RESUMO
This study aims to develop ultrasound-assisted acid-induced egg white protein (EWP)-soy protein isolate (SPI) composite gels and to investigate the mechanistic relationship between the co-aggregation behavior of composite proteins and gel properties through aggregation kinetics monitored continuously by turbidity. The results showed that the inclusion of EWP caused the attenuation of gel properties and maximum aggregation (Amax) because EWP could aggregate with SPI at a higher rate (Kapp), which impeded the interaction between SPI and the formation of a continuous gelling network. In the EWP-dominated system, SPI with higher molecular weights also increased the fractal dimension of gels. Ultrasound improved properties of composite gels, especially the SPI-dominated system. After ultrasound treatment, the small, uniform size of co-aggregates and the decrease in potential led to an increase in the aggregation rate and formation of dense particles, consistent with an increase in gelation rate and texture properties. Excessively fast aggregation generated coarse chains and more pores. Still, the exposure of free sulfhydryl groups assisted the gel structure units to form a compact network through disulfide bonding. On the whole, the study could provide theoretical support for a deeper understanding on the interaction mechanism and gelation of composite proteins.
Assuntos
Géis , Proteínas de Soja , Géis/química , Cinética , Proteínas de Soja/química , Glycine max/química , Ondas Ultrassônicas , Clara de Ovo/química , Agregados Proteicos , Proteínas do Ovo/químicaRESUMO
Sugars played an important role in the processing of products such as cakes, however, their high-calorie character often posed a health risk to consumers. Therefore, this paper aimed to better investigate the effect of sugar substitutes on the improvement of egg white foaming properties and angle cake digestibility characteristics. It was demonstrated that the addition of erythritol improved the surface properties of egg whites, thus enhancing their foaming properties. Particularly, when the erythritol substitution was 50 %, the sugar-egg white complex structure unfolded and had the best foaming capacity. On this basis, the baking performance of angel cakes with sucrose replaced by erythritol was analyzed. When the erythritol substitution was lower than 50 %, the specific volume and the baking loss rate of the cakes were basically unchanged, and the texture and sensory taste of the cakes were all excellent. Finally, the gastrointestinal digestive kinetic analysis suggested that erythritol substitution for sucrose was beneficial for reducing blood glucose levels in vivo. Furthermore, for the MgCl2-based samples, both the degree of protein destruction after digestion was weakened and the glucose-lowering effect was better exerted. Overall, this study provided a new theoretical basis for the low-calorie sugar-substituted health food products development in the future.
Assuntos
Eritritol , Sacarose , Cinética , Edulcorantes/análise , Açúcares , DigestãoRESUMO
This study aims to investigate the mechanism of magnesium ions regulated ovalbumin-lysozyme (OVA-LYS) heteroprotein aggregation behavior via aggregation kinetics model, exploring the relationship between differential aggregation behavior and protein molecular structure, intermolecular interactions and thermal stability. Results showed that the aggregation rate (kapp) and maximum absorbance (Amax) of the OVA-LYS heteroprotein complex were located between OVA and LYS. Meanwhile, the thermal denaturation temperature (Td) and denaturation enthalpy (ΔH) were between the values of OVA and LYS as well. Compared with OVA, the thermal stability of the OVA-LYS heteroprotein complex increased owing to the electrostatic interactions between OVA and LYS, resulting in slower aggregation rate and lower aggregation degree. Molecular dynamics simulations revealed the molecular conformational changes during OVA-LYS binary protein binding and the stability of the complex conformation. Moreover, MgCl2 weakened the OVA-LYS interactions through Debye shielding while increasing thermal stability, allowing the two proteins to aggregate into amorphous precipitates rather than spherical coacervates. Overall, this study provides information to further understand the regulation mechanism of proteins differential aggregation behavior by ions.
Assuntos
Magnésio , Muramidase , Ovalbumina/química , Muramidase/química , Termodinâmica , ÍonsRESUMO
This study aimed to form a novel emulsion gel (EG) through structured oil phase of natural component beeswax (BW), together with ovalbumin (OVA), and to investigate the mechanism of its formation and stabilization in terms of microstructure and processing properties. Confocal laser scanning microscopy (CLSM) demonstrated that the EG formed a continuous double network structure since the superior crystallinity of the oil phase was given by BW. Fourier transform infrared spectroscopy (FT-IR) illustrated that the acylation of the phenolic hydroxyl group in BW with an amide bond in OVA, increased the hydrogen bonding of EG. Furthermore, the immobilization of the oil phase results in better thermal and freeze-thaw stability of EG. Finally, EG was used as a curcumin delivery system, and the presence of BW significantly improved its adaptability to multiple environmental factors. In summary, our study would provide valuable ideas for developing the design of finely structured functional food.