2018
DOI: 10.1002/jsfa.8813
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Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid

Abstract: Experimental results indicated over 90% reduction of the antigenicity at pH 9.5 and temperature of 100 °C. Significant changes of the linear epitopes exposure and location of the conformational epitopes were highlighted after performing heating molecular dynamics simulations of OVM from 25 °C to 100 °C. © 2017 Society of Chemical Industry.

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Cited by 15 publications
(11 citation statements)
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“…Moreover, some of these molecules (ovoinhibitor, ovomucoid, cystatin) possess many disulfide bonds that are likely to confer moderate resistance to denaturation by proteases and gastric juices. Some of these antinutritional factors may be partly denatured by heat [20,22,23,24] during the process of cooking, thus facilitating protein access to digestive proteases. Moreover, some vitamin-binding proteins highly concentrated in egg may also limit some vitamin access—avidin that binds vitamin B12 (biotin) exhibits the highest known affinity in nature between a ligand and a protein [60].…”
Section: Egg Nutrientsmentioning
confidence: 99%
See 1 more Smart Citation
“…Moreover, some of these molecules (ovoinhibitor, ovomucoid, cystatin) possess many disulfide bonds that are likely to confer moderate resistance to denaturation by proteases and gastric juices. Some of these antinutritional factors may be partly denatured by heat [20,22,23,24] during the process of cooking, thus facilitating protein access to digestive proteases. Moreover, some vitamin-binding proteins highly concentrated in egg may also limit some vitamin access—avidin that binds vitamin B12 (biotin) exhibits the highest known affinity in nature between a ligand and a protein [60].…”
Section: Egg Nutrientsmentioning
confidence: 99%
“…However, although the assimilation of egg protein is facilitated by heat-pretreatment and at a high level (91–94% for cooked egg-white proteins), it remains partly incomplete. It is noteworthy that major proteins, essentially egg-white proteins such as the proteinase inhibitor ovomucoid, and major egg-white ovalbumin resist thermal heating [23,24]. This observation is particularly interesting, knowing that egg-derived proteins and many hydrolytic peptides generated in vitro from limited digestion of egg-white proteins possess biological activities of interest for human health and may thus be used as nutraceuticals [16].…”
Section: Introductionmentioning
confidence: 99%
“…Nowadays, the effect of thermal treatment on food proteins is still concerned (Sang et al., ). Currently, the influence of external conditions, such as temperature, pressure, electric field, and solvation on the structure during processing has been the focus of MD studies to access changes of proteins during processing (Russo et al., ; Stănciuc, Banu, Bolea, Patraşcu, & Aprodu, ; Stănciuc, Crețu, Banu, & Aprodu, ; Vagadia, Vanga, Singh, & Raghavan, ). For instance, studies to evaluate external electric field and pressure on proteins can be cited (Singh, Orsat, & Raghavan, ; Wakai, Takemura, Morita, & Kitao, ).…”
Section: Simulation As An Aid For Food Researchmentioning
confidence: 99%
“…Thermal treatment is the common method to eliminate allergen of food proteins. By MD simulation, the secondary and tertiary structure of ovomucoid was found to be altered significantly by thermal treatment with the exposure of the linear epitopes (K159‐S174 and T179‐C186) as temperature increased from 25 to 100 °C (Stănciuc, Crețu, Banu, & Aprodu, ). Additionally, the conformation of the epitopes location was changed.…”
Section: Simulations To Evaluate the Dynamic Behaviors Of Componenmentioning
confidence: 99%
“…Egg protein is also the lowest-cost protein, compared to many other sources, making it affordable for low socioeconomic groups [ 13 ]. However, it is important to remember that egg whites contain protease inhibitors that might decrease amino acid digestibility [ 14 ]. However, these can be easily destroyed by heat, highlighting the importance of cooked eggs being a better source of bioavailable protein.…”
Section: Egg Protein and Prevention Of Malnutrition In Childrenmentioning
confidence: 99%