Soy Protein‐Based Blends, Composites and Nanocomposites

Visakh, P. M.; Nazarenko, Olga B.

doi:10.1002/9781119419075

Cited by 6 publications

(3 citation statements)

References 55 publications

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“…Under the extreme acidic condition (pH 2) after the USSH treatment, the soy proteins became more swelled and opened, as the average hydrodynamic diameter further increased to 468.6 nm. In comparison, at the extreme basic pH (12), the mean hydrodynamic diameter decreased to 199.1 nm, which agreed well with a protein hydrolysis phenomenon reported by others . To better characterize the size of protein particles, the polydispersity index (PDI) values of the SPI dispersions were investigated.…”

Section: Results and Discussionmentioning

confidence: 99%

“…Biodegradable and bio-based polymers have been explored as replacements for the synthetic polymers, and protein is one of the most competitive candidates among all of the sources. − Soy protein, as one of the most abundant plant proteins in nature, is produced in vast quantities in the United States each year . However, pure soy proteins could not be ideally utilized in industry because of their nonprocessable globular structures. − As a result, studies focusing on exploring the method of modifying the conformational structures of soy proteins are necessary.…”

Section: Introductionmentioning

confidence: 99%

“…One of the interactions is the hydrogen bond (H-bond), holding the structure of β-conglycinin (7S, 150–200 kDa) and other parts of SPI. − It was reported that the hydrogen bonds formed between water and soy proteins are not sufficient for the dissolution and denaturation of SPI. While chaotic chemical agents such as urea and glycerol could actively interfere with intermolecular hydrogen bonds in soy proteins, the results revealed that an 8 M urea solution was an effective solvent for opening the globular soy protein structure into random coils. , However, the vast amount of urea in the system remains in produced solid materials as impurities, posing difficulties in applications. Structurally similar to urea, glycerol (Gly) as an amphiphilic agent with a short and flexible chain interacts with protein molecules with extensive H-bonds without causing harm to humans or the environment.…”

Section: Introductionmentioning

confidence: 99%

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Improved Processability of Soy Proteins Due to Conformational Controls under a Combination of Chemical and Mechanical Treatments

Zou

Nguyen

Biers

et al. 2021

ACS Agric. Sci. Technol.

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Conformations of soy proteins in soy protein isolate (SPI) aqueous dispersions determine the processability of the SPI and are affected significantly by pH conditions and the addition of a plasticizer, when mechanical forces are present. In this work, the effect of chemical forces facilitating the physical treatment in modifying the conformational structures of soy proteins was investigated. SPI in a H2O system under extreme pH conditions and a glycerol/H2O system was subjected to a combination of ultrasound and shear (USSH) treatments to increase the processability of soy proteins by conformational denaturation. In the H2O system, the combination of the USSH treatment and different pH conditions provides varied properties of denatured SPI solutions and fabricated SPI–cellophane composite films. In the glycerol/H2O system, with an increased and stabilized viscosity, a higher content of sulfhydryl groups, swelled particle sizes, and unfolded protein structures, glycerol proved to be an efficient structural stabilizing agent assisting the deformation of soy proteins under the USSH treatment. The combinations of the USSH treatment and extreme pH conditions or the glycerol/H2O system proved to be efficient processing methods for increasing the processability of soy proteins as a raw material in products.

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Section: Results and Discussionmentioning

confidence: 99%