ArticleApplied and environmental microbiology1998
Purification and characterization of a novel thermostable alpha-L-arabinofuranosidase from a color-variant strain of Aureobasidium pullulans.
Article in Applied and environmental microbiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 55 citations in OpenAlex.
- An objective criterion to evaluate sequence-similarity networks helps in dividing the protein family sequence space.PLoS computational biology · 2023Article
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- Article
- Direct production of feruloyl oligosaccharides and hemicellulase inducement and distribution in a newly isolated Aureobasidium pullulans strain.World journal of microbiology & biotechnology · 2014Article
- Characterization of a new α-L: -arabinofuranosidase from Penicillium sp. LYG 0704, and their application in lignocelluloses degradation.Molecular biotechnology · 2011Article
- Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1.Protein science : a publication of the Protein Society · 2011Article
- Thermostable enzymes as biocatalysts in the biofuel industry.Advances in applied microbiology · 2010Review
- Mixed-species genomic microarray analysis of fecal samples reveals differential transcriptional responses of bifidobacteria in breast- and formula-fed infants.Applied and environmental microbiology · 2009Article
- Alpha-L-arabinofuranosidases: the potential applications in biotechnology.Journal of industrial microbiology & biotechnology · 2006Review
- Purification and functional characterization of a novel alpha-L-arabinofuranosidase from Bifidobacterium longum B667.Applied and environmental microbiology · 2003Article
- Purification and properties of a feruloyl esterase involved in lignocellulose degradation by Aureobasidium pullulans.Applied and environmental microbiology · 2003Article
- Hemicellulose bioconversion.Journal of industrial microbiology & biotechnology · 2003Review
Corrections and comments
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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
A color-variant strain of Aureobasidium pullulans (NRRL Y-12974) produced alpha-L-arabinofuranosidase (alpha-L-AFase) when grown in liquid culture on oat spelt xylan. An extracellular alpha-L-AFase was purified 215-fold to homogeneity from the culture supernatant by ammonium sulfate treatment, DEAE Bio-Gel A agarose column chromatography, gel filtration on a Bio-Gel A-0.5m column, arabinan-Sepharose 6B affinity chromatography, and SP-Sephadex C-50 column chromatography. The purified enzyme had a native molecular weight of 210,000 and was composed of two equal subunits. It had a half-life of 8 h at 75 degrees C, displayed optimal activity at 75 degrees C and pH 4.0 to 4.5, and had a specific activity of 21.48 mumol min-1. mg-1 of protein against p-nitrophenyl-alpha-L-arabinofuranoside (pNP alpha AF). The purified alpha-L-AFase readily hydrolyzed arabinan and debranched arabinan and released arabinose from arabinoxylans but was inactive against arabinogalactan. The K(m) values of the enzyme for the hydrolysis of pNP alpha AF, arabinan, and debranched arabinan at 75 degrees C and pH 4.5 were 0.26 mM, 2.14 mg/ml, and 3.25 mg/ml, respectively. The alpha-L-AFase activity was not inhibited at all by L-arabinose (1.2 M). The enzyme did not require a metal ion for activity, and its activity was not affected by p-chloromercuribenzoate (0.2 mM), EDTA (10 mM), or dithiothreitol (10 mM).
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