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[Display omitted] • Ultrasound and carrageenan jointly improves the myofibrillar protein gel properties. • Ultrasound combined with carrageenan leads to heated rearrangement aggregation. • Carrageenan acts on protein by crosslinking and insertion. • Carrageenan competes with proteins for binding to water molecules in heating. To improve the limitation of transglutaminase on the quality of myofibrillar protein (MP) gel, this study investigated the synergistic effect of ultrasonic pretreatment in combination with carrageenan on the gel properties of transglutaminase-mediated MP gels. The synergistic effect generated gel with lower surface hydrophobicity and fluorescence intensity. Combined with the secondary structure results, it can be hypothesized that the synergistic effect caused the rearrangement of the proteins and the formation of aggregates wrapping hydrophobic groups, which changed the structure and phase behavior of the proteins. The synergistic effect also improved the formation of dense and interpenetrating gel networks, which reduced cooking loss and produced composite MP gels with optimal gel strength. Moreover, FTIR spectroscopy revealed the presence of electrostatic interactions in the hybrid gel system. This study provides a theoretical basis and experimental foundation for the effective use of high-tech composite functional components to improve the quality of gel products. [ABSTRACT FROM AUTHOR]

In this paper, fermented solid beef inoculated with two starter cultures ( Lactobacillus curvatus and Pediococcus pentosaceus) in different inoculums concentration, fermentation time, and fermentation temperature was evaluated for change of protein composition (water-soluble proteins, insoluble protein, and salt-soluble proteins) and nonprotein nitrogen during fermentation and the relevance with textural properties was also investigated. The amount of water-soluble and salt-soluble proteins decreased while nonprotein and insoluble proteins increased as fermentation progressed. With the increase of inoculums concentration from 0.5% to 2.5%, the amount of water-soluble and salt-soluble proteins decreased from 23.8 to 19.6 mg/g and 51.2 to 33.5 mg/g, respectively, and the amount of nonprotein and insoluble proteins increased from 17.8 to 24.4 mg/g and 20.3 to 49.5 mg/g, respectively. During 0 to 32 hr of fermentation, the water-soluble and salt-soluble proteins decreased from 24.4 to16.0 mg/g and 54.0 to 22.0 mg/g, respectively, and the amount of nonprotein and insoluble proteins increased from 16.3 to 30.8 mg/g and 19.6 to 70.5 mg/g, respectively. With the fermentation temperature increased from 20°C to 40°C, the water-soluble decreased from 34.6 to 21.8 mg/g; the amount of salt-soluble proteins decreased from 60.0 to 21.2 mg/g; the nonprotein and insoluble proteins increased from 16.2 to 24.3 mg/g and 29.7 to 70.4 mg/g, respectively. From SDS-PAGE analysis of water-soluble and salt-soluble proteins, solid beef protein tended to degrade to smaller protein, peptide, and amino acid with protease and peptidases enzymes, and partially form large polymers. Hardness, elasticity, gumminess, and chewiness were significantly negatively correlated with water-soluble and salt-soluble proteins, and were significantly positively correlated with insoluble proteins. The optimum inoculum population, fermentation time, and fermentation temperature were 2%, 32 hr, and 35°C, respectively. Practical applications Our paper studied the effects of fermentation conditions including inoculums concentration, fermentation temperature, and fermentation time on the change of protein composition of fermented solid beef and nonprotein nitrogen. Meanwhile, explored the relationship between the protein composition and texture properties. Fermentation degrades proteins into smaller protein, peptides, and free amino acids. It is beneficial for absorption and good for health. And now the fermentation meat products become more and more popular. However, the quality of beef products is related to muscle proteins that the changes of protein molecules can be effectively affected the properties of products. Our preliminary observation provides a theoretical basis for further researches on quality evaluation of fermentation meat products, and hope to improve the quality of fermentation meat products. [ABSTRACT FROM AUTHOR]

High-intensity pulsed electric field (PEF) was used to extract protein from mussel. Results show that PEF extraction speed is much faster, and the extraction yield of protein is higher compared with traditional methods. Variation of PEF parameters and the extraction yield of protein were determined by single-factor experiments. The processing conditions were optimized by response surface methodology. The maximum extraction yield of protein of 77.08% was achieved under the following conditions: electric field intensity of 20 kV/cm, pulse number of 8 and enzymolysis time of 2 h. PEF can be widely used to extract protein with high speed and low pollution. Practical Applications Freshwater mussel is widely cultured in China and plays a very important role in aquaculture business. Recently, thanks to the nutritional value, advantages for human diets and edibleness as other shellfish such as shrimp, clam, lobster, scallop, abalone and crab, mussel is in growing value. It is valuable to exploit it. This study of PEF method to extract protein from mussel is important to utilize the mussel meat. PEF, with advantages of non-thermal performance, speediness, efficiency, low power and low pollution, is currently used for non-thermal pasteurization of food and extraction of value components from different natural sources. The results of this study are helpful to the further research of PEF method of protein extraction of mussel and, as such, are of practical significance. [ABSTRACT FROM AUTHOR]