Journal
LWT-FOOD SCIENCE AND TECHNOLOGY
Volume 154, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.lwt.2021.112629
Keywords
Myofibrillar protein; Insect protein; pH shift; Thermal stability; Rheological properties
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Funding
- Main Research Program of the Korea Food Research Institute [E0211200-01]
- National Research Council of Science & Technology (NST), Republic of Korea [E0211200-01] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The study showed that isolated insect proteins (IIP) subjected to an acidic pH can enhance the thermal stability and viscosity of myofibrillar protein (MP) gel, while reducing cooking loss and hardness. Acidic IIP also exhibited the highest springiness, gumminess, and chewiness, indicating its potential to improve the quality of MP.
The effect of pH-shifted isolated insect proteins (IIP) on a myofibrillar protein (MP) gel was studied. When extracted the protein of Allomyrina dichotoma, pH of insect was shifted to pH 1 and pH 10. The 40 mg/mL MP was homogenized with 0.25% (w/v) of IP. The thermal stability of actin groups increased with the addition of IIP, and pH-modified IIP showed high thermal stability; viscosity improved with the addition of IIP and pH shift. The pH of IIP treatments was lower than that of the control regardless of pH-shifting condition. Disulfide bonds and hydrophobic interactions had the most effect on forming protein gels. Cooking loss and hardness in IIP-treated group were lower than those of the control, and acidic IIP had the highest springiness, gumminess, and chewiness. Therefore, IIPs subjected to an acidic pH may be used to improve the quality of MP.
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