Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis

Teresa Fontes Leal, Isabel de Sá-Nogueira

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

Bacillus subtilis synthesizes at least one arabinanase encoded by the abnA gene that is able to degrade the polysaccharide arabinan. Here, we report the expression in Escherichia coli of the full-length abnA coding region with a His6-tag fused to the C-terminus. The recombinant protein was secreted to the periplasmic space and correctly processed by the E. coli signal peptidase. The substrate specificity of purified AbnA, the physico-chemical properties and kinetic parameters were determined. Functional analysis studies revealed Glu 215 as a key residue for AbnA hydrolytic activity and indicated that in addition to AbnA B. subtilis secretes other enzyme(s) able to degrade linear 1,5-alpha-l-arabinan.

Original languageEnglish
Pages (from-to)41-48
Number of pages8
JournalFEMS Microbiology Letters
Volume241
Issue number1
DOIs
Publication statusPublished - 1 Dec 2004

Keywords

  • Amino Acid Sequence
  • Bacillus subtilis
  • Escherichia coli
  • Glycoside Hydrolases
  • Molecular Sequence Data
  • Recombinant Proteins
  • Journal Article
  • Research Support, Non-U.S. Gov't

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