Yingjie Yang , Yiwen Ding , Nan Xiao , Shanguang Guo , Minmin Ai
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引用次数: 0
Abstract
The regulation of protein recombination is inherently associated to its functional properties. This study explored the recombination behavior and structural characteristics of egg white protein (EWP), utilizing ultrasound and salt ion-driven modifications of preheated EWP. The research elucidated the mechanism through which the hydration properties of EWP regulate foaming at the gas–liquid interface. Results demonstrated a significant positive correlation between the turbidity and particle size of EWP. An increased level of aggregation of EWP corresponded to larger particle sizes and heightened turbidity. Optimal stability of EWP was observed at 66 °C, under low NaCl concentrations (0–50 mM) and an ultrasonic power of 360 W. Moreover, the mechanical forces generated by high ultrasonic power altered the structure of the protein's rigid regions, making its internal structure more readily extended and exposed. Meanwhile, high salt ion concentration competed with the EWP surface hydration layer, weakening EWP surface hydration layer, forming a “hydrated Na+-water” double-shell structure that enhanced hydration force, exposed amino acid residues, and increased molecular flexibility and surface hydrophobicity. High-temperature preheating made the EWP structure flexible, creating a tough foam film, which, along with the other factors, improved foam stability. Rheological results indicated that ultrasonic enhancement decreased gel stiffness and covalent bond strength, while salt concentration (below 300 mM) had the opposite effect. Electrophoretic results revealed that ultrasonic cavitation and salt ions modified the EWP surface hydration layer. High-temperature treatment (66 °C) further promoted ovalbumin degeneration and disintegration, reducing protein band gray scale.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.