The mechanism underlying the freeze-thaw fractionation of 7S and 11S globulins in soymilk was investigated. Freeze-thawed soymilk demonstrated an increased particle size compared with raw soymilk. Further, when defatted raw soymilk was freeze-thawed, it was fractionated into 7S (supernatant) and 11S (precipitate) globulins, similar to what is found with freeze-thaw of raw soymilk. When raw soymilk samples with different ratios of 11S/7S were freeze-thawed, the 11S-deficient variety showed no precipitate. The addition of sodium sulphite or sodium dodecyl sulphate also inhibited precipitate formation after freeze-thawing, resulting in no fractionation. These results suggest that the fractionation is due to selective precipitation of aggregates of 11S globulins and/or 11S globulins and lipid complexes, in which the protein molecules interact through disulphide bonds and/or hydrophobic interactions.
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http://dx.doi.org/10.1016/j.foodchem.2013.01.103 | DOI Listing |
Food Chem
January 2025
National Institute of Agricultural Sciences, Rural Development Administration, Jeonju 54874, Republic of Korea. Electronic address:
Variations in the proportions of the two major soybean [Glycine max (L.) Merr.] seed globulins, glycinin (11S) and β-conglycinin (7S), significantly affect the nutritional and functional properties of soy-based products, but comprehensive methods for the identification and quantification of individual subunits of these proteins are currently lacking.
View Article and Find Full Text PDFUltrason Sonochem
January 2025
Department of Food Engineering, Heilongjiang Key Laboratory of Food Science and Engineering, Heilongjiang Key Laboratory of Grain Food and Comprehensive Processing, Harbin University of Commerce, Harbin 150028, Heilongjiang, China. Electronic address:
Heat facilitates aggregation and gel formation of soybean proteins. Ultrasonic reduces the size of protein aggregates. This study examined the impact of glycinin (11S) subunits on soybean lipophilic proteins (SLPs) gel formation and underlying mechanisms.
View Article and Find Full Text PDFJ Food Sci
December 2024
School of Biology and Food Engineering, Changshu Institute of Technology, Changshu, P.R. China.
Transglutaminase (TGase)-mediated cross-linking has gained significant attention due to its potential to reduce the allergenicity of food proteins. This study investigates the effects of TGase cross-linking on allergenicity and conformational modifications in a dual-protein system comprising soy protein isolate (SPI) and β-lactoglobulin (β-LG). The results showed that TGase cross-linking effectively decreased the allergenic potential of both SPI and β-LG, with a more pronounced reduction observed in the allergenicity of soy protein in the dual-protein system.
View Article and Find Full Text PDFCarbohydr Polym
February 2025
School of Food Science and Engineering, Hainan University, Haikou 570228, China. Electronic address:
Curr Res Food Sci
November 2024
INRAE, UR BIA, F-44316, Nantes, France.
The food transition towards an increased consumption of plant proteins aimed at limiting environmental impacts requires a diversification of plant protein sources. In this study, we explored the potentialities of the sustainable oilseed crop camelina to provide dietary proteins and to prepare oil-in-water emulsions. An innovative green refinery process, including the removal by ultrasound of the mucilage attached at the surface of the seeds and extraction by grinding in water at pH 8, was used to recover aqueous extracts containing camelina seed proteins.
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