Related Experiment Videos
Biochemical properties of a beta-xylosidase from Clostridium cellulolyticum
S Saxena1, H P Fierobe, C Gaudin
1Laboratoire de Biochimie et Génétique Moléculaire des Anaérobies, IFRC1, Centre National de la Recherche Scientifique, Marseille, France.
Applied and Environmental Microbiology
|September 1, 1995
Abstract:
A 43-kDa beta-xylosidase from Clostridium cellulolyticum was purified to homogeneity. The enzyme releases xylose from p-nitrophenylxylose and xylodextrins with a degree of polymerization ranging between 2 and 5. The N-terminal amino acid sequence of the enzyme showed homologies with three other bacterial beta-xylosidases. By proton nuclear magnetic resonance spectroscopy, the enzyme was found to act by inverting the beta-anomeric configuration.