Osmolyte-induced folding enhances tryptic enzyme activity
| Autor: | E. Brad Thompson, Justin M. Serrette, Raj Kumar |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Glycerol
Protein Denaturation Protein Folding Proteases Time Factors Biophysics Biochemistry Catalysis Methylamines chemistry.chemical_compound Osmotic Pressure medicine Chymotrypsin Trypsin Molecular Biology chemistry.chemical_classification biology Chemistry Enzyme assay Enzyme Activation Kinetics Spectrometry Fluorescence Enzyme Osmolyte biology.protein Protein folding medicine.drug |
| Zdroj: | Archives of Biochemistry and Biophysics. 436:78-82 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/j.abb.2005.01.008 |
| Popis: | Osmolytes form a class of naturally occurring small compounds known to protect proteins in their native folded and functional states. Among the osmolytes, trimethylamine-N-oxide (TMAO) has received special interest lately because it has shown an extraordinary capability to support folding of denatured to native-like species, which show significant functional activity. Most enzymes and/or proteins are commonly stored in glycerol to maintain their activity/function. In the present study, we tested whether TMAO can be a better solute than glycerol for two commonly used proteases, trypsin and chymotrypsin. Our enzyme kinetic data suggest that the enzyme activity of trypsin is significantly enhanced in TMAO compared to glycerol, whereas chymotrypsin activity is not significantly changed in either case. These results are in accordance with the osmolyte effects on the folding of these enzymes, as judged by data from fluorescence emission spectroscopy. These results suggest that TMAO may be a better solute than glycerol to maintain optimal tryptic enzyme activity. |
| Databáze: | OpenAIRE |
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