Improved fractionation of glycinin and beta-conglycinin and partitioning of phytochemicals.
نویسندگان
چکیده
Glycinin-rich and beta-conglycinin-rich products are prepared by soy protein fractionation. Physicochemical characteristics of these proteins affect their unique, important functionality in food systems and industrial applications. Soybean isoflavones and saponins are phytochemicals with potential health benefits. Objectives of this protein fractionation research were to (1) improve protein and phytochemical extraction from defatted soy flakes and recovery in product fractions and (2) evaluate phytochemical partitioning and profile changes during fractionation. Extraction environments (pH, ethanol concentration, temperature, and water-to-flake ratio) were each varied during bench-scale optimization. Optimized conditions of 45 degrees C and 10:1 water-to-flake ratio were compared with previous conditions of 20 degrees C and 15:1 water-to-flake ratio and a soy protein isolate process at pilot scale. Optimized conditions yielded more beta-conglycinin with higher isoflavone and saponin concentrations, but fraction purity was diminished by glycinin contamination. Bench-scale data demonstrated that increased phytochemical extraction did not translate into increased concentrations in product fractions.
منابع مشابه
Identification of glycinin and beta-conglycinin subunits that contribute to the increased protein content of high-protein soybean lines.
Seed protein concentration of commercial soybean cultivars calculated on a dry weight basis ranges from approximately 37 to 42% depending on genotype and location. A concerted research effort is ongoing to further increase protein concentration. Several soybean plant introductions (PI) are known to contain greater than 50% protein. These PIs are exploited by breeders to incorporate the high-pro...
متن کاملDifferential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth.
The degradation of the major seed storage globulins of the soybean (Glycine max [L.] Merrill) was examined during the first 12 days of germination and seedling growth. The appearance of glycinin and beta-conglycinin degradation products was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of cotyledon extracts followed by electroblotting to nitrocellulose and immunostaining...
متن کاملbeta-Conglycinin and glycinin in high-protein soybean seeds.
The agronomic performance and storage proteins of high seed protein lines of soybeans [Glycine max L. (Merr.)] were investigated to determine if the two major storage proteins, beta-conglycinin and glycinin, contribute to the increased protein content of high seed protein lines. Subunits of these two major storage proteins were estimated by scanning SDS-PAGE gels by scanning densitometry. The r...
متن کاملCosuppression of the alpha subunits of beta-conglycinin in transgenic soybean seeds induces the formation of endoplasmic reticulum-derived protein bodies.
The expression of the alpha and alpha' subunits of beta-conglycinin was suppressed by sequence-mediated gene silencing in transgenic soybean seed. The resulting seeds had similar total oil and protein content and ratio compared with the parent line. The decrease in beta-conglycinin protein was apparently compensated by an increased accumulation of glycinin. In addition, proglycinin, the precurs...
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ورودعنوان ژورنال:
- Journal of agricultural and food chemistry
دوره 52 6 شماره
صفحات -
تاریخ انتشار 2004