Linked Life Data

7670194

Source:http://linkedlifedata.com/resource/pubmed/id/7670194

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1995-10-17
pubmed:abstractText
We purified a beta-glucosidase from the mutant strain Candida molischiana 35M5N. Analysis of the kinetic properties of this enzyme did not show any differences between the previously purified wild-type enzyme and that of the mutant. Nevertheless, a study of the stability of the enzyme at different pH levels and temperatures showed the increase resistance of this protein. This enzyme was found to be stable at pH 5 for 145 h and retained 78% of its initial activity after the same time at pH 3.5 (optimal pH) and 30 degrees C. This difference between the wild-type and the mutant enzyme could be explained by differences in the quantity or quality of glycosylation. This glycoprotein showed different forms after deglycosylation. Some peptides from this protein were also sequenced. An homology analysis found similarities between this beta-glucosidase and beta-glucosidases of Candida pelliculosa and Schizophyllum commune.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1320-2
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
A very stable beta-glucosidase from a Candida molischiana mutant strain: enzymatic properties, sequencing, and homology with other yeast beta-glucosidases.
pubmed:affiliation
Chaire de Microbiologie Industrielle et de Génétique des Micro-organismes, ENSA.M-INRA, Montpellier, France.
pubmed:publicationType
Journal Article