期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 61, 期 6, 页码 1196-1204出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf303739n
关键词
Pisum; pea globulins; legumin 11S; vicilin 7S; heat-induced denaturation and aggregation; interaction
资金
- Ministere de l'Economie, des Finances et de l'Industrie (Direction Generale des Entreprises) of the French Government
- Le Grand Dijon
The heat-induced denaturation and aggregation of mixed pea globulins (8%, w/w) were investigated using differential scanning calorimetry (DSC), SDS-PAGE, and size-exclusion chromatography (SEC-HPLC). DSC data showed that the pea proteins denaturation temperature (T-d) was heating-rate dependent. The T-d value decreased by about 4 degrees C by lowering the heating rate from 10 to 5 degrees C/min. The SDS-PAGE analysis revealed that protein denaturation upon heating at 90 degrees C was mainly governed by noncovalent interaction. The SEC-HPLC measurements indicated that low-denatured legumin (approximate to 350-410 kDa) and vicilin/convicilin (approximate to 170 kDa) globulins were heat-denatured and most of their subunits reassociated into high-molecular weight, soluble aggregates (>700 kDa). The addition of N-ethylmaleimide slightly modified the aggregation route of pea globulins. However, partially insoluble macroaggregates were produced in the presence of dithiothreitol, reflecting the stabilizing effect of disulfide bonds within legumin subunits.
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