Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2009-8-5
pubmed:abstractText
A recombinant putative beta-galactosidase from Thermoplasma acidophilum was purified as a single 57 kDa band of 82 U mg(-1). The molecular mass of the native enzyme was 114 kDa as a dimer. Maximum activity was observed at pH 6.0 and 90 degrees C. The enzyme was unstable below pH 6.0: at pH 6 its half-life at 75 degrees C was 28 days but at pH 4.5 was only 13 h. Catalytic efficiencies decreased as p-nitrophenyl(pNP)-beta-D-fucopyranoside (1067) > pNP-beta-D-glucopyranoside (381) > pNP-beta-D-galactopyranoside (18) > pNP-beta-D-mannopyranoside (11 s(-1) mM(-1)), indicating that the enzyme was a beta-glycosidase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1573-6776
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1457-62
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Characterization of an acid-labile, thermostable beta-glycosidase from Thermoplasma acidophilum.
pubmed:affiliation
Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't