the range of 5.9 x 10-2-7.1 x 102 μmol min-1 (mg of enzyme)-1. The lowest one was obtained with dissolved reactants in acetonitrile containing 1% (v/v) of aqueous buffer, and the highest one was obtained with suspended acyl-donor in aqueous medium containing 0.5% (v/v) of Triton X-100.

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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Ac-Phe-Ala-NH, Eutectic mixtures, Frozen solutions, Organic media, Peptide synthesis, Surfactant, α-chymotrypsin
in
Biocatalysis and Biotransformation
volume
17
issue
5
pages
27 pages
publisher
Taylor & Francis
external identifiers
  • scopus:0041467273
ISSN
1024-2422
DOI
10.3109/10242429909015234
language
English
LU publication?
yes
id
84ca8af9-1544-4b7f-9f7c-81199d75fdb3
date added to LUP
2019-06-20 15:18:43
date last changed
2022-01-31 22:13:19
@article{84ca8af9-1544-4b7f-9f7c-81199d75fdb3,
  abstract     = {{<p>The usefulness of different reaction systems for enzymatic peptide synthesis was evaluated by studying the formation of a dipeptide from equimolar amounts of acyl-donor and acyl-acceptor. α-Chymotrypsin (EC 3.4.21.1.), dissolved or deposited on celite,was used for the synthesis of Ac-Phe-Ala-NH<sub>2</sub> from Ac-Phe-OEt and H-Ala-NH<sub>2</sub>. Reactions were carried out at room temperature (≃ 25°C), if not otherwise stated, in aqueous solutions (≤ 21% yield), frozen solutions at -30°C (≤ 60% yield), suspensions in aqueous media with and without 0.5% (v/v) of Triton X-100 (≤ 82% yield), suspensions in hydrophobic organic media with Na<sub>2</sub>CO<sub>3</sub> <sup>.</sup> 10H<sub>2</sub>O as water source (≤ 90% yield), eutectic mixtures at 37°C (≤ 97% yield), and acetonitrile containing 1-5% (v/v) of aqueous buffer (≤ 99% yield). Initial rates of synthesis were in the range of 5.9 x 10<sup>-2</sup>-7.1 x 10<sup>2</sup> μmol min<sup>-1</sup> (mg of enzyme)<sup>-1</sup>. The lowest one was obtained with dissolved reactants in acetonitrile containing 1% (v/v) of aqueous buffer, and the highest one was obtained with suspended acyl-donor in aqueous medium containing 0.5% (v/v) of Triton X-100.</p>}},
  author       = {{Björup, Peter and Adlercreutz, Patrick and Clapés, Pere}},
  issn         = {{1024-2422}},
  keywords     = {{Ac-Phe-Ala-NH; Eutectic mixtures; Frozen solutions; Organic media; Peptide synthesis; Surfactant; α-chymotrypsin}},
  language     = {{eng}},
  month        = {{01}},
  number       = {{5}},
  pages        = {{319--345}},
  publisher    = {{Taylor & Francis}},
  series       = {{Biocatalysis and Biotransformation}},
  title        = {{Useful methods in enzymatic synthesis of peptides : A comparative study focussing on kinetically controlled synthesis of Ac-Phe-Ala-NH<sub>2</sub> catalyzed by α-chymotrypsin}},
  url          = {{http://dx.doi.org/10.3109/10242429909015234}},
  doi          = {{10.3109/10242429909015234}},
  volume       = {{17}},
  year         = {{1999}},
}