Debranching of arabinoxylan: properties of the thermoactive recombinant α-L-arabinofuranosidase fromClostridium stercorarium (ArfB) |
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Authors: | W H Schwarz K Bronnenmeier B Krause F Lottspeich W L Staudenbauer |
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Institution: | 1. Institut für Mikrobiologie, Technische Universit?t München, Arcisstr. 21, D-80290, München, Germany 2. Max-Planck-Institut für Biochemie, D-82143, Martinsried, Germany
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Abstract: | The gene arfB encoding α-L-arabino-furanosidase B of the cellulolytic thermophile Clostridium stercorarium was expressed in Escherichia coli from a 2.2-kb EcoRI DNA fragment. The recombinant gene product ArfB was purified by fast-performance liquid chromatography. It has a tetrameric
structure with a monomeric relative molecular mass of 52 00. The optima for temperature and pH are 70 °C and 5.0 respectively.
The enzyme appears to have no metal cofactor requirement and is sensitive to sulfhydryl reagents. It hydrolyzes aryl and alkyl
α-L-arabinofuranosides and cleaves arabinosyl side-chains from arabinoxylan (oat-spelt xylan) and from xylooligosaccharides produced
by recombinant endoxylanase XynA from the same organism. The identity of the N-terminal amino acid sequences indicates that
ArfB corresponds to the major α-arabinosidase activity present in the culture supernatant of C. stercorarium.
Received: 30 September 1994/Received revision: 24 November 1994/Accepted: 16 December 1994 |
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