Linked Life Data

12017991

Source:http://linkedlifedata.com/resource/pubmed/id/12017991

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-20
pubmed:abstractText
Glycation by the Maillard reaction is an ubiquitous reaction of condensation of a reducing sugar with amino groups of proteins, which products could improve the functional and/or biological properties for food and non-food uses. It can induce structural modifications in proteins, modifying their properties. The aim of this work was to investigate the association behavior and the conformational changes of beta-lactoglobulin (BLG) after its glycation by the Maillard reaction with several alimentary sugars (arabinose, galactose, glucose, lactose, rhamnose and ribose). Protein samples were heated in the presence or in the absence (heated control) of different sugars during 3 days at 60 degrees C. Glycation induced oligomerization of BLG monomers. Depending on the reactivity of the sugar, the population of produced oligomers showed smaller or greater heterogeneity in molecular masses. Analysis of modified BLG by circular dichroism and by its susceptibility to pepsinolysis showed that the conditions of heating used did not significantly alter the conformation of BLG. Heating of BLG in presence of sugars induced only minor structural modification, when using the less reactive sugars such as lactose and rhamnose. It was, however, at the origin of major three-dimensional destructuring in the case of the more reactive sugars such as arabinose and ribose. Pepsinolysis of glycated BLG did not affect about 62 and 35% of the protein molecules modified with lactose or rhamnose, and arabinose or ribose, respectively. The increase of susceptibility of glycated BLG to pepsinolysis could be related to the alteration of the conformation of the protein when glycation was performed with highly reactive sugars, as observed by circular dichroism and calorimetry analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0027-769X
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
58-63
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Maillard glycation of beta-lactoglobulin induces conformation changes.
pubmed:affiliation
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, BP 71627, F-44316 Nantes, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't