Linked Life Data

11302177

Source:http://linkedlifedata.com/resource/pubmed/id/11302177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-4-13
pubmed:abstractText
Thermostability of thaumatin and mechanisms of thermoinactivation were examined at 80 degrees C in the pH range from 2 to 10. The sweetness of thaumatin disappeared on heating at pH above 7 for 15 min, but the sweetness remained even after heating at 80 degrees C for 4 h at pH 2. This indicated that the sweet protein thaumatin is more thermoresistant under acid conditions than under neutral or alkaline conditions. Prolonged heating of thaumatin under acid conditions slowly reduced sweetness, and produced a heterogeneous population of molecules, all of which was soluble and monomeric. The resultant molecules were clearly distinct from those generated by heating at pH above 7. Hydrolysis of peptide bonds and other irreversible chemical reactions slowly took place in the molecule heated under acid conditions, and it would be, in part, a cause of thermoinactivation of thaumatin under acid conditions. The thermostability of thaumatin and the mechanism of thermoinactivation were largely dependent on pH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
409-13
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Sweetness of sweet protein thaumatin is more thermoresistant under acid conditions than under neutral or alkaline conditions.
pubmed:affiliation
Research Institute for Food Science, Kyoto University, Uji, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't