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  • Title: Purification and properties of a thermostable extracellular beta-D-xylosidase produced by a thermotolerant Aspergillus phoenicis.
    Author: Rizzatti AC, Jorge JA, Terenzi HF, Rechia CG, Polizeli ML.
    Journal: J Ind Microbiol Biotechnol; 2001 Mar; 26(3):156-60. PubMed ID: 11420656.
    Abstract:
    A beta-D-xylosidase was purified from cultures of a thermotolerant strain of Aspergillus phoenicis grown on xylan at 45 degrees C. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-100. The purified enzyme was a monomer of molecular mass 132 kDa by gel filtration and SDS-PAGE. Treatment with endoglycosidase H resulted in a protein with a molecular mass of 104 kDa. The enzyme was a glycoprotein with 43.5% carbohydrate content and exhibited a pl of 3.7. Optima of temperature and pH were 75 degrees C and 4.0-4.5, respectively. The activity was stable at 60 degrees C and had a Km of 2.36 mM for p-nitrophenyl-beta-D-xylopiranoside. The enzyme did not exhibit xylanase, cellulase, galactosidase or arabinosidase activities. The purified enzyme was active against natural substrates, such as xylobiose and xylotriose.
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