Toward the design of insect-based meat analogue: The role of calcium and temperature in coagulation behavior of ce:italic>Alphitobius diaperinus/ce:italic> proteins

摘要

This study focused on the coagulation behavior of protein from larvae ofAlphitobius diaperinus. The effect of incremental CaCl2concentration (10, 15, 20 and 20?mmol/L) and temperature (90, 100?°C) on physical-chemical properties of insectcoagulawas investigated. A yield between 76 and 83?g of coagulum was obtained from 100?g of fresh larvae, decreasing with higher temperature and CaCl2. Protein-protein interactions and microstructure ofcoagulawere analyzed respectively by means of protein solubility, SDS-PAGE and SEM. When higher temperature was applied, hydrophobic interactions and disulphide bonds increased due to a larger degree of protein denaturation, thereby contributing to the formation of large protein aggregates. Thus, significant increase in hardness of thecoagulawas observed, with specimens at 20?mmol/L CaCl2being more than twice harder at 100?°C than at 90?°C. Moreover, proteins homologous to actin and tropomyosin contributed to the coagulum structure by hydrophobic interactions, whereas hemolymph proteins formed disulphide bonds. Increasing concentration of CaCl2from 10 to 20?mmol/L, at 100?°C, displayed a smoother network that increasedcoagulahardness from 1200 to 2900?g respectively. Results of this study provide important information for the product development in relation to insect protein-based meat analogues.