Folia Microbiologica

, 42:544 | Cite as

Purification and characterization of a β-glucosidase fromAspergillus niger

  • M. H. Rashid
  • K. S. Siddiqui


The high-molar mass from of β-glucosidase fromAspergillus niger strain NIAB280 was purified to homogeneity with a 46-fold increase in purification by a combination of ammonium sulfate precipitation, hydrophobic interaction, ion-exchange and gel-filtration chromatography. The native and subunit molar mass was 330 and 110 kDa, respectively. The pH and temperature optima were 4.6–5.3 and 70°C, respectively. TheK m andk cat for 4-nitrophenyl β-d-glucopyranoside at 40°C and pH 5 were 1.11 mmol/L and 4000/min, respectively. The enzyme was activated by low and inhibited by high concentrations of NaCl. Ammonium sulfate inhibited the enzyme. Thermolysin periodically inhibited and activated the enzyme during the course of reaction and after 150 min of proteinase treatment only 10% activity was lost with concomitant degradation of the enzyme into ten low-molar-mass active bands. When subjected to 0–9 mol/L transverse urea-gradient-PAGE for 105 min at 12°C, the nonpurified β-glucosidase showed two major bands which denatured at 4 and 8 mol/L urea, respectively, with half-lives of 73 min.


Cellobiose Ammonium Sulfate Wheat Bran Ammonium Sulfate Precipitation Kallar Grass 
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Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 1997

Authors and Affiliations

  • M. H. Rashid
    • 1
  • K. S. Siddiqui
    • 1
  1. 1.National Institute for Biotechnology and Genetic EngineeringFaisalabadPakistan

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