Linked Life Data

8782717

Source:http://linkedlifedata.com/resource/pubmed/id/8782717

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-12-19
pubmed:abstractText
The kinetics of adsorption and hydrolysis by an extracellular PHB depolymerase from Alcaligenes faecalis were studied at 37 degrees C on the surface of five types of polyhydroxyalkanoate (PHA) films. The films of poly[(R)-3-hydroxybutyrate] (P(3HP)), poly(3-hydroxypropionate) (P(3HP)), and poly(4-hydroxybutyrate)(P(4HB)) were hydrolyzed by the enzyme, while the films of poly[(S)-2-hydroxypropionate)(P(2HP)) and poly(6-hydroxyhexanoate)(P(6HH)) were not eroded. The PHB depolymerase with binding and catalytic domains adsorbed on the surface of all PHA films used, and the adsorption kinetics were found to obey the Langmuir isotherm. The cross-area per one molecule of enzyme binding to the surface of PHA film was estimated to be 17 +/- 8 (nm2/molecule). It has been concluded that the binding domain of enzyme is non-specific for the binding to the surface of PHA film, while the active site in a catalytic domain is specific for the hydrolysis of PHA molecules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0141-8130
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Adsorption kinetics of bacterial PHB depolymerase on the surface of polyhydroxyalkanoate films.
pubmed:affiliation
Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
pubmed:publicationType
Journal Article