Purification and Characterization of β-Xylosidase from Trichoderma sp. SY

摘要

A β-xylosidase was purified from the culture of Trichoderma sp. SY. The ten-day-old culture filtrate was concentrated, followed by ion-exchange chromatography and gel filtration chromatography. As a result, β-xylosidase was finally purified about 53-fold and appeared as a single band by SDS-PAGE. The optimum pH and temperature were 5.0 and 55℃, respectively, and the molecular weight about 80 kDa. The purified β-xylosidase was found to be inhibited by various metal ions but not inhibited by xylose.