Linked Life Data

7093285

Source:http://linkedlifedata.com/resource/pubmed/id/7093285

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-9-24
pubmed:abstractText
An acidic endo-1,4-beta-xylanase (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) of Aspergillus niger catalyzes degradation of linear 1,4-beta-xylooligosaccharides by multiple reaction pathways analogous to those catalyzed by lysozyme and alpha-amylases. Quantitative product analysis of enzyme-substrate mixtures using 1-3H-reducing end-labeled xylooligosaccharides and [U-14C]xylotriose led to the following conclusions: (1) bond cleavage frequencies of xylotriose, xylotetraose and xylopentaose are strongly dependent on substrate concentration; (2) at relatively low concentration of the oligosaccharides the enzyme catalyzes transglycosylic reactions leading to products larger than the substrates; (3) xylobiose and to a low extent also xylose, are utilized as glycosyl acceptors in the transfer reactions; (4) the enzyme-glycosyl intermediates effective in the transfer reactions are formed only from the non-reducing part of oligosaccharides, since no evidence was obtained for condensation of two molecules of oligosaccharides; (5) the enzyme does not catalyze degradation of xylobiose and aryl beta-xylosides at an appreciable rate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
704
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
114-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Reaction pathways of substrate degradation by an acidic endo-1,4-beta-xylanase of Aspergillus niger.
pubmed:publicationType
Journal Article