The influence of water on protease‐catalyzed peptide synthesis in acetonitrile/water mixtures
Reslow, Mats ; Adlercreutz, Patrick LU
and Mattiasson, Bo
LU
(1988)
In European Journal of Biochemistry
177(2).
p.313-318
- Abstract
Protease‐catalyzed peptide synthesis in acetonitrile water mixtures, containing 0–90% water, was investigated. α‐Chymotrypsin, as well as thermolysin, were deposited on solid supports, prior to exposure to the reaction media. Peptide syntheses were performed using both a kinetically controlled process (chymotrypsin) and an equilibrium‐controlled synthesis (thermolysin). The activity of chymotrypsin decreased at low water contents. However, at low water contents (1–10%) hydrolytic side reactions were suppressed and high yields of dipeptides were obtained. Optimal water content for the thermolysin‐catalyzed reaction was 4–8%. The dipeptides produced were fully soluble in the reaction mixtures. High operational stability for α‐chymotrypsin... (More)
Protease‐catalyzed peptide synthesis in acetonitrile water mixtures, containing 0–90% water, was investigated. α‐Chymotrypsin, as well as thermolysin, were deposited on solid supports, prior to exposure to the reaction media. Peptide syntheses were performed using both a kinetically controlled process (chymotrypsin) and an equilibrium‐controlled synthesis (thermolysin). The activity of chymotrypsin decreased at low water contents. However, at low water contents (1–10%) hydrolytic side reactions were suppressed and high yields of dipeptides were obtained. Optimal water content for the thermolysin‐catalyzed reaction was 4–8%. The dipeptides produced were fully soluble in the reaction mixtures. High operational stability for α‐chymotrypsin was obtained during 216 h of reaction.
(Less)
- author
- Reslow, Mats
; Adlercreutz, Patrick
LU
and Mattiasson, Bo
LU
- organization
- publishing date
- 1988-01-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- European Journal of Biochemistry
- volume
- 177
- issue
- 2
- pages
- 6 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0023788217
- pmid:3056721
- ISSN
- 0014-2956
- DOI
- 10.1111/j.1432-1033.1988.tb14377.x
- language
- English
- LU publication?
- yes
- id
- 36f79471-81e1-4c99-b962-191240249de2
- date added to LUP
- 2019-06-22 18:59:01
- date last changed
- 2024-01-01 12:28:44
@article{36f79471-81e1-4c99-b962-191240249de2,
abstract = {{<p>Protease‐catalyzed peptide synthesis in acetonitrile water mixtures, containing 0–90% water, was investigated. α‐Chymotrypsin, as well as thermolysin, were deposited on solid supports, prior to exposure to the reaction media. Peptide syntheses were performed using both a kinetically controlled process (chymotrypsin) and an equilibrium‐controlled synthesis (thermolysin). The activity of chymotrypsin decreased at low water contents. However, at low water contents (1–10%) hydrolytic side reactions were suppressed and high yields of dipeptides were obtained. Optimal water content for the thermolysin‐catalyzed reaction was 4–8%. The dipeptides produced were fully soluble in the reaction mixtures. High operational stability for α‐chymotrypsin was obtained during 216 h of reaction.</p>}},
author = {{Reslow, Mats and Adlercreutz, Patrick and Mattiasson, Bo}},
issn = {{0014-2956}},
language = {{eng}},
month = {{01}},
number = {{2}},
pages = {{313--318}},
publisher = {{Wiley-Blackwell}},
series = {{European Journal of Biochemistry}},
title = {{The influence of water on protease‐catalyzed peptide synthesis in acetonitrile/water mixtures}},
url = {{http://dx.doi.org/10.1111/j.1432-1033.1988.tb14377.x}},
doi = {{10.1111/j.1432-1033.1988.tb14377.x}},
volume = {{177}},
year = {{1988}},
}