Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties

Zheng, Haixue; Yang, Xiaoquan; Tang, Chuan-He; Li, Lin; Ahmad, Ijaz

doi:10.1016/j.foodres.2007.10.013

Cited by 47 publications

(29 citation statements)

References 34 publications

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“…EAI and ESI were determined using the method described by Zheng et al [21] with slight modifications, which consisted of mixing 10 mg of the protein isolates with 10 mL of distilled water together with 3.33 mL of canola oil. The pH of the dispersion was adjusted in a range of 2.0-10.0 by the addition of HCl (0.1 N) or NaOH (0.1 N) according to the case.…”

Section: Emulsion Activity Index (Eai) and Emulsion Stability Index (mentioning

confidence: 99%

Functional Properties of Lupinus angustifolius Seed Protein Isolates

Lara-Rivera

García-Alamilla

Lagunes-Gálvez

et al. 2017

Journal of Food Quality

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Protein isolates prepared by alkaline solubilization followed by isoelectric precipitation and freeze-drying from six varieties of Lupinus angustifolius (Haags Blaue, Sonate, Probor, Borlu, Boregine, and Boruta) grown in Mexico were evaluated for functional properties: nitrogen solubility, water-holding capacity (WHC), oil holding capacity (OHC), emulsion activity index (EAI), emulsion stability index (ESI), foaming capacity (FC), foam stability (FS), and gelling minimum concentration (GMC). The nitrogen solubility values, WHC, OHC, and FC did not show significant differences between the protein isolates. The solubility of the isolates was minimal at pH of 4.0 and 5.0 while the regions of maximum solubility were found at pH of 2.0 and 10.0. There were significant differences in EAI and ESI depending on the varieties used. The isolates of the Boregine and Borlu varieties showed the highest EAI with 29.3 and 28.3 m 2 g −1 , respectively, while the lowest index was recorded in the isolate obtained from the Sonate variety (24.6 m 2 g −1 ). Like solubility, these indices also increased at both extremes of pH evaluated; both properties were minimal in the isoelectric pH range (4.0 to 5.0).

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Section: Emulsion Activity Index (Eai) and Emulsion Stability Index (mentioning

confidence: 99%

Functional Properties of Lupinus angustifolius Seed Protein Isolates

Lara-Rivera

García-Alamilla

Lagunes-Gálvez

et al. 2017

Journal of Food Quality

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“…Sunflower protein solubility profiles were determined according to the method described by Zheng, Yang, Tnag, Li, and Ahmad (2008). Protein powder was mixed with deionized water (3% w/w), and the mixture pH was adjusted to 1.0-13.0 with 4 M NaOH or 4 M HCl.…”

Section: Protein Characterizationmentioning

confidence: 99%

A new way of valorizing biomaterials: The use of sunflower protein for α-tocopherol microencapsulation

Nesterenko

Alric

Violleau

et al. 2013

Food Research International

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“…Thus, part of the increased solubilities for the samples treated under the more drastic conditions can be related to the denaturated state of the proteins (Table 2), which might have contributed to changes in the number of hydrophobic residues, charge, electrostatic repulsion and ionic hydration, which are parameters affecting protein solubility [26]. In principle, it is usually understood that denatured protein has a lower solubility as compared to native protein; however, Zheng et al [27] also reported the higher solubility of fully denatured protein as compared to partly denatured and native spray-dried proteins, suggesting that protein solubility is influenced by several factors not only by the degree of exposed hydrophobic groups.…”

Section: Protein Solubilitymentioning

confidence: 99%

Functional Properties of Soy Protein Isolates Produced from Ultrasonicated Defatted Soy Flakes

Karki

Lamsal

Grewell

et al. 2009

J Americ Oil Chem Soc

111

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This study aimed to determine the effect of pretreating defatted soy flakes with ultrasound on soy protein isolate (SPI) yield and functionality. Defatted soy flakes dispersed into water (16%, w/w) were sonicated for 30, 60 and 120 s at ultrasonic amplitudes of 21 and 84 lm pp (peak to peak amplitude in lm), representing low and high power, respectively. The power densities were 0.30 and 2.56 W mL -1 , respectively. The SPI yield increased by 13 and 34%, after sonication for 120 s at low and high power, respectively. The sonication of defatted soy flakes for 120 s at the higher power level improved the SPI solubility by 34% at pH 7.0, while decreasing emulsification and foaming capacities by 12 and 26%, respectively, when compared to control SPI. Rheological behavior of the SPI was also modified with significant loss in consistency coefficient due to sonication. Some of these results could be explained by the loss of the protein native state with increased sonication time and power.

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Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties

Cited by 47 publications

References 34 publications

Functional Properties of Lupinus angustifolius Seed Protein Isolates

Functional Properties of Lupinus angustifolius Seed Protein Isolates

A new way of valorizing biomaterials: The use of sunflower protein for α-tocopherol microencapsulation

Functional Properties of Soy Protein Isolates Produced from Ultrasonicated Defatted Soy Flakes

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