2021
DOI: 10.1016/j.cocis.2021.101507
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Combining plant and dairy proteins in food colloid design

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Cited by 24 publications
(7 citation statements)
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“…In contrast, the total free SH content decreased significantly after cross-linking in all samples, indicating disulphide bond formation between pea and whey proteins due to TGase promoting thiol-disulphide exchange reactions between heteroproteins (Kristensen et al, 2022; H. T. . Several studies have demonstrated that new disulphide linkage between globulins in legume proteins and β-lactoglobulin in whey protein is induced by TGase (S. N. Hinderink et al, 2021). The surface free SH content shows negligible difference according to cross-linking (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…In contrast, the total free SH content decreased significantly after cross-linking in all samples, indicating disulphide bond formation between pea and whey proteins due to TGase promoting thiol-disulphide exchange reactions between heteroproteins (Kristensen et al, 2022; H. T. . Several studies have demonstrated that new disulphide linkage between globulins in legume proteins and β-lactoglobulin in whey protein is induced by TGase (S. N. Hinderink et al, 2021). The surface free SH content shows negligible difference according to cross-linking (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Heat-induced gelation is a widely used method in the food industry for inducing gel formation, particularly with globular proteins found in dairy and plant proteins [139,140]. Heat-induced gelation involves heating the emulsion and subsequently cooling it at low temperatures to produce emulsion gels [141].…”
Section: Heat-set Gelsmentioning
confidence: 99%
“…In this regard, proteins are widely utilized in different food industries, including dairy, baking, confectionary, and beverage, in the form of micro‐ or nanoparticles as surfactants, stabilizers, and thickening agents (Kim et al, 2020; Ribeiro et al, 2021). The interfacial properties of proteins highly depend on their molecular weight, surface hydrophobicity/hydrophilicity ratio, structure, and amino acid composition, as well as the environmental conditions, such as pH, temperature, concentration, and ionic strength (Gentile, 2020; Hinderink et al, 2021). Previously, the surface properties and mechanisms of animal‐based proteins, especially dairy and egg proteins, have been well studied and characterized (Ha et al, 2019; Liu, Oey, et al, 2019).…”
Section: Introductionmentioning
confidence: 99%