Biochemical properties of a beta-xylosidase from Clostridium cellulolyticum.

نویسندگان

  • S Saxena
  • H P Fierobe
  • C Gaudin
  • F Guerlesquin
  • J P Belaich
چکیده

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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عنوان ژورنال:
  • Applied and environmental microbiology

دوره 61 9  شماره 

صفحات  -

تاریخ انتشار 1995