Abstract
A 43.kDa β-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 β-xylosidases. By proton nuclear magnetic resonance spectroscopy, the enzyme was found to act by inverting the β-anomeric configuration.
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CITATION STYLE
Saxena, S., Fierobe, H. P., Gaudin, C., Guerlesquin, F., & Belaich, J. P. (1995). Biochemical properties of a β-xylosidase from Clostridium cellulolyticum. Applied and Environmental Microbiology, 61(9), 3509–3512. https://doi.org/10.1128/aem.61.9.3509-3512.1995
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