Linked Life Data

15508280

Source:http://linkedlifedata.com/resource/pubmed/id/15508280

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-10-28
pubmed:abstractText
Catalase enzyme (EC 1.11.1.6) was immobilized by entrapping in cellulose acetate beads. This organic matrix is highly resistant to mechanical stability and can be used under various conditions. Initial studies were conducted to examine the immobilization ability of catalase on the matrix previously activated with a series of reagent normally and the best results were obtained with the beads activated with Ce(SO4)2. In the optimization studies of the immobilized enzyme optimum pH and temperature were found as pH:7.0 (Tris-HCl, 50 mM) and 35 degrees C. In the characterization studies of the immobilized enzyme some parameters such as storage and thermal stability were investigated. Finally, the immobilized enzyme was used for the decomposition of hydrogen peroxide in milk samples and also by using a catalase biosensor prepared the decomposition level of hydrogen peroxide was detected.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1073-1199
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
443-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Catalase immobilization in cellulose acetate beads and determination of its hydrogen peroxide decomposition level by using a catalase biosensor.
pubmed:affiliation
Department of Biochemistry, Faculty of Science, Ege University, Bornova-Izmir, Turkey.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't