食品工业科技2026，Vol.47Issue(8)：132-142,11.DOI:10.13386/j.issn1002-0306.2025040310
加热温度对罗非鱼肌球蛋白结构及功能特性的影响
Effect of Heating Temperature on the Structure and Functional Properties of Tilapia Myosin
摘要
Abstract
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.关键词
罗非鱼肌球蛋白/加热温度/功能特性/风味结合能力/结构变化Key words
tilapia myosin/heating temperature/functional properties/flavor-binding ability/structural changes分类
轻工纺织引用本文复制引用
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[J].食品工业科技,2026,47(8):132-142,11.基金项目
国家自然科学基金地区科学基金项目(32360632) （32360632）
广西自然科学基金资助(2025GXNSFAA069201) （2025GXNSFAA069201）
国家自然科学基金青年科学基金项目(32001688) （32001688）
北部湾大学大学生创新创业训练计划资助项目(S202411607194,S202411607195). （S202411607194,S202411607195）
