Linked Life Data

486717

Source:http://linkedlifedata.com/resource/pubmed/id/486717

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1979-12-20
pubmed:abstractText
The investigated catalyst system consists of immobilized Arthrobacter cells containing the enzyme glucose isomerase, which catalyzes the isomerization of glucose into fructose. The internal structure of the catalyst was determined from electrom microscope photographs of replicas of freeze-etched catalyst. On the basis of the photographs a model for the internal structure of the catalyst was proposed. This structure was subsequently used to describe the reaction including mass-transfer effects. It appeared that under normal operating conditions the external mass-transfer rate does not influence the overall rate of reaction. The effect of internal mass-transfer resistances on the overall reaction rate can well be accounted for by the so-called porous sphere model. The intrinsic kinetics of the isomerization catalyzed by the present catalyst system can be represented by a modified Michaelis-Menten equation for a reversible one-substrate reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3592
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1711-24
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Mass-transfer effects on the rate of isomerization of D-glucose into D-fructose, catalyzed by whole-cell immobilized glucose isomerase.
pubmed:publicationType
Journal Article