Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-9-4
pubmed:abstractText
In this study, lipoxygenase from potato tuber has been purified by a method involving hydrophobic chromatography and the purified enzyme immobilized by covalent coupling to oxirane acrylic beads. The immobilized lipoxygenase exhibited increased long-term stability without a significant modification of the kinetic parameters. The comparative study on the effects of inhibitors such as dithizone, NDGA, phenidone, and beta-mercaptoethanol on the free and immobilized enzyme highlighted the importance of the lipoxygenase--support interaction, concluding that the immobilization process could cause the protection of the iron atom in the enzyme. The enzymatic specificity was maintained for the immobilized lipoxygenase, and their stability increased as compared to the free enzyme, making if feasible to use the enzyme in a multistep reaction to produce large quantities of leukotriene A4 or other related compounds of interest in the chemical industry and medicine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
8756-7938
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
394-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Immobilization of potato tuber lipoxygenase on oxirane acrylic beads.
pubmed:affiliation
Departmento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't