Title
Differences in denaturation of genetic variants of soy glycinin
Author
TNO Voeding
Lakemond, C.M.M.
de Jongh, H.H.J.
Gruppen, H.
Voragen, A.G.J.
Publication year
2002
Abstract
In heat denaturation studies conducted in the past the genetic variants of glycinin have been considered as a homogeneous group of proteins. In this work the validity of this assumption was tested. It was found by calorimetric studies that glycinin denatures heterogeneously at pH 7.6. When the temperature of isothermal treatment is increased from 70 to 82°C the proportion of glycinin remaining native progressively decreases from 95% to 5% while the denaturation temperature of the glycinin remaining native increases from 88.5 to 95°C. Similar trends were found for pH 3.8. Fractionation and subsequent analysis (MALDI-TOF and CE) of isothermally treated samples demonstrated that at pH 7.6 the heterogeneous denaturation is caused by differences in thermal stability of the genetic variants of glycinin. The stability increases in the order G2/G3/G1 < A4 < G5 < G4. Chemicals/CAS: glycinin, 9007-93-6; Globulins; glycinin, 9007-93-6; Soybean Proteins.
Subject
glycinin
calorimetry
capillary electrophoresis
chemistry
comparative study
drug stability
genetic variability
genetics
heating
mass spectrometry
matrix assisted laser desorption ionization time of flight mass spectrometry
pH
protein denaturation
protein modification
soybean
thermostability
Calorimetry
Drug Stability
Globulins
Heat
Hydrogen-Ion Concentration
Protein Denaturation
Soybean Proteins
Soybeans
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Variation (Genetics)
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DOI
https://doi.org/10.1021/jf0110405
TNO identifier
236608
ISSN
0021-8561
Source
Journal of Agricultural and Food Chemistry, 50 (50), 4275-4281
Document type
article