ArticleApplied and environmental microbiology1998
Purification and substrate specificities of two alpha-L-arabinofuranosidases from Aspergillus awamori IFO 4033.
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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12 citing papers in PubMed.
- Structures of endo-1,5-α-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Genomics review of holocellulose deconstruction by aspergilli.Microbiology and molecular biology reviews : MMBR · 2014Review
- Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.The Journal of biological chemistry · 2014Article
- Characterization of a new α-L: -arabinofuranosidase from Penicillium sp. LYG 0704, and their application in lignocelluloses degradation.Molecular biotechnology · 2011Article
- Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo- and endo-type enzymes in glycoside hydrolase family 43.The Journal of biological chemistry · 2010Article
- Novel bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase (ABF3) from Penicillium purpurogenum.Applied and environmental microbiology · 2010Article
- Characterization of a modular enzyme of exo-1,5-alpha-L-arabinofuranosidase and arabinan binding module from Streptomyces avermitilis NBRC14893.Applied microbiology and biotechnology · 2008Article
- Mutagenesis and mechanistic study of a glycoside hydrolase family 54 alpha-L-arabinofuranosidase from Trichoderma koningii.The Biochemical journal · 2007Article
- The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose.The Biochemical journal · 2006Article
- Alpha-L-arabinofuranosidases: the potential applications in biotechnology.Journal of industrial microbiology & biotechnology · 2006Review
- Genetic and biochemical characterization of a highly thermostable alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus.Applied and environmental microbiology · 2000Article
- Purification, characterization and gene cloning of two alpha-L-arabinofuranosidases from streptomyces chartreusis GS901.The Biochemical journal · 2000Article
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6 authors.
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Abstract
alpha-L-Arabinofuranosidases I and II were purified from the culture filtrate of Aspergillus awamori IFO 4033 and had molecular weights of 81,000 and 62,000 and pIs of 3.3 and 3.6, respectively. Both enzymes had an optimum pH of 4.0 and an optimum temperature of 60 degreesC and exhibited stability at pH values from 3 to 7 and at temperatures up to 60 degrees C. The enzymes released arabinose from p-nitrophenyl-alpha-L-arabinofuranoside, O-alpha-L-arabinofuranosyl-(1-->3)-O-beta-D-xylopyranosyl-(1-->4)-D-x ylopyranose, and arabinose-containing polysaccharides but not from O-beta-D-xylopyranosyl-(1-->2)-O-alpha-L-arabinofuranosyl-(1-->3)-O-b eta-D-xylopyranosyl-(1-->4)-O-beta-D-xylopyranosyl-(1-->4)-D-xylopyra nose. alpha-L-Arabinofuranosidase I also released arabinose from O-beta-D-xylopy-ranosyl-(1-->4)-[O-alpha-L-arabinofuranosyl- (1-->3)]- O-beta-D-xylopyranosyl-(1-->4)-D-xylopyranose. However, alpha-L-arabinofuranosidase II did not readily catalyze this hydrolysis reaction. alpha-L-Arabinofuranosidase I hydrolyzed all linkages that can occur between two alpha-L-arabinofuranosyl residues in the following order: (1-->5) linkage > (1-->3) linkage > (1-->2) linkage. alpha-L-Arabinofuranosidase II hydrolyzed the linkages in the following order: (1-->5) linkage > (1-->2) linkage > (1-->3) linkage. alpha-L-Arabinofuranosidase I preferentially hydrolyzed the (1-->5) linkage of branched arabinotrisaccharide. On the other hand, alpha-L-arabinofuranosidase II preferentially hydrolyzed the (1-->3) linkage in the same substrate. alpha-L-Arabinofuranosidase I released arabinose from the nonreducing terminus of arabinan, whereas alpha-L-arabinofuranosidase II preferentially hydrolyzed the arabinosyl side chain linkage of arabinan.
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