Preparation and characteristics of coprecipitate proteins from oilseeds and legumes seeds

Youssef, Abou-Bakr M.; Abu-Foul, N.S.; Moharram, Y. G.

doi:10.1002/food.19950390512

Cited by 10 publications

(3 citation statements)

References 17 publications

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“…The addition of polysaccharides can form biopolymers, which are surface active materials, essential in stabilizing food formulations as foams, emulsions and dispersions against heat or pressure (Benichou, Aserin, & Garti, 2002). The coprecipitation of proteins from different vegetable sources blends or with whey proteins show higher nutritional values and better functional properties than those of their individual protein isolates Youssef, Abu-Foul, & Moharram, 1995). Application of genetic engineering to oilseed proteins can affect functional properties in different degree depending on the protein (Heywood, Myers, Bailey, & Johnson, 2002;Kim, Kamiya, Sato, Utsumi, & Kito, 1990;Tandang, Adachi, Inui, Maruyama, & Utsumi, 2004).…”

Section: Modification Of Oilseed Proteins For Improving Their Functiomentioning

confidence: 99%

Functionality of oilseed protein products: A review

Moure

Sineiro

Domı́nguez

et al. 2006

Food Research International

466

319

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Section: Modification Of Oilseed Proteins For Improving Their Functiomentioning

confidence: 99%

Functionality of oilseed protein products: A review

Moure

Sineiro

Domı́nguez

et al. 2006

Food Research International

466

319

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“…Sheep milk protein co-precipitates were found to have a high foaming capacity and good stability at all pH values [20]. Additionally, the nutritional properties of protein co-precipitates can be enhanced by altering their amino acid compositions [21]. A recent study showed that protein co-precipitates, as a food ingredient, can provide angiotensin-converting enzyme (ACE) inhibitory activity and antioxidant activities for high-selectivity applications [22].…”

Section: Introductionmentioning

confidence: 99%

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

et al. 2019

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The secondary structure of a protein has been identified to be a crucial indicator that governs its water solubility. Tilapia protein isolate (TPI), soybean protein isolate (SPI), and tilapia-soybean protein co-precipitates (TSPC3:1, TSPC2:1, TSPC1:1, TSPC1:2, and TSPC1:3) were prepared by mixing tilapia meat and soybean meal at different mass ratios. The results demonstrated that the water solubility of TSPCs was significantly greater than that of TPI (p <0.05). The changes in ultraviolet–visible and near-ultraviolet circular dichroism spectra indicated that the local structure of TSPCs was different from that of TPI and SPI. Fourier transform infrared Spectroscopy revealed the co-existence of TPI and SPI structures in TSPCs. The secondary structures of TSPCs were predominantly α-helix and β-sheet. TSPC1:1 was unique compared to the other TSPCs. In addition, there was a good correlation between the water solubility and secondary structure of TSPCs, in which the correlation coefficients of α-helix and β-sheet were −0.964 (p <0.01) and 0.743, respectively. TSPCs displayed lower α-helix contents and higher β-sheet contents compared to TPI, which resulted in a significant increase in their water solubility. Our findings could provide insight into the structure–function relationship of food proteins, thus creating more opportunities to develop innovative applications for mixed proteins.

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“…Driven by pH, proteins from different sources are simultaneously dissolved and precipitated to promote interaction between heteroproteins; generate additional disulfide bonds; change the subunit composition [ 10 ]; and alter the surface charge, solubility, and surface hydrophobicity of the proteins, thus effectively improving their functional properties [ 11 ]. Studies have found that legume–rapeseed Co has better nutritional and functional properties than single protein [ 12 ], and soy–whey protein Co has high water-holding and gel formation capacity [ 13 ]. Previously, we investigated the functional properties of soy–tilapia Co and found that the solubility and emulsifying properties of the Co were better than those of the single protein [ 14 , 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation

Zhou

Zhang

Cao

et al. 2021

Foods

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Currently, the application of protein mixture derived from plants and animals is of great interest to the food industry. However, the synergistic effects of isolated protein blends (BL) are not well established. Herein, the development of a more effective method (co-precipitation) for the production of protein mixtures from pea and grass carp is reported. Pea protein isolate (PPI), grass carp protein isolate (CPI), and pea–carp protein co-precipitates (Co) were prepared via isoelectric solubilization/precipitation using peas and grass carp as raw materials. Meanwhile, the BL was obtained by blending PPI with CPI. In addition, the subunit composition and functional properties of Co and BL were investigated. The results show that the ratios of vicilin to legumin α + β and the soluble aggregates of Co were 2.82- and 1.69-fold higher than that of BL. The surface hydrophobicity of Co was less than that of BL, PPI, and CPI (p < 0.05). The solubility of Co was greater than that of BL, PPI, and CPI (p < 0.05), and the foaming activity was higher than that of BL and CPI (p < 0.05) but slightly lower than that of PPI. In addition, based on the emulsifying activity index, particle size, microstructure, and viscosity, Co had better emulsifying properties than BL, PPI, and CPI. The study not only confirmed that co-precipitation was more effective than blending for the preparation of mixed protein using PPI and CPI but also provided a standard of reference for obtaining a mixture of plant and animal proteins.

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Preparation and characteristics of coprecipitate proteins from oilseeds and legumes seeds

Cited by 10 publications

References 17 publications

Functionality of oilseed protein products: A review

Functionality of oilseed protein products: A review

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

A Comparative Functional Analysis of Pea Protein and Grass Carp Protein Mixture via Blending and Co-Precipitation

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