Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-9-16
pubmed:abstractText
A phosphotriesterase (PTE) capable of hydrolyzing organophosphate esters was purified from Escherichia coli strain DH-5 alpha carrying a cloned opd gene from Flavobacterium. The effects of pH, temperature and metal ion concentrations on enzyme stability and activity were investigated. Optimum conditions for PTE's catalytic activity were determined to be 35 degrees C and pH 8.5. Protein-metal equilibrium binding experiments showed that PTE could accommodate two equivalents of Co2+ or Zn2+ ions. PTE protein was found to have higher affinity for Co2+. In addition, Co2+ was found to possess the most positive effects in maintaining and restoring PTE's stability and catalytic activity when compared to other divalent metal ions. Assessment of the feasibility of PTE operation in a practical environment was performed in a system designed to mimic a continuously stirred tank reactor (CSTR) with different solution compositions in the flow reservoir. PTE was deactivated in 24 hours when the inflow solution contained 5% ethanol or 1 mM EDTA, while it retained one third of its initial activity in a deionized water stream. When the inflow solution contained 1 mM Co2+, PTE was found to retain activity throughout the 24-hour experiment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0360-1234
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
347-67
pubmed:dateRevised
2009-7-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Characterization of a phosphotriesterase from genetically-engineered Escherichia coli.
pubmed:affiliation
Department of Civil Engineering, University of Maryland, College Park, MD 20742, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.