1991
DOI: 10.1021/jf00006a004
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Electrophoretic, solubility and functional properties of commercial soy protein isolates

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Cited by 137 publications
(116 citation statements)
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“…The WSI of soya bean fl our and soya and maize concentrates was around 35 %, while that of the hydrolysates (02 and 09) ranged from 32.71 to 95.65 %. Arrese et al (6) reported the WSI values of soya proteins of 36.3 to 83.6 % and according to Tomotake et al (5), WSI of a buckwheat isolate at similar pH value as used in our study was around 50 %, followed by the soya protein isolate, with values below 20 % and that of peanut fl our of 30 % (12). Therefore, the values of WSI obtained in some analyzed samples (Table 2) are higher than those reported for similar products.…”
Section: Functional Analysis Of Vegetable and Cereal Proteinssupporting
confidence: 63%
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“…The WSI of soya bean fl our and soya and maize concentrates was around 35 %, while that of the hydrolysates (02 and 09) ranged from 32.71 to 95.65 %. Arrese et al (6) reported the WSI values of soya proteins of 36.3 to 83.6 % and according to Tomotake et al (5), WSI of a buckwheat isolate at similar pH value as used in our study was around 50 %, followed by the soya protein isolate, with values below 20 % and that of peanut fl our of 30 % (12). Therefore, the values of WSI obtained in some analyzed samples (Table 2) are higher than those reported for similar products.…”
Section: Functional Analysis Of Vegetable and Cereal Proteinssupporting
confidence: 63%
“…Currently there is a lot of information regarding functional properties of proteins starting with the overwhelming general data about soya and oilseed-derived materials (4,6,7). Several authors have compared the physicochemical and functional properties of buckwheat protein, soya protein isolate and casein (5,6,8).…”
Section: Introductionmentioning
confidence: 99%
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“…Many authors [1,4,7,8] have studied the effect of heath treatment under different conditions on different functional properties of soy isolates. It has been reported that the functionality depends basically on the degree of dissociation, denaturation, and aggregation of the glycinin and β-congycinin [9,10]. Also, as an indicator of modification during preparation processes of commercial and laboratory-prepared soy protein isolates, has been recognized the relationship between solubility and surface hydrophobicity [11].…”
Section: Introductionmentioning
confidence: 99%
“…Gel formation is not beneficial in fibre spinning with a number of studies reported in the literature on the thermal denaturation of soybean (German et al, 1982;Petruccelli and Anon, 1995;Sorgentini et al, 1995). In addition, the denaturation temperatures of β-conglycinin and glycinin have been reported to be in the 72-80 o C and 85-95 o C range, respectively (Arrese et al 1991;Berli et al, 1999). Zhang et al (2003) reported benefits in terms of viscosity stability when thermal denaturation was used compared to alkali denaturation in the spinning of PVA/soybean blend fibres.…”
Section: Thermal Denaturationmentioning
confidence: 99%