2022
DOI: 10.1134/s1068162022020170
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Current Data about Milk Caseins

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Cited by 9 publications
(2 citation statements)
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“…The higher the proportion of casein in the total protein, the more potentially allergenic. This is because casein allergic reactions may trigger a Th2 response, disrupting the Th1/Th2 immune balance and predisposing the infant to sensitization by other milk proteins such as β-lactoglobulin and α-lactoglobulin [ 22 ]. These proteins have a complex tertiary structure and similarities in peptide chain conformation, recognizing similar T and B cell epitopes [ 23 ].…”
Section: Allergy Mechanism Of Various Food Allergensmentioning
confidence: 99%
“…The higher the proportion of casein in the total protein, the more potentially allergenic. This is because casein allergic reactions may trigger a Th2 response, disrupting the Th1/Th2 immune balance and predisposing the infant to sensitization by other milk proteins such as β-lactoglobulin and α-lactoglobulin [ 22 ]. These proteins have a complex tertiary structure and similarities in peptide chain conformation, recognizing similar T and B cell epitopes [ 23 ].…”
Section: Allergy Mechanism Of Various Food Allergensmentioning
confidence: 99%
“…There are four main subunits of casein: alpha s1-casein, alpha s2-casein, beta-casein, and kappa-casein, which make up 38%, 10%, 36%, and 13% of casein composition, respectively [215]. The primary, secondary, and tertiary structures of casein are less ordered and more flexible than those of typical globular proteins [216,217]. The structure of casein contains polar and hydrophobic domains with a degree of flexibility, giving limited proteolysis and enhanced functionality [218].…”
Section: Animal Proteins-caseinmentioning
confidence: 99%