rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1992-12-3
|
pubmed:abstractText |
Beta-glucosidase was purified from a crude cellulase preparation from Aspergillus niger by affinity chromatography on a methacrylamide-N-methylene-bis-methacrylamide copolymer bearing cellobiamine. The purified enzyme was a dimer with an isoelectric point of 4.0. The molecular mass of the enzyme was estimated to be 240 kDa by gel-permeation chromatography. The enzyme hydrolyzed specifically beta-glucosidic bonds and catalyzed transglucosylation of the beta-glucosyl group of cellobiose to yield 4-O-beta-gentiobiosylglucose in the presence of organic solvents or under neutral conditions.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0014-2956
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
209
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
651-9
|
pubmed:dateRevised |
2007-7-23
|
pubmed:meshHeading |
pubmed-meshheading:1425671-Aspergillus niger,
pubmed-meshheading:1425671-Carbohydrate Conformation,
pubmed-meshheading:1425671-Carbohydrate Sequence,
pubmed-meshheading:1425671-Chromatography, Affinity,
pubmed-meshheading:1425671-Chromatography, Gel,
pubmed-meshheading:1425671-Chromatography, Ion Exchange,
pubmed-meshheading:1425671-Kinetics,
pubmed-meshheading:1425671-Molecular Sequence Data,
pubmed-meshheading:1425671-Molecular Weight,
pubmed-meshheading:1425671-Oligosaccharides,
pubmed-meshheading:1425671-Substrate Specificity,
pubmed-meshheading:1425671-beta-Glucosidase
|
pubmed:year |
1992
|
pubmed:articleTitle |
Purification and properties of Aspergillus niger beta-glucosidase.
|
pubmed:affiliation |
Wood Research Institute, Kyoto University, Japan.
|
pubmed:publicationType |
Journal Article
|