Myofibrillar protein (MP) gels with desirable textural properties are highly favored by customers. In the present study, the effects of different charged polysaccharides, including neutral dextran (DX), anionic κ-carrageenan (KC) and cationic chitosan (CS), on modulating the thermal gelation properties of microbial transglutaminase (MTGase)-mediated MP were investigated. The results suggested that the thermal gelation characteristics of composite gel systems formed by combining MTGase with three polysaccharides respectively were improved, regardless of polysaccharide ion types. Furthermore, cationic CS was the most effective in increasing water-holding capacity (WHC), texture properties, and viscoelastic characteristics of composite gels, followed by neutral DX and then anionic KC. Based on the results of water state and distribution, the incorporation of three polysaccharides strengthened the water entrapment effect of MTGase-mediated MP gel network. Additionally, cationic CS displayed the greatest effect on driving the generation of β-sheet structures, facilitating the formation of disulfide bonds and enhancing hydrophobic interactions, thereby contributing to the formation of a uniform and well-organized gel matrix network. These findings provide theoretical support for formula optimization and quality improvement of meat products by modulating MP during thermal processing.
Xiaomin Zhang, Shuxia Wu, Cheng Tang et al.· International Journal of Bio...· 0 citations
Growing demand for sustainable, nutritious, and high-quality protein foods has highlighted limitations of single-source proteins and promoted interest in dual-protein systems (DPS). DPS are edible protein matrices intentionally formed from two distinct primary protein components, derived from different biological sources or complementary protein fractions, and processed within a shared physicochemical environment. This review integrates their definition, fabrication strategies, interaction mechanisms, functional properties, nutritional implications, and food applications. Protein-protein interactions, including electrostatic, hydrophobic, hydrogen-bonding, and disulfide-mediated interactions, regulate unfolding, aggregation, interfacial adsorption, and network formation. Processing methods such as blending, co-precipitation, ultrasound, microwave treatment, pH shifting, fermentation, germination, and enzymatic cross-linking further modify structure and functionality. These changes affect solubility, emulsification, foaming, gelation, rheology, digestibility, and storage stability. Nutritionally, DPS may improve amino acid complementarity, digestion behavior, and bioactive peptide release, but their benefits depend on protein source, ratio, processing conditions, and matrix. Applications in meat and seafood analogues, dairy-like systems, bakery products, beverages, and structured foods show potential for quality and sustainability improvement. However, sensory defects, allergenicity, limited digestibility evidence, and insufficient consumer studies remain challenges. This review provides a framework for designing stable, nutritious, sustainable, and acceptable dual-protein foods.
Xue Bai, Kai Zhou, Ranran Pang et al.· Journal of Food Science· 0 citations
Temperature-dependent variations in the molecular characteristics of intact spores, including changes associated with Ca2+-dipicolinic acid, protein-related, and nucleic acid-related spectral features under different sporulation temperatures are revealed.
Mengya Li, Kequan Xing, Sun-Hee Wang et al.· Food Research International· 0 citations