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Effect of Heating Temperature on the Structure and Functional Properties of Tilapia Myosin
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Gang YOU1, Changyu WANG1, Gaigai NIU1, *, Youmei QIN1, Yizhi HUANG1, Jialu WU1, Fuyu XIE1, Tianyi ZHAO2
Science and Technology of Food Industry | 2026, 47(8) : 132 - 142
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Science and Technology of Food Industry | 2026, 47(8): 132-142
• Research and Investigation •
Effect of Heating Temperature on the Structure and Functional Properties of Tilapia Myosin
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Gang YOU1, Changyu WANG1, Gaigai NIU1, *, Youmei QIN1, Yizhi HUANG1, Jialu WU1, Fuyu XIE1, Tianyi ZHAO2
Affiliations
  • 1Guangxi College and University Key Laboratory of High-value Utilization of Seafood and Prepared Food in Beibu Gulf, Guangxi Zhuang Autonomous Region Engineering Research Center of Marine Food Nutrition and Processing Technology Innovation, Laboratory of Beibu Gulf Marine Product Healthy Aquaculture and Green Processing, College of Food Engineering, Beibu Gulf University, Qinzhou 535000, China
  • 2Qinzhou Agricultural Technique Promotion Center, Qinzhou 535000, China
Published: 2026-04-15 doi: 10.13386/j.issn1002-0306.2025040310
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To explore the effect of heating temperature on myosin functional properties, this study systematically analyzed the correlation between its functional properties (solubility, turbidity, emulsifying activity, and flavor binding capacity) and structural changes of tilapia myosin at different temperatures (40~90 ℃). Results demonstrated that with increasing temperature, myosin solubility significantly decreased (51.91% reduction at 90 ℃ vs 40 ℃) (P<0.05), while turbidity and emulsifying activity exhibited a V-shaped trend (initial decline followed by increase). Conversely, flavor-binding capacity displayed an inverted V-shaped pattern, with critical transition points concentrated at 50~60 ℃. Temperature-mediated functional changes were closely associated with structural transitions. In the low-temperature phase (40~50 ℃), partial denaturation induced structural unfolding, characterized by reduced α-helix (5.44% decrease) and β-sheet (42.08% decrease) contents, alongside a 102.64% increase in random coils. This exposed internal hydrophobic groups (0.30% increase in surface hydrophobicity) and active sulfhydryl groups (10.23% increase), enhancing hydrophobic interactions and providing additional flavor-binding sites. However, weakened electrostatic repulsion reduced emulsifying activity. In the medium-temperature stage (50~60 ℃), the unfolding of myosin structure intensified, leading to a 19.59% increase in surface hydrophobicity. The exposed active sites of myosin enhanced flavor-binding capacity, reduced the solubility and increased emulsifying activity and turbidity. In the high-temperature phase (60~90 ℃), irreversible denaturation promoted dense aggregate formation via hydrophobic interactions and disulfide bonds, evidenced by increased β-sheet (19.85%) and β-turn (4.72%) contents. Aggregation led to turbidity increase (6.21% increase at 90 ℃ vs. 40 ℃) (P<0.05), reduced surface hydrophobicity (26.95% reduction), and diminished active sulfhydryl content (76.27% reduction). Although the network formed between myosin molecules enhanced the emulsifying activity (29.68% increase at 80 ℃ vs 60 ℃), it masked flavor-binding sites, decreasing flavor retention. The research results provided theoretical references for the regulation of heat treatment parameters in fish meat product processing.

tilapia myosin  /  heating temperature  /  functional properties  /  flavor-binding ability  /  structural changes
游刚, 王昌宇, 牛改改, 覃由美, 黄一支, 吴佳璐, 谢福瑜, 赵天义. 加热温度对罗非鱼肌球蛋白结构及功能特性的影响. 食品工业科技, 2026 , 47 (8) : 132 -142 . DOI: 10.13386/j.issn1002-0306.2025040310
Gang YOU, Changyu WANG, Gaigai NIU, Youmei QIN, Yizhi HUANG, Jialu WU, Fuyu XIE, Tianyi ZHAO. Effect of Heating Temperature on the Structure and Functional Properties of Tilapia Myosin[J]. Science and Technology of Food Industry, 2026 , 47 (8) : 132 -142 . DOI: 10.13386/j.issn1002-0306.2025040310
Year 2026 volume 47 Issue 8
110
55
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doi: 10.13386/j.issn1002-0306.2025040310
  • Receive Date:2025-04-25
  • Online Date:2026-10-24
  • Published:2026-04-15
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  • Received:2025-04-25
Affiliations
    1Guangxi College and University Key Laboratory of High-value Utilization of Seafood and Prepared Food in Beibu Gulf, Guangxi Zhuang Autonomous Region Engineering Research Center of Marine Food Nutrition and Processing Technology Innovation, Laboratory of Beibu Gulf Marine Product Healthy Aquaculture and Green Processing, College of Food Engineering, Beibu Gulf University, Qinzhou 535000, China
    2Qinzhou Agricultural Technique Promotion Center, Qinzhou 535000, China
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表12种不同金属材料的力学参数
科
Family
属数
Number of
genus
种数
Number of
species
占总种数比例
Percentage of
total species (%)
属
Genus
种数
Number of
species
占总种数比例
Percentage of total
species (%)
鹅膏菌科Amanitaceae 2 11 5.26 鹅膏菌属 Amanita 10 4.78
小菇科 Mycenaceae 2 12 5.74 丝盖伞属 Inocybe 5 2.39
多孔菌科 Polyporaceae 8 14 6.70 蜡蘑属 Laccaria 5 2.39
红菇科 Russulaceae 3 23 11.00 小皮伞属 Marasmius 6 2.87
小菇属 Mycena 11 5.26
光柄菇属 Pluteus 5 2.39
红菇属 Russula 17 8.13
栓菌属 Trametes 5 2.39
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