sclerotiorum. In recent decades, the utilization of β-xylosidases has become prevalent across various processing industries. This enzyme exhibited notable characteristics: it displayed strong susceptibility to inhibition by divalent cations and sensitivity to denaturing agents like SDS and EDTA. Activation was found when thiol-containing reducing agents were present. Such distinctive properties render this enzyme particularly intriguing for various biotechnological applications in industries related to animal feed, juice, and wine. Furthermore, Knob et al. achieved the purification of P. sclerotiorum's β-xylosidase and established homogeneity using a quick and economical method. Structural analysis revealed its dimeric nature, with a native molecular mass estimated at 144 kDa. Moreover, the enzyme was identified as a glycoprotein, comprising a substantial 56.4% carbohydrate content. This report describes the characterization and purification of a β-xylosidase derived from P. sclerotiorum, highlighting its potential uses in a range of biotechnological processes in sectors including wine, juice, and animal feed. The properties of β-xylosidase also make it an attractive option for use sclerotiorum have revealed compelling potential for various industrial applications.