Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-1-19
pubmed:abstractText
Recently, four external invertase isoforms (EINV1, EINV2, EINV3, and EINV4) have been isolated from S. cerevisiae. However, there is nothing known about their structural features and thermodynamics of unfolding. Since this information is essential for understanding their functioning at the molecular level as well as applicable in the food industry, we investigated guanidinium-chloride induced structural changes of the isoforms by CD and fluorescence spectroscopy. The resulting unfolding curves measured for each isoform at different temperatures were described simultaneously by a reversible two-state model to obtain the corresponding thermodynamic parameters. Here, we show that they are different for different isoforms and demonstrate that they correlate with the surface charge density of the native isoforms which follows the order EINV1 < EINV2 < EINV3 < EINV4. It appears that at physiological temperatures the thermodynamic stability of the isoforms follows the same order, while above 55 °C, the order is the opposite EINV1 > EINV2 > EINV3 ? EINV4. This suggests that increasing the efficiency of the food industry processes involving invertase would require the application of EINV3 and/or EINV4 at physiological temperatures and EINV1 at elevated temperatures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1520-5118
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
727-32
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Thermodynamics and structural features of the yeast Saccharomyces cerevisiae external invertase isoforms in guanidinium-chloride solutions.
pubmed:affiliation
Department of Chemistry, Institute for Chemistry, Technology and Metallurgy, University of Belgrade, Studentski trg 12-16, 11000 Belgrade, Serbia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't