2015
DOI: 10.1016/j.ifset.2015.09.010
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High pressure modification of egg components: Exploration of calorimetric, structural and functional characteristics

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Cited by 29 publications
(22 citation statements)
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“…() pressurized EW up to 400 MPa for 15 min and reported an increase in EW foam stability by HHP treatment at 400 MPa for 5 min. Similar findings have been reported by Singh and Ramaswamy () who found HHP treatment at 350 to 450 MPa for 5 min led to the most stable EW foam, compared to more severe conditions of 550 MPa for 5 to 15 min. Using differential scanning calorimetry (DSC), it has been determined that HHP‐induced denaturation of EW proteins started at 350 MPa for 5 min and progressively increased at 550 MPa for 10 to 15 min, where the formation of aggregates and separation of liquid in EW were visually noticed (Singh & Ramaswamy, ).…”
Section: Changes In Protein Functionality Due To Hhp Processingsupporting
confidence: 90%
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“…() pressurized EW up to 400 MPa for 15 min and reported an increase in EW foam stability by HHP treatment at 400 MPa for 5 min. Similar findings have been reported by Singh and Ramaswamy () who found HHP treatment at 350 to 450 MPa for 5 min led to the most stable EW foam, compared to more severe conditions of 550 MPa for 5 to 15 min. Using differential scanning calorimetry (DSC), it has been determined that HHP‐induced denaturation of EW proteins started at 350 MPa for 5 min and progressively increased at 550 MPa for 10 to 15 min, where the formation of aggregates and separation of liquid in EW were visually noticed (Singh & Ramaswamy, ).…”
Section: Changes In Protein Functionality Due To Hhp Processingsupporting
confidence: 90%
“…Using differential scanning calorimetry (DSC), it has been determined that HHP‐induced denaturation of EW proteins started at 350 MPa for 5 min and progressively increased at 550 MPa for 10 to 15 min, where the formation of aggregates and separation of liquid in EW were visually noticed (Singh & Ramaswamy, ). HHP‐induced protein aggregation, which resulted from the association of unfolded proteins via hydrophobic interactions, was accompanied by the loss of protein solubility, likely accounting for the diminished foam stability (Singh & Ramaswamy, ).…”
Section: Changes In Protein Functionality Due To Hhp Processingmentioning
confidence: 99%
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“…A major component of angel food cake meringue is egg white, so it suggests that longer mixing times of egg white can aid in meringue formation from pasteurized shell eggs. While evaluating these foaming properties of egg whites, it is important to keep in mind that during foam formation, the proteins undergo additional denaturation at the interface (Singh & Ramaswamy, , ; Singh et al., ). It has been known since the 1960s that pasteurization of liquid egg white product decreases the foaming ability, and increasing the mixing time can improve foaming (Kline et al., ; Singh, ), but very limited research is available about the effects of mixing speed and time on the foaming, and functionality of meringues and angel food cakes.…”
Section: Resultsmentioning
confidence: 99%
“…Measuring the rheological, thermal, and functional values of HHP‐treated whole liquid egg and egg yolk revealed that HHP produces a high viscosity in egg products, which is the result of denaturation and aggregation of egg proteins (Singh and others ). Pressure‐induced changes in the proteins are reflected in the foaming and functional characteristics of pressurized egg (Singh and Ramaswamy ).…”
Section: Structural and Functional Modifications Of Hhp‐treated Egg Amentioning
confidence: 99%