2021
DOI: 10.1016/j.idairyj.2021.105175
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Heat-induced denaturation and bioactivity changes of whey proteins

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Cited by 41 publications
(24 citation statements)
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“…According to a previous study [ 16 ], pasteurization of whey, ultrafiltration, evaporation, and spray-drying decrease the percentage of native on the total protein content in these types of WPCs. Heat induced modifications such as oxidation and glycation of proteins, formation of lysine-alanine crosslinks, pH, the exposure of cleavage sites due to protein unfolding, and the structure of aggregates affect the hydrolysis and digestibility of whey proteins [ 40 ]. The modified lysine residues of β-LG lactosylated under mild heat treatments has been found resistant to trypsin [ 41 ].…”
Section: Resultsmentioning
confidence: 99%
“…According to a previous study [ 16 ], pasteurization of whey, ultrafiltration, evaporation, and spray-drying decrease the percentage of native on the total protein content in these types of WPCs. Heat induced modifications such as oxidation and glycation of proteins, formation of lysine-alanine crosslinks, pH, the exposure of cleavage sites due to protein unfolding, and the structure of aggregates affect the hydrolysis and digestibility of whey proteins [ 40 ]. The modified lysine residues of β-LG lactosylated under mild heat treatments has been found resistant to trypsin [ 41 ].…”
Section: Resultsmentioning
confidence: 99%
“…Thomsen et al (2005) observed lipid oxidation, the occurrence of the Maillard reaction, and the generation of oxygen radicals and a variety of oxidation products during the drying of cow milk. Moreover, heating could cause rapid and violent molecular vibrations that disrupt hydrogen bonds and nonpolar hydrophobic interactions, promoting lipid oxidative and browning reactions (Zhang et al, 2021). Oxidative stress leads to increased nucleotide metabolism, amino acid transport, and protein turnover in bifidobacteria, whereas carbohydrate metabolism slows down (Zuo et al, 2018).…”
Section: Discussionmentioning
confidence: 99%
“…The hydrolysis products obtained during the enzymatic digestion of whey proteins have various functional properties, including thermal stability and antioxidant properties (Zhang et al, 2021). Furthermore, the hydrolysis of whey proteins could lead to the breaking of peptide bonds, generating peptides with different molecular weights, hydrophobicities, amino acid compositions, peptide sequences, and antioxidant activities (Wong et al, 2020).…”
Section: Introductionmentioning
confidence: 99%
“…Salar et al [ 37 ] recommended that gentle pasteurization of BC (57 °C for 30 min) together with drying methods (freeze or spray drying) could act as hurdle technology which results in the reduction in microbial load with minimal impact on bioactive constituents (lactoferrin and IgG) and antioxidant activities of BC. Bovine colostrum immunoglobulin (IgG) was shown to be 15% denatured after long-time pasteurization (63 °C for 30 min) and 34% denatured after high-temperature, short-time pasteurization (72 °C for 15 s) by Chatterton et al [ 39 ], while the IgG was completely inactivated by ultra-heat treatment [ 40 ]. Another study, conducted by Elizondo-Salazar et al [ 41 ], indicates that the thermal treatment (60 °C or >60 °C for <1 h) completely denatured immunoglobulin IgG 1 but had less effect on IgG 2 concentration.…”
Section: Impact Of Processing Techniques and Conditions On Colostrum ...mentioning
confidence: 99%