Using temporal dominance of sensations (TDS), multiple-sip TDS, chemical composition evaluation, and microstructural analysis to assess the impact of repeated reheating cycles on chicken soup.

Reheating chicken soup is a common culinary practice in daily life. To investigate the impact of reheating frequency on the sensory quality of chicken soup, temporal dominance of sensations (TDS) and multi-TDS were used to characterize changes in dominant sensory attributes during consumption. Additionally, E-nose and E-tongue were utilized to analyze differences in aroma and taste profiles. The alterations in sensory properties were further elucidated by analyzing variations in amino acids, volatile compounds. The findings revealed that there was no significant disparity between fresh soup and heating. However, saltiness and umami, as the most prominent dominant characteristics, intensified with increasing reheating cycles. This can be attributed to an elevation in certain amino acids that contribute to umami perception. Conversely, a reduction in some aldehydes weakened the flavor associated with fat and meat components. Moreover, enlarged oil droplets with uneven distribution within heated soup may account for the heightened greasiness sensation.

Catechins affect the oil-holding capacity of meat batters by changing the structure and emulsifying properties of surface proteins at the fat globules.

The effects of different concentrations of catechins on the oil-holding capacity, myofibrillar proteins (MPs) structure and adsorbed properties of interfacial proteins in meat batters were investigated. The addition of 100 mg/kg catechin had no negative effects on the physicochemical properties of meat batter. However, 500 and 1500 mg/kg catechin caused an increase in drip loss and deterioration of dynamic rheological properties; the total sulfhydryl content, surface hydrophobicity and α-helix ratio of MPs decreased significantly (p < 0.05); in meat emulsions, the emulsifying property was reduced, the particle size increased, and less interfacial protein was absorbed on the fat globules. All concentrations of catechins significantly (p < 0.05) inhibited lipid oxidation in meat batters. Medium and high concentrations of catechins induced aggregation of MPs via covalent and noncovalent interactions between MPs and MPs or MPs and catechins, which destroyed the gel and emulsifying property of protein and eventually decrease the oil-holding capacity of meat batters.

The Effects of Ethanol and Rutin on the Structure and Gel Properties of Whey Protein Isolate and Related Mechanisms.

The effects of different levels of rutin (0, 0.05%, 0.1%, 0.2% and 0.3% w/v) and ethanol on the structure and gel properties of whey protein isolate (WPI) were examined. The results showed that the addition of ethanol promoted the gel formation of WPI. The addition of rutin increased the gel strength of WPI and maintained the water-holding capacity of the gel. Ethanol caused an increase in thiol content and surface hydrophobicity, but rutin decreased the thiol content and surface hydrophobicity of WPI. The particle size, viscosity and viscoelasticity of WPI increased at rutin levels of 0.2% and 0.3%, indicating that rutin caused cross-linking and aggregation of WPI, but rutin had no significant effect on the zeta-potential, indicating that electrostatic interactions were not the main force causing the changes in protein conformation and gel properties. Ethanol and rutin improved the gel properties of WPI possibly by inducing cross-linking of WPIs via hydrophobic and covalent interactions.

Improved effect of flaxseed gum on the weakened gelling properties of myofibrillar protein induced by catechin.

The effect of flaxseed gum (FG) on the weakened gelling properties of myofibrillar proteins (MP) induced by catechin was investigated. Different levels of FG and catechin were incorporated into MP and the chemical changes of MP were studied; MP emulsions and gels with different levels of FG and catechin were prepared and their properties were studied. Catechin promoted the loss of thiol and the exposure of the hydrophobic groups of MP and increased the particle size and apparent viscosity of emulsions, resulting in a poor gel network. The incorporation of FG enhanced the gel strength, water holding capacity and dynamic rheological properties, which might be attributed to the formation of uniform and stabilized emulsions with high apparent viscosity and the enhanced disulfide cross-linking and hydrophobic interactions during heat-induced gelation. FG could be a potential approach in overcoming the deterioration of protein gels caused by catechin.