食品与发酵工业 >

2026 , Vol. 52 >Issue 10: 258 - 266

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.043166

研究报告

不同加热条件对梅花鹿腿肉品质及其肌原纤维蛋白特性的影响

  • 李越佳 ,
  • 王琛 ,
  • 李潇 ,
  • 韩艳秋 ,
  • 叶馨阳
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  • (辽宁省农业科学院,辽宁 沈阳,110161)
第一作者:硕士,工程师(通信作者,E-mail:15142553298@163.com)

收稿日期: 2025-04-29

  修回日期: 2025-10-21

  网络出版日期: 2026-06-15

基金资助

辽宁省农业科学院院长基金项目(1207405)

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Effects of different heating conditions on meat quality and myofibrillar protein properties of sika deer leg meat

  • LI Yuejia ,
  • WANG Chen ,
  • LI Xiao ,
  • HAN Yanqiu ,
  • YE Xinyang
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  • (Liaoning Academy of Agricultural Sciences, Shenyang 110161, China)

Received date: 2025-04-29

  Revised date: 2025-10-21

  Online published: 2026-06-15

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摘要

为探究不同加热条件下梅花鹿腿肉品质及其肌原纤维蛋白的变化规律,对不同加热温度和加热时间下梅花鹿腿肉的剪切力、质构、蒸煮损失、微观结构及其肌原纤维蛋白的浊度、表面疏水性、羰基含量、总巯基含量以及二级结构进行测定和分析。结果表明,随着加热温度的上升和加热时间的延长,鹿腿肉剪切力、硬度、咀嚼性和胶黏性呈下降趋势,蒸煮损失显著上升;扫描电镜观察发现,加热会破坏肌肉组织结构的完整性,致使肌纤维收缩,肌纤维束间的孔隙增大,肌内膜与肌束膜破裂。肌原纤维蛋白的浊度和表面疏水性均在70 ℃时上升,而在90 ℃以上不断下降;蛋白质羰基含量持续上升,总巯基含量持续下降;傅里叶红外光谱显示,热处理可能促进β-转角的解构和β-折叠的生成。综上所述,加热会改变肌原纤维蛋白的特性和结构,并且对鹿腿肉的品质产生影响。

关键词： 加热条件; 梅花鹿腿肉; 品质; 肌原纤维蛋白

本文引用格式

李越佳 , 王琛 , 李潇 , 韩艳秋 , 叶馨阳 . 不同加热条件对梅花鹿腿肉品质及其肌原纤维蛋白特性的影响[J]. 食品与发酵工业, 2026 , 52(10) : 258 -266 . DOI: 10.13995/j.cnki.11-1802/ts.043166

Abstract

To investigate the changes in quality of sika deer leg meat and myofibrillar proteins under varying heating conditions, this study assessed and analyzed shear force, texture, cooking loss, microstructure of sika deer leg meat, as well as turbidity, surface hydrophobicity, carbonyl group content, total sulfhydryl group content, and secondary structure of myofibrillar proteins.These parameters were assessed under different heating temperatures and durations.Results indicated that as heating temperature and time increased, the shear force, hardness, chewiness, and adhesiveness of sika deer leg meat exhibited a decreasing trend while cooking loss significantly increased.Scanning electron microscopy revealed that heating compromised the integrity of muscle tissue structure, this resulted in muscle fiber contraction with an increase in pore size between muscle fiber bundles and disruption of endomysium and perimysium.Turbidity and surface hydrophobicity of myofibrillar rose at 70 ℃ but decreased at temperatures exceeding 90 ℃.The protein carbonyl group content consistently increased while the total sulfhydryl content steadily declined.Fourier-transform infrared spectroscopy analysis suggested that heat treatment may promote the deconstruction of β-angle and the formation of β-fold.In conclusion, heating alters both the properties and structure of myofibrillar proteins which subsequently impacts the quality of sika deer leg meat.

Key words： heating condition; sika deer leg meat; quality; myofibrillar protein

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