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. 1995 Sep;61(9):3509–3512. doi: 10.1128/aem.61.9.3509-3512.1995

Biochemical properties of a beta-xylosidase from Clostridium cellulolyticum.

S Saxena 1, H P Fierobe 1, C Gaudin 1, F Guerlesquin 1, J P Belaich 1
PMCID: PMC167631  PMID: 7574661

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.

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Selected References

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