A new thermostable alpha-L-arabinofuranosidase from a novel thermophilic bacterium

Research output: Contribution to journalArticle


An alpha-L-arabinofuranosidase gene was identified in a sequenced genome of a novel thermophilic bacterium, which belongs to the recently described phylum of Thermomicrobia. Amino acid sequence comparison of the enzyme (designated AraF) revealed similarity to glycoside hydrolases of family 51. The gene was cloned into Escherichia coli and its recombinant product expressed and purified. The enzyme appeared to be a hexamer. AraF was optimally active at 70degreesC (over 10 min) and pH 6 having 92% residual activity after 1 h at 70degreesC. AraF had a K-m value of 0.6 rum and V-max value of 122 U mg(-1) on p-nitrophenyl-alpha-L-arabinofuranoside. AraF was almost equally active on branched arabinan and debranched arabinan, properties not previously found in alpha-L-arabinofuranosidases in GH family 51.


  • Hakon Birgisson
  • O Fridjonsson
  • F K Bahrani-Mougeot
  • G O Hreggvidsson
  • J K Kristjansson
  • Bo Mattiasson
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Industrial Biotechnology
Original languageEnglish
Pages (from-to)1347-1351
JournalBiotechnology Letters
Issue number17
Publication statusPublished - 2004
Publication categoryResearch