Source:http://linkedlifedata.com/resource/pubmed/id/16944135
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2006-11-28
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| pubmed:abstractText |
A novel alpha-L-arabinofuranosidase (alpha-AraF) belonging to glycoside hydrolase (GH) family 43 was cloned from Humicola insolens and expressed in Aspergillus oryzae. (1)H-NMR analysis revealed that the novel GH43 enzyme selectively hydrolysed (1-->3)-alpha-L-arabinofuranosyl residues of doubly substituted xylopyranosyl residues in arabinoxylan and in arabinoxylan-derived oligosaccharides. The optimal activity of the cloned enzyme was at pH 6.7 and 53 degrees C. Two other novel alpha-L-arabinofuranosidases (alpha-AraFs), both belonging to GH family 51, were cloned from H. insolens and from the white-rot basidiomycete Meripilus giganteus. Both GH51 enzymes catalysed removal of (1-->2) and (1-->3)-alpha-L-arabinofuranosyl residues from singly substituted xylopyranosyls in arabinoxylan; the highest arabinose yields were obtained with the M. giganteus enzyme. Combinations (50:50) of the GH43 alpha-AraF from H. insolens and the GH51 alpha-AraFs from either M. giganteus or H. insolens resulted in a synergistic increase in arabinose release from water-soluble wheat arabinoxylan in extended reactions at pH 6 and 40 degrees C. This synergistic interaction between GH43 and GH51 alpha-AraFs was also evident when a GH43 alpha-AraF from a Bifidobacterium sp. was supplemented in combination with either of the GH51 enzymes. The synergistic effect is presumed to be a result of the GH51 alpha-AraFs being able to catalyse the removal of single-sitting (1-->2)-alpha-L- arabinofuranosyls that resulted after the GH43 enzyme had catalysed the removal of (1-->3)-alpha-L-arabinofuranosyl residues on doubly substituted xylopyranosyls in the wheat arabinoxylan.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabinose,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Xylans,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-N-arabinofuranosidase,
http://linkedlifedata.com/resource/pubmed/chemical/arabinoxylan
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0175-7598
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
73
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
850-61
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| pubmed:meshHeading |
pubmed-meshheading:16944135-Amino Acid Sequence,
pubmed-meshheading:16944135-Arabinose,
pubmed-meshheading:16944135-Ascomycota,
pubmed-meshheading:16944135-Aspergillus oryzae,
pubmed-meshheading:16944135-Bifidobacterium,
pubmed-meshheading:16944135-Cloning, Molecular,
pubmed-meshheading:16944135-Enzyme Stability,
pubmed-meshheading:16944135-Gene Expression,
pubmed-meshheading:16944135-Glycoside Hydrolases,
pubmed-meshheading:16944135-Hydrogen-Ion Concentration,
pubmed-meshheading:16944135-Magnetic Resonance Spectroscopy,
pubmed-meshheading:16944135-Molecular Sequence Data,
pubmed-meshheading:16944135-Oligosaccharides,
pubmed-meshheading:16944135-Polyporales,
pubmed-meshheading:16944135-Sequence Alignment,
pubmed-meshheading:16944135-Substrate Specificity,
pubmed-meshheading:16944135-Temperature,
pubmed-meshheading:16944135-Triticum,
pubmed-meshheading:16944135-Xylans
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| pubmed:year |
2006
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| pubmed:articleTitle |
A novel GH43 alpha-L-arabinofuranosidase from Humicola insolens: mode of action and synergy with GH51 alpha-L-arabinofuranosidases on wheat arabinoxylan.
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| pubmed:affiliation |
Novozymes A/S, Krogshøjvej 36, 2880 Bagsvaerd, Denmark.
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| pubmed:publicationType |
Journal Article
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