Physico-chemical, functional, and structural properties of un-defatted, cold and hot defatted yellow lupin protein isolates

Effects of power ultrasound on oxidation and structure of beef proteins during curing processing

Effect of phenolic compound removal on rheological, thermal and physico-chemical properties of soybean and flaxseed proteins

Salted duck egg white (SDEW) is a major by-product during salted egg yolk manufacturing. Due to the high salt concentration, SDEW has not been efficiently utilized. Moreover, functional properties of SDEW are altered by salt during pickling. To improve the functional properties, the effect of κ-carrageenan (κ-CAR) addition on the protein structure and gel properties of SDEW was investigated in this study. The surface hydrophobicity and free sulfhydryl content of SDEW protein increased, while total sulfhydryl content decreased significantly with the addition of κ-CAR (0.02-0.10%). Fourier-transform infrared spectroscopy analysis revealed that the relative content of α-helix and β-turn decreased, β-sheet and random coil increased, indicating the variation tendency of protein structure from order to disorder. As κ-CAR addition increased, the texture profiles including hardness, gumminess, chewiness, springiness, cohesiveness and resilience of SDEW gel were all improved. Water holding capacity increased significantly by 32.33% in the presence of 0.10% κ-CAR addition. The scanning electron microscopy indicated that the microstructure of SDEW/κ-CAR mixed gel was more smooth and compact. The results suggested that adding κ-CAR can be an effective method to improve gel quality of SDEW. This study is expected to provide theoretical basis for modification of SDEW protein, as well as preparation of food ingredients with better gel properties from SDEW. © 2020 Society of Chemical Industry.

This study investigated the effect of industrial microwave (MW) processing, and sous vide (SV) on goat and lamb biceps femoris, where samples were cooked to the same tenderness. The cooked meat quality and ultrastructure were analyzed along with determining the protein surface hydrophobicity, particle size distribution, secondary structure, and protein digestibility. MW-processing resulted in higher cooking loss and more ultrastructural damage than SV and also induced higher myofibrillar protein surface hydrophobicity. Both processes caused a significant increase (p < 0.05) in the β-sheet and an increase in the random coils with a reduction (p < 0.05) in α-helix and β-turns. Both processes led to different protein hydrolysis patterns (observed through SDS-PAGE), but overall free amino N release after digestion was not significantly different among them. The results suggest that MW and SV modify meat protein structure differently, but with the same meat tenderness level, these processes can lead to similar overall protein digestibility.

Attenuation of ionic interactions profoundly lowers the kinetic thermal stability of Pyrococcus furiosus triosephosphate isomerase

Damage of proteins at the air/water interface: Surface tension characterizes globulin interface stability.

Impact of germination on structural, functional properties and in vitro protein digestibility of sesame (Sesamum indicum L.) protein

Heat induced denaturation, aggregation and gelation of almond proteins in skim and full fat almond milk

Application of PRODAN fluorescent probe to measure surface hydrophobicity of proteins interacting with κ-carrageenan

Unlocking the role of small heat shock proteins and apoptosis in postmortem proteolysis and meat quality characteristics of skeletal muscles under different conditions

Effect of different acidic or alkaline environments on structural characteristics, functional and physicochemical properties of lentinus edodes protein

With increasing consumer demand for healthy and sustainable food, plant proteins have been used widely in meat substitutes, dairy alternatives, and functional foods. However, in comparison with animal proteins, plant proteins often exhibit weaker functional properties, such as solubility, emulsifying, and gelation, which limit their application in food processing. The aim of this study was to investigate the effects of high-intensity ultrasound treatments (HIUTs) on the physicochemical properties, structural characteristics, emulsifying properties, and antioxidant capacity of shiitake mushroom protein isolate (SMPI). This study investigates how HIUTs affect SMPI. It also provides insights into potential applications within the food industry. When treated with a 300 W intensity ultrasound, SMPI exhibited higher solubility, water-holding capacity (WHC), oil-holding capacity (OHC), and antioxidant activity in comparison with the control (0 W). These results indicate that HIUT can enhance the functional properties of SMPI significantly. The molecular structure of SMPI after ultrasound treatment also underwent significant changes, suggesting that the treatment affects not only the physical properties but also the spatial conformation of SMPI. The concentration of free sulfhydryl (-FSH) group concentrations increased from 3.615 ± 0.080 μmol g-1to 13.020 ± 0.061 μmol g-1, and the emulsifying ability index (EAI) significant increased, indicating that a significant change produced in the tertiary structure of SMPI. The findings suggest that ultrasonic treatment can alter the physicochemical and functional attributes of SMPI significantly, increasing its potential for use within the food industry. © 2024 Society of Chemical Industry.

Improving the quality of egg yolk granules via cryogenic processing: A comprehensive analysis of structural, physicochemical, and functional properties.

Rheological, structural and thermal characteristics of protein isolates obtained from album (Chenopodium album) and quinoa (Chenopodium quinoa) seeds

Background: To date, there is no x-ray crystallography or structures from nuclear magnetic resonance (NMR) on royal jelly proteins available in the online data banks. In addition, characterization of proteins in royal jelly is not fully accomplished to date. Although new investigations unravel novel proteins in royal jelly, the majority of a protein family is present in high amounts (80-90%). Objective: In this review, we attempted to predict the three-dimensional structure of royal jelly proteins (especially the major royal jelly proteins) to allow visualization of the four protein surface properties (aromaticity, hydrophobicity, ionizability and (hydrogen (H)-bond) by using bioinformatics tools. Furthermore, we gathered the information on available therapeutic activities of crude royal jelly and its proteins. Methods: For protein modeling, prediction and analysis, the Phyre2 web portal systematically browsed in which the modeling mode was intensive. On the other side, to build visualized understanding of surface aromaticity, hydrophobicity, ionizability and H-bond of royal jelly proteins, the Discovery Studio 4.1 (Accelrys Software Inc.) was used. Results: Our in silico study confirmed that all proteins treasure these properties, including aromaticity, hydrophobicity, ionizability and (hydrogen (H)-bond. Another finding was that newly discovered proteins in royal jelly do not belong to the major royal jelly protein group. Conclusion: In conclusion, the three dimensional structure of royal jelly proteins along with its major characteristics were successfully elucidated in this review. Further studies are warranted to elucidate the detailed physiochemical properties and pharmacotherapeutics of royal jelly proteins.