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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
|
| pubmed:dateCreated |
1999-3-22
|
| pubmed:abstractText |
The precise substrate specificities of an alpha-L-arabinofuranosidase from Trichoderma reesei were investigated. The enzyme released arabinose at appreciable rates from p-nitrophenyl-alpha-L-arabinofuranoside, O-alpha-L-arabinofuranosyl-(1-->3)-O-beta-D-xylopyranosyl-(1-->4) -D-xylopyranose (A1X2), arabinan, arabinoxylan, arabinogalactan, debranched-arabinan and gum arabic, but not from O-beta-D-xylopyranosyl-(1-->4)-[O-alpha-L-arabinofuranosyl-(1-->3)] -O-beta-D-xylopyranosyl-(1-->4)-D-xylopyranose (A1X3) or O-beta-D-xylopyranosyl-(1-->2)-O-alpha-L-arabinofuranosyl -(1-->3)-O-beta-D-xylopyranosyl-(1-->4)-O-beta-D-xylopyranosyl-(-->4) -D-xylopyranose (A1X4). The enzyme hydrolyzed methyl 2-O-, methyl 3-O- and methyl 5-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranosides to arabinose and methyl alpha-L-arabinofuranoside with the order of hydrolysis being: (1-->5)- > (1-->2)- > or = (1-->3)-linkages. The enzyme hydrolyzed the (1-->3)-linkage faster than the (1-->5)-linkage of methyl 3,5-di-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside. The degree of conversion of arabinan and debranched-arabinan to monosaccharides by the enzyme was 33.0% and 9.1%, respectively. The alpha-L-arabinofuranosidase preferentially cleaved the arabinosyl side-chain from the arabinan rather than the terminal arabinosyl residue of the arabinan backbone.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0916-8451
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
62
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2205-10
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9972241-Carbohydrate Conformation,
pubmed-meshheading:9972241-Carbohydrate Sequence,
pubmed-meshheading:9972241-Glycoside Hydrolases,
pubmed-meshheading:9972241-Glycosylation,
pubmed-meshheading:9972241-Hydrolysis,
pubmed-meshheading:9972241-Molecular Sequence Data,
pubmed-meshheading:9972241-Oligosaccharides,
pubmed-meshheading:9972241-Polysaccharides,
pubmed-meshheading:9972241-Substrate Specificity,
pubmed-meshheading:9972241-Trichoderma
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Substrate specificity of the alpha-L-arabinofuranosidase from Trichoderma reesei.
|
| pubmed:affiliation |
Institute of Applied Biochemistry, University of Tsukuba, Japan. sakaneko@nfri.affrc.go.jp
|
| pubmed:publicationType |
Journal Article
|