Effects of different heating conditions on protein composition in each muscle type of yellowtail (Seriola quinqueradiata)

Abstract

To clarify the factors influencing the physical properties of fish after heat treatments, we investigated changes in the properties of proteins in the dorsal ordinary and dark muscle of yellowtail (Seriola quinqueradiata) heated under different conditions commonly used for the purposes of food hygiene. High-temperature/short-time heating (85℃ for 90 s and 75℃ for 60 s) affected the protein solubility more than low-temperature/long-time heating (63℃ for 30 min). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and differential scanning calorimetry showed that low-temperature/long-time heating reduced the degree of actin denaturation in fish compared with that by other heating conditions. In addition, collagen solubility was enhanced with low-temperature/long-time heating. Therefore, these results suggest that differences in the degree of actin and collagen denaturation are responsible for the enhanced meat tenderness and diminished meat shrinkage, resulting from low-temperature/ long-time heating.

Influence of mixing speed, solids concentration and enzyme dosage on dry solids yield and protein recovery during enzymatic hydrolysis of sardine (Sardina pilchardus) processing by-products using Alcalase 2.4L: a multivariable optimisation approach

“…Chan et al [82] showed that thermal treatment causes thermal aggregation, which reduces protein solubility as more hydrophobic surfaces of the protein become exposed to water. This is in agreement with Furuta et al [77] who showed that heating fish protein at 75 °C for 1 min or at 95 °C for 1.5 min significantly reduced protein solubility. Enzyme hydrolysis reactions are typically quenched at temperatures above 80 °C for at least 15 min [8,[83][84][85], which is sufficient time to lose protein to thermal aggregation.…”

“…The presence of unhydrolysed protein in the sludge is typical of enzyme hydrolysis processes where not all substrate is accessible to enzyme or soluble during the enzymatic reaction [49,60,75,76]. Different studies have shown that the denaturation temperature of fish protein generally ranges from 65 to 95 °C [77][78][79][80][81][82]. Chan et al [82] showed that thermal treatment causes thermal aggregation, which reduces protein solubility as more hydrophobic surfaces of the protein become exposed to water.…”