Mycelia-associated β-xylosidase in pellets of Aspergillus sps.

Henrik Stålbrand, Bärbel Hahn-Hägerdal, Kati Réczey, Folke Tjerneld

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

A screening of 10 strains of Aspergillus for pellet formation and mycelia-associated β-xylosidase activity was performed in media containing glucose and glucose supplemented with methyl β-d-xylopyranoside. The aim was to produce an immobilized enzyme preparation. Three strains with high mycelia-associated β-xylosidase activity were investigated for enzyme leakage and enzyme stability:A. terreus QM 1991, A. phoenicis ATCC 13157, and A. phoenicis QM 329. The pellets of A. phoenicis QM 329 had the highest β-xylosidase activity (280 IU/g dry wt mycelia) after 333 h of incubation. From measurements of both cell-bound enzyme activity and the activity in solution, it could be concluded that for Aspergillus phoenicis QM 329 and ATCC 13157 the decrease in β-xylosidase activity bound to the pellets was owing to enzyme leakage. For Aspergillus terreus QM 1991, the decrease of pellet-bound β-xylosidase activity was the result of both leakage and enzyme deactivation at 50°C. β-Xylosidase in pellets of A. phoenicis QM329 hydrolyzes xylobiose and p-nitrophenyl β-d-xylopyranoside with the same rate of conversion.

Original languageEnglish
Pages (from-to)261-272
Number of pages12
JournalApplied Biochemistry and Biotechnology
Volume34-35
Issue number1
DOIs
Publication statusPublished - Mar 1 1992

Keywords

  • Aspergillus
  • immobilization
  • mycelial pellets
  • xylobiose hydrolysis
  • β-xylosidase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology

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