Linked Life Data

15993389

Source:http://linkedlifedata.com/resource/pubmed/id/15993389

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2005-7-15
pubmed:abstractText
A novel colanic acid-degrading enzyme was isolated from a mixed culture filtrate obtained by enrichment culturing of a compost sample using colanic acid as carbon source. The enzyme was partially purified resulting in a 17-fold increase in specific activity. Further purification by Native PAGE revealed that the enzyme is part of a high-molecular weight multi protein complex of at least six individual proteins. The enzyme showed a temperature optimum at 50 degrees C while after 5h at 50 degrees C and pH7 still 70% of the total activity was left. The pH optimum was found to be pH7. Analysis of the degradation products showed that the enzyme is a novel 1,4-beta-fucoside hydrolase that liberates repeating units of colanic acid with varying degrees of acetylation. Km and Vmax of the enzyme were determined against the native substrate as well as its de-O-acetylated and depyruvated forms. Compared to the native substrate the affinity of the enzyme for the modified substrates was much lower. However, for the de-O-acetylated sample a dramatic increase in catalytic efficiency was observed. The native form of the substrate showed substrate inhibition at high concentrations, probably due to the formation of nonproductive substrate complexes. Removal of the acetyl groups probably prevents this effect resulting in a higher catalytic efficiency.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0008-6215
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
340
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1780-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15993389-Anions, pubmed-meshheading:15993389-Carbohydrate Conformation, pubmed-meshheading:15993389-Catalysis, pubmed-meshheading:15993389-Chromatography, pubmed-meshheading:15993389-Chromatography, Ion Exchange, pubmed-meshheading:15993389-Dose-Response Relationship, Drug, pubmed-meshheading:15993389-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15993389-Glycoside Hydrolases, pubmed-meshheading:15993389-Hydrogen-Ion Concentration, pubmed-meshheading:15993389-Kinetics, pubmed-meshheading:15993389-Mass Spectrometry, pubmed-meshheading:15993389-Models, Chemical, pubmed-meshheading:15993389-Polysaccharides, pubmed-meshheading:15993389-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:15993389-Substrate Specificity, pubmed-meshheading:15993389-Temperature, pubmed-meshheading:15993389-alpha-L-Fucosidase
pubmed:year
2005
pubmed:articleTitle
Characterisation of a 1,4-beta-fucoside hydrolase degrading colanic acid.
pubmed:affiliation
Wageningen University, Department of Agrotechnology and Food Sciences, Laboratory of Food Chemistry, Bomenweg 2, 6703 HD Wageningen, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't