Whey Proteins 2019
DOI: 10.1016/b978-0-12-812124-5.00006-0
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Thermal Denaturation, Aggregation, and Methods of Prevention

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Cited by 27 publications
(28 citation statements)
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“…Taking whey protein as an example, the formation of hydrogels by thermal gelation consists of three steps: (i) unfolding of polypeptide chains in proteins, (ii) assembly of primary aggregates, and then (iii) random cross‐linking of the aggregates (Wagner et al., 2020; Wijayanti et al., 2014, 2018). After thermal denaturation, whey proteins will have a larger hydrophobic cavity with more binding sites and higher binding affinity to copigment anthocyanins through hydrophobic interactions and hydrogen bonding.…”
Section: Synergistic Effects Of Copigmentation and Encapsulationmentioning
confidence: 99%
“…Taking whey protein as an example, the formation of hydrogels by thermal gelation consists of three steps: (i) unfolding of polypeptide chains in proteins, (ii) assembly of primary aggregates, and then (iii) random cross‐linking of the aggregates (Wagner et al., 2020; Wijayanti et al., 2014, 2018). After thermal denaturation, whey proteins will have a larger hydrophobic cavity with more binding sites and higher binding affinity to copigment anthocyanins through hydrophobic interactions and hydrogen bonding.…”
Section: Synergistic Effects Of Copigmentation and Encapsulationmentioning
confidence: 99%
“…Most of the major whey proteins are highly ordered globular proteins, and thus they are very heat sensitive as they are liable to structural damage at the time of processing treatments in the dairy industries (e.g., high-pressure homogenization, and heat treatments). Generally, whey proteins tend to unfold from their original structure, revealing amino acids such as cysteine, which contains a free sulfhydryl (-SH) group when they are exposed to temperatures greater than 65 °C [ 39 ]. Moreover, the exposed free sulfhydryl group is now readily available and highly reactive, allowing other denatured whey proteins and proteins that contain the exposed sulfhydryl groups (e.g., κ-casein) to interact and aggregate to form a new (S-S) disulfide bond [ 35 ].…”
Section: Effects Of Uht Processing On Milk Proteinsmentioning
confidence: 99%
“…The effects of denaturation and interaction with other proteins are minor as compared to β-lactoglobulin and α-lactalbumin, whereas, in the milk, the denaturation of whey proteins is dominated by the denaturation of β-lactoglobulin, which is about 50% of the whey proteins. However, α-lactalbumin is also important [ 39 ].…”
Section: Effects Of Uht Processing On Milk Proteinsmentioning
confidence: 99%
“…Aroma binding ability of proteins is highly dependent on the conformational state of the protein, and more particularly on the sites available to bind aroma compounds. It is well known that β-lactoglobulin is readily denatured by heat treatment (Wijayanti, Brodkorb, Hogan, & Murphy, 2019), and the resulting change of conformation is likely to influence its retention abilities. Few studies have been performed on the aroma retention abilities of Table 2 Mean partition coefficients (K G/S × 10 2 ) of aroma compounds in water and in protein solutions (WPI, MFA, PFA) flavored with the strawberry aroma.…”
Section: Aroma Retention In Mfa and Pfa Versus Wpi Aqueous Protein Somentioning
confidence: 99%