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In this study, 1.5% (m/m) tilapia myofibrillar protein (MP) and corn oil (0%, 10%, 68% or 70%, V/V) were used to prepare emulsions. Molecular dynamics (MD) combined with Raman spectroscopy was used to investigate the structural changes of MP adsorbed at the emulsion interface. MD simulation showed that the spatial conformation of myosin was changed when the protein adsorbed onto the interface of emulsions with different proportions of oil phase; the secondary structure contained about 48% α-helix, and the structure remained relatively stable after the protein adsorbed onto the interface. The change of myosin spatial conformation was accompanied by the increase of solvent accessible surface area (SASA) and the enhancement of hydrophobic interaction, which made the emulsion stable. Raman spectra showed secondary structural changes similar to those of MD. In addition, Raman spectroscopy results showed that tryptophan (Trp) and tyrosine (Tyr) residues were exposed on the protein surface and participated in hydrogen bond formation and hydrophobic interaction, which was conducive to the stability of the emulsion system. In conclusion, changes in the spatial conformation and the microenvironment of side chain groups of MP adsorbed at the oil/water interface of emulsions can promote the hydrogen bond and hydrophobic interaction between protein molecules, and consequently the formation of a tight interfacial film at the oil/water interface, which is conducive to improving the stability of emulsions.

• Effect of peptide concentration on high internal phase emulsion (HIPE) was studied. • Effect of HIPE on the three-dimensional - printing surimi ink was studied. • Peptide concentration affected the microstructure and rheology of HIPE. • The addition of HIPE decreased the porosity of surimi. The effect of a high internal phase emulsion (HIPE) on three-dimensional-printed surimi gel inks was studied. Increasing the concentration of collagen peptide decreased the particle size of HIPE droplets and improved the viscoelasticity and stability. For example, when the collagen peptide concentration was 5 wt%, the viscoelasticity of the HIPE was high, as indicated by the presence of small and uniform particles, which formed a monolayer in the outer layer of the oil droplets to form stable a HIPE. A HIPE was used as the filling material to fill the surimi gel network, which reduced the porosity of the network. Surimi protein and peptides have dual emulsifying effects on the stabilization of oil. After adding the emulsion, the texture, gel properties and rheological properties of the surimi were reduced, and its printing adaptability was improved. This study provides new ideas for the production of surimi and its application in 3D printing. [ABSTRACT FROM AUTHOR]

• MP emulsion gel was prepared with one-step homogenization for use as lipid carriers. • MP emulsion gel had great stability and high G′ after heating and freezing. • Surimi products had great stability and low gel strength when lipid content hit 35%. • Dual emulsification of MP in emulsion gel and surimi were keys to stable lipid. In this study, surimi products rich in lipids were prepared by using myofibril protein (MP) emulsion gel as carriers. The MP emulsion gel (MP concentration, c = 1.5%, oil fraction, ø = 0.68) was prepared by one-step homogenization. The emulsion gel maintained a high elastic modulus (G′) after heating and freezing treatment. Confocal laser scanning microscopy revealed that the structure of the emulsion gel was a hybrid network consisting of polymers of cross-linked MP and aggregated protein-stabilized emulsion (W/O/W multiple structures) droplets. The double emulsification of the emulsion gel and MP stabilized the oil droplets in the surimi product, preventing water and oil from leaching out. The microstructure also showed smaller gaps between MPs with increased porosity, while oil droplets were stably embedded in the surimi gel matrix. Moreover, adding MP emulsion gel significantly reduced the surimi gel strength compared to adding oil directly (p < 0.05). [ABSTRACT FROM AUTHOR]

The key clock protein Period2 (Per2) has been suggested to play an essential role in regulating endothelial function. It also regulates the expression of plasminogen activator inhibitor-1, but its role in stroke development has not been studied. To explore the possible association between Per2 and ischemic stroke (IS), 479 Chinese IS patients and 306 healthy controls were recruited, and five tag single nucleotide polymorphisms representing thePer2locus were genotyped using the Sequenom MassARRAY system. A significant difference was observed in the genotypic distribution (p = 0.014) and allele frequency (p = 0.005) of rs10462023, with carriers of the G allele being more prone to developing IS. After adjusting for possible risk factors including smoking, alcohol use, and history of hypertension and diabetes, a significant association was still apparent. Haplotype analysis also supported the association between Per2 and IS. This study suggests thatPer2variations are associated with IS and may represent genetic risk factors for IS in a Chinese population. [ABSTRACT FROM PUBLISHER]