ArticleThe Biochemical journal1994
Purification and characterization of an alpha-L-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA).
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 45 citations in OpenAlex.
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.Biotechnology for biofuels · 2015Article
- Direct production of feruloyl oligosaccharides and hemicellulase inducement and distribution in a newly isolated Aureobasidium pullulans strain.World journal of microbiology & biotechnology · 2014Article
- Distinct actions by Paenibacillus sp. strain E18 α-L-arabinofuranosidases and xylanase in xylan degradation.Applied and environmental microbiology · 2013Article
- Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase.The Biochemical journal · 2001Article
- Genetic and biochemical characterization of a highly thermostable alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus.Applied and environmental microbiology · 2000Article
- Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains.The Biochemical journal · 1998Article
- Purification and characterization of a novel thermostable alpha-L-arabinofuranosidase from a color-variant strain of Aureobasidium pullulans.Applied and environmental microbiology · 1998Article
- Purification and properties of ArfI, an alpha-L-arabinofuranosidase from Cytophaga xylanolytica.Applied and environmental microbiology · 1998Article
- New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme.The Biochemical journal · 1997Article
- Cloning of genes encoding alpha-L-arabinofuranosidase and beta-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae.Applied and environmental microbiology · 1996Article
- Purification and characterization of two arabinofuranosidases from solid-state cultures of the fungus Penicillium capsulatum.Applied and environmental microbiology · 1996Article
- Purification and characterization of alpha-L-arabinofuranosidase from Bacillus stearothermophilus T-6.Applied and environmental microbiology · 1995Article
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The gene encoding an alpha-L-arabinofuranosidase (abfA) was homologously cloned in Streptomyces lividans and its DNA sequence was determined. The enzyme was purified from the cytoplasm of the hyperproducing clone S. lividans IAF116. Its M(r) was estimated by gel filtration and found to be approx. 380,000. Since SDS/PAGE indicated a native protein of M(r) 69,000, it can be concluded that the native protein consists of several subunits of that size. The pI value was 4.6. The kinetic constants determined with p-nitrophenyl alpha-L-arabinofuranoside as substrate were a Vmax of 180 units/mg of protein and a Km of 0.6 mM. The specific activity of the purified enzyme on this substrate was 153 units/mg of protein. Optimal enzyme activity was obtained at 60 degrees C and pH 6.0. The enzyme cleaved p-nitrophenyl alpha-L-arabinofuranoside, but had no activity on a variety of other p-nitrophenyl glycosides, except on p-nitrophenyl beta-D-xylopyranoside. The enzyme showed no activity on oat-spelts (Avena sativa) xylan or arabinogalactan, but acted on beet (Beta) arabinan or arabinoxylan. Hydrolysis occurred on arabino-oligoxylosides obtained from oat-splets xylan after digestion with xylanases. Since S. lividans normally does not secrete arabinofuranosidase, this enzyme may play a role in the assimilation of arabinose moieties from arabinose-containing xylo-oligosaccharides generated by beta-xylosidases or xylanases.
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