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  • Influence of reactive oxygen species on the enzyme stability and activity in the presence of ionic liquids.

Influence of reactive oxygen species on the enzyme stability and activity in the presence of ionic liquids.

PloS one (2013-09-26)
Pankaj Attri, Eun Ha Choi
ZUSAMMENFASSUNG

In this paper, we have examined the effect of ammonium and imidazolium based ionic liquids (ILs) on the stability and activity of proteolytic enzyme α-chymotrypsin (CT) in the presence of cold atmospheric pressure plasma jet (APPJ). The present work aims to illustrate the state of art implementing the combined action of ILs and APPJ on the enzyme stability and activity. Our circular dichroism (CD), fluorescence and enzyme activity results of CT have revealed that buffer and all studied ILs {triethylammonium hydrogen sulphate (TEAS) from ammonium family and 1-butyl-3-methyl imidazolium chloride ([Bmim][Cl]), 1-methylimidazolium chloride ([Mim][Cl]) from imidazolium family} are notable to act as protective agents against the deleterious action of the APPJ, except triethylammonium dihydrogen phosphate (TEAP) ammonium IL. However, TEAP attenuates strongly the deleterious action of reactive oxygen species (ROS) created by APPJ on native structure of CT. Further, TEAP is able to retain the enzymatic activity after APPJ exposure which is absent in all the other systems.This study provides the first combined effect of APPJ and ILs on biomolecules that may generate many theoretical and experimental opportunities. Through this methodology, we can utilise both enzyme and plasma simultaneously without affecting the enzyme structure and activity on the material surface; which can prove to be applicable in various fields.

MATERIALIEN
Produktnummer
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Produktbeschreibung

Sigma-Aldrich
αα-Chymotrypsin aus Rinderpankreas, Type II, lyophilized powder, ≥40 units/mg protein
Sigma-Aldrich
(+)-Campher-10-sulfonsäure (β), 99%
Sigma-Aldrich
αα-Chymotrypsin, (TLCK treated to inactivate residual tryspin activity), Type VII, essentially salt-free, lyophilized powder, ≥40 units/mg protein
Sigma-Aldrich
αα-Chymotrypsin aus Rinderpankreas, Type I-S, essentially salt-free, lyophilized powder
Sigma-Aldrich
αα-Chymotrypsin aus Rinderpankreas, ≥40 units/mg protein, vial of 5 mg
Sigma-Aldrich
αα-Chymotrypsin aus Rinderpankreas, suitable for protein sequencing, salt-free, lyophilized powder
Sigma-Aldrich
1-Methyl-imidazolium-chlorid, 95%
Sigma-Aldrich
α-Chymotrypsin from human pancreas, lyophilized powder
Sigma-Aldrich
α-Chymotrypsin−Agarose from bovine pancreas, lyophilized powder, 2,000-3,500 units/g agarose (One ml gel will yield 65-120 units)