Milk Proteins 2020
DOI: 10.1016/b978-0-12-815251-5.00009-8
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The whey proteins in milk: Thermal denaturation, physical interactions, and effects on the functional properties of milk

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Cited by 23 publications
(14 citation statements)
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“…More importantly, for reconstituted skim milk the presence of soluble aggregates involving κ‐CN (Figure 1a) could also interfere with rennet's access to the active site of entrapped κ‐CN molecules. Aggregates in reconstituted skim milk are heat‐induced during skim milk powder processing via thiol (S‐H)‐disulfide (S‐S) interactions and appear as intermediate bands on SDS‐PAGE (Anema 2020). In the present study, such bands could be clearly seen in whey samples (Figure 3a1 and b1) and appeared to be covalently bonded since all other forms of interactions are supposedly dissociated under nonreducing SDS‐PAGE conditions.…”
Section: Discussionmentioning
confidence: 99%
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“…More importantly, for reconstituted skim milk the presence of soluble aggregates involving κ‐CN (Figure 1a) could also interfere with rennet's access to the active site of entrapped κ‐CN molecules. Aggregates in reconstituted skim milk are heat‐induced during skim milk powder processing via thiol (S‐H)‐disulfide (S‐S) interactions and appear as intermediate bands on SDS‐PAGE (Anema 2020). In the present study, such bands could be clearly seen in whey samples (Figure 3a1 and b1) and appeared to be covalently bonded since all other forms of interactions are supposedly dissociated under nonreducing SDS‐PAGE conditions.…”
Section: Discussionmentioning
confidence: 99%
“…2018), showing that the presence of some intact κ‐CN molecules is inevitable unless conditions applied allow a complete hydrolysis. Furthermore, unlike other CNs, κ‐CN is not sensitive to Ca ions (Huppertz 2013) and located preferentially on the micellar surface (Anema 2020); thus, unhydrolysed soluble molecules of κ‐CN would end up in whey.…”
Section: Discussionmentioning
confidence: 99%
“…Both β-Lg and α-La in the unfolded status preferentially bind to the surface of casein micelles by reacting with κ-casein [ 26 ]. When severe heat treatments are applied, other inter and intramolecular interactions occur, leading to the formation of insoluble protein aggregates, also entrapping fat globules [ 32 , 33 ]. Aside from heating conditions, the protein concentration and pH of the medium also regulate the degree of whey protein binding to casein instead of self-aggregation, and this dramatically impacts milk protein functionality and behavior [ 34 ].…”
Section: Approaches and Methodologies For Modifying The Properties Of...mentioning
confidence: 99%
“…Chemical, physical, and enzymatical treatments can be applied to induce protein crosslinking since proteins have several reactive groups (e.g., side chains of glutamine, lysine, tyrosine, cysteine) [ 39 , 40 ]. Disulfide bonds are naturally occurring crosslinks in whey proteins, which may rearrange when subject to thermal treatments, enzymatic catalysis, or oxidative conditions, with a significant impact on protein functionality [ 32 ]. The creation of inter- and intra-molecular disulfide bonds leads to the formation of a stronger, more rigid protein network with enhanced resistance to proteolysis [ 41 ].…”
Section: Approaches and Methodologies For Modifying The Properties Of...mentioning
confidence: 99%
“…Heat-treated milk is next initially cooled down to 75 C to allow effective homogenization by utilizing two-stage homogenizer (168 bar). Milk possesses numerous heat unstable components such as enzymes or whey protein, which under high temperature can denature and react with inorganic elements and clump together (Anema, 2020;Anema & McKenna, 1996).…”
Section: Milk Blend Processingmentioning
confidence: 99%