Effects of acetonitrile-water mixtures on α-chymotrypsin catalyzed dipeptide synthesis
Björup, Peter ; Wehtje, Ernst LU and Adlercreutz, Patrick LU
(1996)
In Biocatalysis and Biotransformation
13(3).
p.189-200
- Abstract
α-Chymotrpysin (EC 3.4 21.1) was immobilized by deposition on celite and subsequent cross-linking with glutaraldehyde. The effects of different mixtures of aqueous buffer and acetonitrile on the immobilized preparation were evaluated using a dipeptide synthesis as model reaction. The initial reaction rate at 6-95% of water increased with increasing water content. The maximum yield of peptide had two maxima; the first one at 6% of water (92%) and the second one at 80% of water (39%). The presence of two maxima was due to severe enzyme inactivation at intermediate water contents (50-60%). The immobilisation procedure slowed the inactivation of α-chymotrypsin. Cross-linked enzyme was inactivated to a lesser extent than both free enzyme and... (More)
α-Chymotrpysin (EC 3.4 21.1) was immobilized by deposition on celite and subsequent cross-linking with glutaraldehyde. The effects of different mixtures of aqueous buffer and acetonitrile on the immobilized preparation were evaluated using a dipeptide synthesis as model reaction. The initial reaction rate at 6-95% of water increased with increasing water content. The maximum yield of peptide had two maxima; the first one at 6% of water (92%) and the second one at 80% of water (39%). The presence of two maxima was due to severe enzyme inactivation at intermediate water contents (50-60%). The immobilisation procedure slowed the inactivation of α-chymotrypsin. Cross-linked enzyme was inactivated to a lesser extent than both free enzyme and enzyme that had been deposited on celite. The increased resistance to inactivation was, however, not sufficient to make peptide synthesis attractive at intermediate water contents (50-60%). In order to obtain good peptide yields, low water contents (below 10%) should be used.
(Less)
- author
- Björup, Peter
; Wehtje, Ernst
LU
and Adlercreutz, Patrick
LU
- organization
- publishing date
- 1996-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Amidase activity, Celite, Cross-linked α-chymotrpysin, Enzymatic dipeptide synthesis, Enzyme inactivation, Esterase activity
- in
- Biocatalysis and Biotransformation
- volume
- 13
- issue
- 3
- pages
- 12 pages
- publisher
- Taylor & Francis
- external identifiers
-
- scopus:0000893045
- ISSN
- 1024-2422
- DOI
- 10.3109/10242429608997675
- language
- English
- LU publication?
- yes
- id
- 9b9849ed-8f26-4743-88a8-cf4dd6f6bbc8
- date added to LUP
- 2019-06-22 09:06:44
- date last changed
- 2022-01-31 22:18:39
@article{9b9849ed-8f26-4743-88a8-cf4dd6f6bbc8,
abstract = {{<p>α-Chymotrpysin (EC 3.4 21.1) was immobilized by deposition on celite and subsequent cross-linking with glutaraldehyde. The effects of different mixtures of aqueous buffer and acetonitrile on the immobilized preparation were evaluated using a dipeptide synthesis as model reaction. The initial reaction rate at 6-95% of water increased with increasing water content. The maximum yield of peptide had two maxima; the first one at 6% of water (92%) and the second one at 80% of water (39%). The presence of two maxima was due to severe enzyme inactivation at intermediate water contents (50-60%). The immobilisation procedure slowed the inactivation of α-chymotrypsin. Cross-linked enzyme was inactivated to a lesser extent than both free enzyme and enzyme that had been deposited on celite. The increased resistance to inactivation was, however, not sufficient to make peptide synthesis attractive at intermediate water contents (50-60%). In order to obtain good peptide yields, low water contents (below 10%) should be used.</p>}},
author = {{Björup, Peter and Wehtje, Ernst and Adlercreutz, Patrick}},
issn = {{1024-2422}},
keywords = {{Amidase activity; Celite; Cross-linked α-chymotrpysin; Enzymatic dipeptide synthesis; Enzyme inactivation; Esterase activity}},
language = {{eng}},
month = {{01}},
number = {{3}},
pages = {{189--200}},
publisher = {{Taylor & Francis}},
series = {{Biocatalysis and Biotransformation}},
title = {{Effects of acetonitrile-water mixtures on α-chymotrypsin catalyzed dipeptide synthesis}},
url = {{http://dx.doi.org/10.3109/10242429608997675}},
doi = {{10.3109/10242429608997675}},
volume = {{13}},
year = {{1996}},
}