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Protease K is treated with guanidine hydrochloride(cas 50-01-1)

To study the process of inactivating protease K, try to elucidate the relationship between conformational and enzyme activity.

Protease K was treated with guanidine hydrochloride(cas 50-01-1), and the enzyme activity was determined by denaturing casein as substrate. Fluorescence spectroscopy was used to study the conformational changes of enzyme molecules and calculate the relevant thermodynamic parameters.

With the increase of guanidine hydrochloride concentration, the enzyme activity and fluorescence intensity of protease K decreased, the red shift of the peak position, the endogenous fluorescence quenching effect of the potassium iodide on the enzyme molecule, the increase of the fold fraction; the thermal denaturation of the protease K The temperature and the maximum stable temperature decrease; the entropy of the unfolding process becomes larger than 0. Conclusion Protease K is more stable to low concentration of guanidine hydrochloride, 3.5 mol·L-1 is the critical concentration of guanidine hydrochloride induced protease K denaturation; the stability of space conformation Is the basis for maintaining the activity of the enzyme. The thermal stability of the protease K decreases with the increase of the concentration of guanidine hydrochloride(cas 50-01-1). The folding process of the guanidine hydrochloride-induced protease K is entropy-driven.

 

 

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