Production of beta-xylosidase activity by Trichoderma harzianum strains

Nine Trichoderma harzianum strains were screened for beta-xylosidase activity when grown in solid-state cultures on media containing wheat bran as the carbon source. All strains produced beta-xylosidase activity, the most active being in extracts of cultures of T. harzianum strain 4. A beta-xylosida...

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Bibliographic Details
Published inCurrent microbiology Vol. 33; no. 2; p. 71
Main Authors de A Ximenes, F, de Paula Silveira, F Q, Filho, E X
Format Journal Article
LanguageEnglish
Published United States 01.08.1996
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Summary:Nine Trichoderma harzianum strains were screened for beta-xylosidase activity when grown in solid-state cultures on media containing wheat bran as the carbon source. All strains produced beta-xylosidase activity, the most active being in extracts of cultures of T. harzianum strain 4. A beta-xylosidase was purified by ammonium sulfate precipitation, ultrafiltration, gel filtration, and ion exchange chromatography from solid-state cultures of T. harzianum strain C. Enzyme preparations yielded a single band when stained for protein following electrophoresis. The molecular weight value, calculated following SDS-PAGE, was determined to be 60 kDa. beta-Xylosidase was most active at pH 4.0-4.5 and 70 degrees C. This enzyme had a Km value of 0.053 mM. The phenol-sulfuric acid method detected the presence of a small amount of carbohydrate in the purified enzyme preparation. beta-Xylosidase was active against some p-nitrophenylglycosides. The enzyme was inactive against xylan and PNPG. beta-xylosidase activity was inhibited by xylose and SDS. Iodoacetamide, dithiothreitol, gluconolactone, glucose, and mercuric chloride failed to inactivate this enzyme's activity. A synergistic effect was observed when beta-xylosidase from T. harzianum strain C and beta-xylanase from Aspergillus fumigatus were incubated with pretreated arabinoxylan.
Bibliography:F60
F
ISSN:0343-8651
1432-0991
DOI:10.1007/s002849900077