The interaction between sodium alginate and myofibrillar proteins: The rheological and emulsifying properties of their mixture.

The interaction between sodium alginate (SA) and turbot myofibrillar proteins (TMP) and the effects of SA concentration (0.1%-0.5%) on the rheological and emulsifying properties of the mixture at neutral pH were investigated. TMP and SA formed complexes through electrostatic repulsion and hydrophobic interaction. The FT-IR analysis indicated that hydrogen bonding was also related to the interaction. With the addition of SA, the electrostatic repulsion between molecules enhanced, which prevented protein aggregation and improved the stability of dispersions. The TMP/SA mixture showed non-Newtonian shear-thinning behavior. The viscosity gradually increased with the increasing SA concentration. TMP and SA formed an interconnected gel-like network structure with a predominant elastic behavior. The strength of network increased due to the strong repulsion between the two biopolymers. Both EAI and ESI of TMP significantly increased after SA addition. The addition of SA reduced droplet size of emulsions. The emulsions also showed pseudoplastic behavior. Addition of SA increased stability of emulsions by increasing viscosity of continuous phase. Complexation with SA effectively improved the rheological and emulsifying properties of fish myofibrillar proteins. These results contributed to the efficient utilization of marine fish proteins as functional ingredients in food products.

Physicochemical and emulsifying properties of mussel water-soluble proteins as affected by lecithin concentration.

The effects of lecithin addition at different concentrations (0-2.0%) on the physicochemical and emulsifying properties of mussel water-soluble proteins (MWP) were investigated. In solution system, low lecithin concentration (0.5%-1.0%) induced the aggregation and increased turbidity of composite particles. Lecithin addition caused changes in secondary structure and induced partial unfolding of MWP. Hydrophobic interactions between MWP and lecithin may contribute to the exposure of chromophores and hydrophobic groups of MWP. The interfacial tension decreased with lecithin addition. However, at a high lecithin concentration (1.5%-2.0%), the degree of aggregation and state of unfolding alleviated due to competitive adsorption. In emulsion system, with the low concentration of lecithin addition (0.5%-1.0%), droplet size and surface charge of emulsion decreased. The emulsion activity index, emulsion stability index, percentage of adsorbed protein increased. Both creaming stability and viscoelastic properties improved. At an intermediate lecithin concentration (1.0%), the emulsion showed the highest physical stability, while further addition of lecithin caused a slight deterioration in emulsifying properties. Overall, these results indicated the possibility that the lecithin-MWP mixed emulsifiers can be used to obtain emulsions with desirable properties.

Application of high-pressure homogenization for improving the physicochemical, functional and rheological properties of myofibrillar protein.

The present work investigated effects of high-pressure homogenization (HPH) pressure (0, 40, 80 and 120 MPa) on physicochemical, functional and rheological properties of clam myofibrillar protein (CMP). Results showed that HPH changed the CMP secondary and tertiary structures. Absolute zeta potential and protein solubility increased but particle size and turbidity of CMP decreased after HPH treatment. Both of emulsifying properties and foaming properties were significantly improved. The shear stress, apparent viscosity and the viscosity coefficients reduced, but flow index increased. Application of HPH improved the physicochemical, functional and rheological properties of CMP, and 120 MPa was the optimal pressure for modification.

High-Pressure Homogenization Pre-Treatment Improved Functional Properties of Oyster Protein Isolate Hydrolysates.

The effects of HPH (high-pressure homogenization) pre-treatment on the functional properties of OPIH (oyster protein isolates hydrolysates) were studied. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles, solubility, particle size distribution, zeta potential, surface hydrophobicity, emulsifying activity index and microstructure of emulsions were analyzed. Results indicated that HPH pre-treatment increased the accessibility of OPI to trypsin hydrolysis, resulting in decease in particle size, increase in solubility, absolute zeta potential, surface hydrophobicity and emulsifying activity index. In addition, HPH pre-treated OPIH emulsions became more uniform and the particle size of droplets decreased. These results revealed that HPH pre-treatment has the potential to modify the functional properties of OPIH.

Effects of high-pressure homogenization on functional properties and structure of mussel (Mytilus edulis) myofibrillar proteins.

Mussel myofibrillar proteins (MMP) suspensions (10.6% ±â€¯0.5%, w/v) were treated by high-pressure homogenization (HPH) at 0 (control), 20, 40, 60, 80 or 100 MPa for 3 cycles. Particle size distribution, zeta potential, solubility, water and oil holding capacity, emulsifying, foaming properties, secondary structure, free sulfhydryl and surface hydrophobicity of the obtained suspensions were analyzed. The results showed that functional properties of MMP significantly (P < 0.05) improved after HPH treatment. Absolute zeta potential, emulsifying activity index, emulsion stability index, foaming ability and foaming stability increased by 23.64 mV, 14.99 m2/g, 4.3 min, 17.3% and 29.7% at 80 MPa, protein solubility and oil holding capacity increased by 7.4% and 1300% at 100 MPa. However, HPH treatment significantly (P < 0.05) decreased particle size and water holding capacity. HPH treatment altered secondary structure, tertiary and quaternary structure. Functionality improvements mainly resulted from changes in structure and decrease in particle size. The results showed that HPH has potential for improving functional properties of MMP, thus expand its application in food industry.