FOOD SCIENCE ›› 2025, Vol. 46 ›› Issue (18): 393-346.doi: 10.7506/spkx1002-6630-20250422-184

• Reviews • Previous Articles    

Factors Affecting Heat-Induced Gel Properties of Myofibrillar Protein and Their Mechanisms of Action: A Review

ZHANG Lei, SUN Hailei, MAO Yanwei, WANG Mengxue, HAN Yongsheng, MA Weidong, ZHANG Yimin   

  1. (1. College of Food Science and Engineering, Shandong Agricultural University, Tai’an 271018, China; 2. Animal Husbandry and Veterinary Branch, Heilongjiang Academy of Agricultural Sciences, Qiqihar 150086, China; 3. Shaanxi Agricultural and Animal Husbandry Breeding Farm, Baoji 712199, China)
  • Published:2025-08-19

Abstract: Myofibrillar protein is a salt-soluble protein that determines the quality of muscle, and its heat-induced gel properties directly affect the quality of emulsified and minced meat products. Meat researchers worldwide have been interested in the factors affecting the gel properties of myofibrillar protein. Structural and functional modification of myofibrillar proteins can improve the functional properties of myofibrillar protein gels. Currently, the main strategies for modifying myofibrillar proteins include addition of exogenous substances and physical treatments. However, a comprehensive summary of the effects of different treatments on the structure and function of myofibrillar proteins is lacking. Therefore, this review focuses on the various factors that affect and improve the gel properties of myofibrillar proteins and their mechanisms of action in terms of the environment in which the proteins exist, physical modification techniques and exogenous additives, clarifying that different environments in which myofibrillar proteins exist and physical modification techniques affect their gel properties by altering their conformation and that exogenous additives affect their gel properties by binding to the proteins to form aggregates. This review provides a theoretical reference for enhancing the quality of gelled meat products.

Key words: myofibrillar protein; gel properties; exogenous additives; physical modification techniques; surrounding environment of proteins

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