ArticleJournal of microbiology (Seoul, Korea)2012
Detailed modes of action and biochemical characterization of endo-arabinanase from Bacillus licheniformis DSM13.
Article in Journal of microbiology (Seoul, Korea), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Exo- and Endo-1,5-α-L-Arabinanases and Prebiotic Arabino-Oligosaccharides Production.Journal of microbiology and biotechnology · 2025Review
- Thermophilic Hemicellulases Secreted by Microbial Consortia Selected from an Anaerobic Digester.International journal of molecular sciences · 2024Article
- Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster ofInternational journal of molecular sciences · 2024Article
- Arabinan hydrolysis by GH43 enzymes of Hungateiclostridium clariflavum and the potential synergistic mechanisms.Applied microbiology and biotechnology · 2022Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An endo-arabinanase (BLABNase) gene from Bacillus licheniformis DSM13 was cloned and expressed in Escherichia coli, and the biochemical properties of its encoded enzyme were characterized. The BLABNase gene consists of a single open reading frame of 987 nucleotides that encodes 328 amino acids with a predicted molecular mass of about 36 kDa. BLABNase exhibited the highest activity against debranched α-(1,5)-arabinan in 50 mM sodium acetate buffer (pH 6.0) at 55°C. Enzymatic characterization revealed that BLABNase hydrolyzes debranched or linear arabinans with a much higher activity than branched arabinan from sugar beet. Enzymatic hydrolysis pattern analyses demonstrated BLABNase to be a typical endo-(1,5)-α-S-arabinanase (EC 3.2.1.99) that randomly cleaves the internal α-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated. Our results indicated that BLABNase acts preferentially along with the oligosaccharides longer than arabinopentaose, thus enabling the enzymatic production of various arabino-oligosaccharides.
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