Abstract:β-Glucosidase extract was separated from a rubber seed protein solution to study the effect of different concentrations of denaturants on β-glucosidase activity, and laser particle size analysis and molecular fluorescence spectroscopy were used to study the effect of denaturants on the spatial structure of β-glucosidase. β-Glucosidase activity showed a declining trend with increased denaturant concentration, and increased temperature accelerated the pace of this decline. Analysis of the spatial structure of β-glucosidase showed that the molecular particle size in the enzyme solution decreased after the enzyme was denatured by urea, implying that the polymeric structure of β-glucosidase was depolymerized. β-Glucosidase could be activated at a low urea concentration within one hour, and enzyme activity improved significantly, which shows that the spatial structure changes of the enzyme were related to urea concentration. Analysis of fluorescence spectra showed that the location of the fluorescence peak moved with increased urea concentration in the enzyme solution, indicating that tryptophan residues were continuously exposed and the protein structure was continuously opened.
