Journal of Thermal Analysis and Calorimetry
Volume/Issue:
Volume 89: Issue 3
Thermal properties of globulin from buckwheat ( Fagopyrum esculentum Moench)
Effects of salts and protein perturbants
Author:
C. Tang South China University of Technology Department of Food Science and Technology Guangzhou 510640 P. R. China

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Pages:
941–951
Online Publication Date:
11 Jul 2007
Publication Date:
01 Sep 2007
Article Category:
Research Article
DOI:
https://doi.org/10.1007/s10973-005-7376-2
Keywords:
buckwheat proteins; denaturation; DSC; Fagopyrum esculentum Moench; globulin
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Abstract  

The thermal properties of buckwheat (Fagopyrum esculentum Moench) proteins with different lipid contents (2.5, 6.5 and 17.8%) were studied by differential scanning calorimetry (DSC) under various medium conditions. From DSC curves, many DSC characteristics including denaturation temperature (Td), enthalpy change (ΔH) and the width at half peak height (ΔT1/2) of endothermic peaks were obtained and evaluated. The DSC curves of various buckwheat proteins (BWPs) in the 0.05 M phosphate buffer (pH 7.0) showed a major endotherm at about 102°C and a minor endotherm at about 80°C, attributed to thermal transitions of 13S and 8S globulins, respectively. Td and ΔH of the globulins of BWPs were independent of their lipid contents, while the presence of high lipid content (17.8%) to some extent increased the ΔT1/2. The progressive increase in Td of 13S globulins with increase in NaCl concentration, suggests a more compact conformation with higher thermal stability. The influence of chaotropic salts on the DSC characteristics of 13S globulins was also independent of their lipid contents. Thermal analysis of the 13S globulins in the presence of protein perturbants (including urea, sodium dodecyl sulfate, ethylene glycol, dithiothreitol and N-ethylmaleimide) indicated that hydrophobic and hydrogen bondings are the major interactions for stabilizing protein conformation of buckwheat 13S globulins and the SS-SH interchange also attributes to the stabilization of the protein conformation.

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Cover Journal of Thermal Analysis and Calorimetry
Journal of Thermal Analysis and Calorimetry
Print ISSN:
1388-6150
Online ISSN:
1572-8943

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation		 1969
Volumes
per Year		 1
Issues
per Year		 24
Founder Akadémiai Kiadó
Founder's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher		 Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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