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In vitro Digestion of Emulsions in a Single Droplet via Multi Subphase Exchange of Simulated Gastrointestinal Fluids

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Soluble, folded and active subtilisin in a protic ionic liquid.

Francesco Falcioni¹, Hazel R Housden, Zhenlian Ling

¹CNAP, Department of Biology, University of York, York, United Kingdom YO10 5YW.

Chemical Communications (Cambridge, England)

|January 21, 2010

Summary

This summary is machine-generated.

Subtilisin enzyme activity was observed in diethanolammonium chloride (DEA Cl) ionic liquid, but chymotrypsin showed no activity in any protic ionic liquids (PILs) tested. This highlights the influence of ionic liquids on protease function.

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Area of Science:

Biochemistry
Enzymology
Ionic Liquids

Background:

Proteases are crucial enzymes in biological processes.
Ionic liquids (ILs) offer unique solvent properties.
Investigating enzyme activity in ILs is key for biocatalysis.

Purpose of the Study:

To evaluate the activity of chymotrypsin and subtilisin in protic hydroxylalkylammonium ionic liquids.
To determine the impact of specific ionic liquids on protease functionality.

Main Methods:

Assaying protease activity using the model substrate N-acetyl-L-phenylalanine ethyl ester (APEE).
Dissolving proteases (chymotrypsin and subtilisin) in various protic hydroxylalkylammonium ionic liquids.
Comparing enzyme activity across different ionic liquid environments.

Main Results:

Subtilisin exhibited activity solely in diethanolammonium chloride (DEA Cl).
Chymotrypsin demonstrated no detectable activity in any of the tested protic ionic liquids.
The choice of ionic liquid significantly affected protease stability and function.

Conclusions:

Diethanolammonium chloride (DEA Cl) can support subtilisin activity.
Chymotrypsin's activity is inhibited in the tested protic ionic liquids.
Protic ionic liquids present a challenging but potentially tunable medium for protease applications.