2012
DOI: 10.1016/j.jfoodeng.2011.08.018
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Comparative study of high intensity ultrasound effects on food proteins functionality

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Cited by 589 publications
(361 citation statements)
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“…The declining trend in the surface hydrophobicity might be attributed to the formation of protein aggregates and denaturation at high ultrasonication, which may protect hydrophobic sites from exposure in the proteins and also lead to increasing the extent of bonding; thus, the surface hydrophobicity decreased [26,53]. Ultrasonic pretreatment makes partial denaturation of proteins, and partial denaturation of proteins will expose some of the hydrophobic peptides buried in the natural form to effectively alter the surface properties of the protein and cause an increase in hydrophobicity and this change is likely to be the main reason for the aggregation of proteins during refolding [27,54,55]. The simultaneous exposure of the hydrophobic peptide is beneficial for the enhancement of ACE inhibitory activity of hydrolysates.…”
Section: Effect Of Ultrasound Power On Surface Hydrophobicity (Ho) Ofmentioning
confidence: 99%
“…The declining trend in the surface hydrophobicity might be attributed to the formation of protein aggregates and denaturation at high ultrasonication, which may protect hydrophobic sites from exposure in the proteins and also lead to increasing the extent of bonding; thus, the surface hydrophobicity decreased [26,53]. Ultrasonic pretreatment makes partial denaturation of proteins, and partial denaturation of proteins will expose some of the hydrophobic peptides buried in the natural form to effectively alter the surface properties of the protein and cause an increase in hydrophobicity and this change is likely to be the main reason for the aggregation of proteins during refolding [27,54,55]. The simultaneous exposure of the hydrophobic peptide is beneficial for the enhancement of ACE inhibitory activity of hydrolysates.…”
Section: Effect Of Ultrasound Power On Surface Hydrophobicity (Ho) Ofmentioning
confidence: 99%
“…Cysteine, and methionine are the amino acids thought to be most susceptible to oxidative changes due to the susceptibility of their sulfur groups to radical attack. Changes induced by high intensity ultrasound depend on the nature of the protein and its degree of denaturation and aggregation (Arzeni et al, 2012). High intensity ultrasound induces modifications on food protein functionalities such as gelation, viscosity and solubility and those changes are believed to be closely related to molecular modifications, mainly hydrophobicity increase and particle size variation.…”
Section: Power Ultrasound Negative Effects In Meat Processingmentioning
confidence: 99%
“…Recent studies using ultrasound in baking process included Harris (2011), who produced gluten-free products with improved texture, and Tan et al (2011), who reported improved cake aeration with lower hardness and density. Other works that have applied ultrasound on proteins, which have measured changes in protein solubility, conductivity, foam ability , size of fat globule, protein denaturation (Villamiel and de Jong 2000), consistency index, and gelation properties (Arzeni et al 2012), suggested that proteins induced by ultrasound have potential in structural and functional improvements (Gülseren et al 2007).…”
Section: Introductionmentioning
confidence: 99%