ArticleApplied and environmental microbiology2003
Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium longum B667.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 108 citations in OpenAlex.
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- Utilization of diverse oligosaccharides for growth by Bifidobacterium and Lactobacillus species and their in vitro co-cultivation characteristics.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- β-l-ACS chemical biology · 2023Article
- Metatranscriptomic analysis of the gut microbiome of black soldier fly larvae reared on lignocellulose-rich fiber diets unveils key lignocellulolytic enzymes.Frontiers in microbiology · 2023Article
- Hydrolysis of Arabinoxylo-oligosaccharides by α-L-Arabinofuranosidases and β-D-Xylosidase fromJournal of microbiology and biotechnology · 2022Article
- Bifidobacterium castoris strains isolated from wild mice show evidence of frequent host switching and diverse carbohydrate metabolism potential.ISME communications · 2022Article
- Biochemical and Molecular Dynamics Study of a Novel GH 43 α-l-Arabinofuranosidase/β-Xylosidase FromFrontiers in bioengineering and biotechnology · 2022Article
- Potential applications of recombinant bifidobacterial proteins in the food industry, biomedicine, process innovation and glycobiology.Food science and biotechnology · 2021Review
- Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic YeastJournal of microbiology and biotechnology · 2021Article
- Plant Glycan Metabolism by Bifidobacteria.Frontiers in microbiology · 2021Review
- Multiple Transporters and Glycoside Hydrolases Are Involved in Arabinoxylan-Derived Oligosaccharide Utilization in Bifidobacterium pseudocatenulatum.Applied and environmental microbiology · 2020Article
- Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris.Applied microbiology and biotechnology · 2020Article
- Molecular Characterization, Regioselective and Synergistic Action of First Recombinant Type III α-L-arabinofuranosidase of Family 43 Glycoside Hydrolase (PsGH43_12) from Pseudopedobacter saltans.Molecular biotechnology · 2020Article
- Revisiting the Metabolic Capabilities ofMicroorganisms · 2020Article
- Identification of a Key Enzyme for the Hydrolysis of β-(1→3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide fromMarine drugs · 2020Article
- Characterisation of novel biomass degradation enzymes from the genome of Cellulomonas fimi.Enzyme and microbial technology · 2018Article
- Characterisation of a Hydroxycinnamic Acid Esterase From theFrontiers in microbiology · 2018Article
- A novel trifunctional, family GH10 enzyme from Acidothermus cellulolyticus 11B, exhibiting endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities.Extremophiles : life under extreme conditions · 2018Article
- Comparative Genomics Reveals the Regulatory Complexity of Bifidobacterial Arabinose and Arabino-Oligosaccharide Utilization.Frontiers in microbiology · 2018Article
- A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose.Microbial cell factories · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gene encoding a novel alpha-L-arabinofuranosidase from Bifidobacterium longum B667, abfB, was cloned and sequenced. The deduced protein had a molecular mass of about 61 kDa, and analysis of its amino acid sequence revealed significant homology and conservation of different catalytic residues with alpha-L-arabinofuranosidases belonging to family 51 of the glycoside hydrolases. Regions flanking the gene comprised two divergently transcribed open reading frames coding for hypothetical proteins involved in sugar metabolism. A histidine tag was introduced at the C terminus of AbfB, and the recombinant protein was overexpressed in Lactococcus lactis under control of the tightly regulated, nisin-inducible nisA promoter. The enzyme was purified by nickel affinity chromatography. The molecular mass of the native protein, as determined by gel filtration, was about 260 kDa, suggesting a homotetrameric structure. AbfB was active at a broad pH range (pH 4.5 to 7.5) and at a broad temperature range (20 to 70 degrees C), and it had an optimum pH of 6.0 and an optimum temperature of 45 degrees C. The enzyme seemed to be less thermostable than most previously described arabinofuranosidases and had a half-life of about 3 h at 55 degrees C. Chelating and reducing agents did not have any effect on its activity, but the presence of Cu(2+), Hg(2+), and Zn(2+) markedly reduced enzymatic activity. The protein exhibited a high level of activity with p-nitrophenyl alpha-L-arabinofuranoside, with apparent K(m) and V(max) values of 0.295 mM and 417 U/mg, respectively. AbfB released L-arabinose from arabinan, arabinoxylan, arabinobiose, arabinotriose, arabinotetraose, and arabinopentaose. No endoarabinanase activity was detected. These findings suggest that AbfB is an exo-acting enzyme and may play a role, together with other glycosidases, in the degradation of L-arabinose-containing polysaccharides.
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