The growing demand for healthier meat products and the advancement of functional foods have positioned myofibrillar protein (MP)-based emulsions and emulsion gels as a central focus in food texture engineering. The primary challenge in research on MP-based emulsions and emulsion gels is to elucidate and precisely control the multi-scale coupling mechanisms, from interfacial film dynamics to network formation. This review consolidates recent advances in MP-based emulsions and emulsion gels, summarising the adsorption and conformational evolution of MP at the oil-water interface. It evaluates interfacial engineering strategies to enhance stability and examines the synergistic effects of thermal bulk gelation, interfacial protein evolution and thermal droplet motion on network formation. Finally, the potential of these systems for advanced food applications is discussed. This will enable precise design and application of MP-based emulsions and emulsion gels in food systems.
Jingming Zhang, Hong-Lei Zhao, Chuanai Cao et al.· Food Chemistry· 0 citations
Soluble soybean polysaccharide (SSPS) demonstrates distinct structure and function in forming non-covalent complexes with soy protein isolate (SPI) and stabilizing diacylglycerol (DAG) emulsions. The complexation between SPI and SSPS was predominantly driven by non-covalent interactions, specifically electrostatic forces and hydrogen bonding. SSPS induced SPI unfolding, increased secondary structure disorder, molecular flexibility, particle size and surface charge. At 0.1% SSPS, SSPS cross-linked SPI, exposing hydrophobic groups and increasing surface hydrophobicity and amphiphilicity. However, with 0.2% SSPS, the increased coverage began to shield these hydrophobic groups, reducing surface hydrophobicity. With 0.3%-0.4% SSPS, SSPS formed a continuous hydrophilic network that improved stability and viscosity via steric hindrance, while competitively adsorbing onto the DAG interface and becoming the dominant stabilizer. Thus, SSPS acts as a structural modulator that governs SPI complexation and competitively stabilizes DAG emulsions, utilizing DAG's amphiphilic hydroxyl groups to optimize interface performance for functional lipid use.