2023
DOI: 10.1016/j.foodhyd.2023.109069
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Effect of ultrasound and alkali-heat treatment on the thermal gel properties and catechin encapsulation capacity of ovalbumin

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Cited by 18 publications
(1 citation statement)
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“…The effects of cavitation, dynamic agitation, shear, and turbulence induced by ultrasound can alter the molecular structure of proteins, affecting their characteristics and functionalities. The application of ultrasound can disrupt protein aggregates, enhancing their solubility in water, increasing stability, and altering the binding mode, thereby facilitating the interaction and encapsulation of hydrophobic compounds by proteins. The intrinsically disordered conformation of casein prevents its heat-mediated degradation, a process often employed in the food industry. Like carvacrol, micellar casein is also recognized as GRAS, being naturally biocompatible and biodegradable …”
Section: Introductionmentioning
confidence: 99%
“…The effects of cavitation, dynamic agitation, shear, and turbulence induced by ultrasound can alter the molecular structure of proteins, affecting their characteristics and functionalities. The application of ultrasound can disrupt protein aggregates, enhancing their solubility in water, increasing stability, and altering the binding mode, thereby facilitating the interaction and encapsulation of hydrophobic compounds by proteins. The intrinsically disordered conformation of casein prevents its heat-mediated degradation, a process often employed in the food industry. Like carvacrol, micellar casein is also recognized as GRAS, being naturally biocompatible and biodegradable …”
Section: Introductionmentioning
confidence: 99%