Abstract：
:The gene encoding α-L-arabinofuranosidase (AFase) from Paenibacillus sp. DG-22 was cloned, sequenced, and expressed in Escherichia coli. The AFase gene (abfA) comprises a 1,509 bp open reading frame encoding 502 amino acids with a molecular mass of 56,520 daltons. The deduced amino acid sequence of the gene shows that AbfA is an enzyme consisting of only a catalytic domain, and that the enzyme has significant similarity to AFases classified into the family 51 of the glycosyl hydrolases. abfA was subcloned into the pQE60 expression vector to fuse it with a six-histidine tag and the recombinant AFase (rAbfA) was purified to homogeneity. The specific activity of the recombinant enzyme was 96.7 U/mg protein. Determination of the apparent molecular mass by gel-filtration chromatography indicated that AbfA has a tetrameric structure. The optimal pH and temperature of the enzyme were 6.0 and 60°C, respectively. The enzyme activity was completely inhibited by 1 mM HgCl2. rAbfA was active only towards p-nitrophephenyl α-L-arabinofuranoside and exhibited Km and Vmax values of 3.5 mM and 306.1 U/mg, respectively. rAbfA showed a synergistic effect in combination with endoxylanase on the degradation of oat spelt xylan and wheat arabinoxylan.
journal_name
J Microbiol Biotechnoljournal_title
Journal of microbiology and biotechnologyauthors
Lee SH,Lee YEdoi
10.4014/jmb.1308.08078subject
Has Abstractpub_date
2014-02-28 00:00:00pages
236-44issue
2eissn
1017-7825issn
1738-8872pii
10.4014/jmb.1308.08078journal_volume
24pub_type
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