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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
1993-10-4
|
| pubmed:abstractText |
alpha-L-Arabinofuranosidase was purified from a cell-free extract of Aspergillus niger 5-16 by chromatographies on DEAE-Toyopearl, SP-Toyopearl, Ultro-gel AcA 44, Mono P, and TSK-Gel G3000SW. The final preparation thus obtained showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight and isoelectric point were 67,000 by SDS-polyacrylamide gel electrophoresis and pH 3.5 by isoelectric focusing. The alpha-L-arabinofuranosidase contained amino acids in the order of Asx > Gly > Ala > Thr > Glx = Ser. The enzyme had maximum activity at pH 4.0 and 60 degrees C, and was stable from pH 4 to 7 and at temperatures up to 30 degrees C. The enzyme activity was not affected considerably by either metal ions or chemical reagents. The enzyme released arabinose from p-nitrophenyl-alpha-L-arabinofuranoside, O-alpha-L-arabinofuranosyl-(1-->3)-O-beta-D-xylopyranosyl-(1-->4)-D- xylopyranose, and arabinan, but not from O-beta-D-xylopyranosyl-(1-->4)-O-[alpha-L-arabinofuranosyl- (1-->3)]-O-beta-D-xylopyranosyl-(1-->4)-D-xylopyranose, O-beta-D-xylopyranosyl-(1-->2)-O-alpha-L-arabinofuranosyl-(1-->3)-O-beta -D- xylopyranosyl-(1-->4)-O-beta-D-xylopyranosyl-(1-->4)-D-xylopyranose, gum arabic, or arabinoxylan. The limit of hydrolysis of arabinan was about 58% even when the enzyme was sufficiently in excess.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
B
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Arabinose,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Metals,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-N-arabinofuranosidase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0916-8451
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
57
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1161-5
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7763988-Amino Acids,
pubmed-meshheading:7763988-Arabinose,
pubmed-meshheading:7763988-Aspergillus niger,
pubmed-meshheading:7763988-Carbohydrate Sequence,
pubmed-meshheading:7763988-Chromatography, Gel,
pubmed-meshheading:7763988-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7763988-Enzyme Stability,
pubmed-meshheading:7763988-Glycoside Hydrolases,
pubmed-meshheading:7763988-Hydrogen-Ion Concentration,
pubmed-meshheading:7763988-Hydrolysis,
pubmed-meshheading:7763988-Isoelectric Point,
pubmed-meshheading:7763988-Metals,
pubmed-meshheading:7763988-Molecular Sequence Data,
pubmed-meshheading:7763988-Molecular Weight,
pubmed-meshheading:7763988-Oligosaccharides,
pubmed-meshheading:7763988-Polysaccharides,
pubmed-meshheading:7763988-Substrate Specificity,
pubmed-meshheading:7763988-Temperature
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Purification and some properties of intracellular alpha-L-arabinofuranosidase from Aspergillus niger 5-16.
|
| pubmed:affiliation |
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
|
| pubmed:publicationType |
Journal Article
|