Abstract
The purification of β-xylosidase (gb- d-xyloside xylohydrolase, EC 3.2.1.37) from Neocallimastix frontalis was performed by ammonium sulphate precipitation, ion exchange chromatography, gel filtration and preparative isoelectric focusing. The enzyme has a molecular mass of 180 000 Da, an isoelectric point at pH 4.35 and catalysed the hydrolysis of p- nitrophenyl-β- d- xylopyranoside optimally at pH 6.5 and 35°C with K m of 0.33 mg ml −1. The enzymatic activity was strongly increased by the presence of Ca 2+, Mn 2+, Zn 2+, Co 2+ or Mg 2+ and completely inhibited by Hg 2+ and p-chloromercuribenzoate. The purified protein also had a low level of xylanase activity.
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