食品科学 ›› 2020, Vol. 41 ›› Issue (13): 61-68.doi: 10.7506/spkx1002-6630-20191128-280

• 基础研究 • 上一篇    下一篇

加热温度对麻鸭肌原纤维蛋白结构与凝胶特性的影响

王正雯,田宏伟,周富裕,张志芳,何俊,孙杨赢,曹锦轩,潘道东   

  1. (1.宁波大学 浙江省动物蛋白食品精深加工技术重点实验室,浙江 宁波 315800;2.宁波大学食品与药学学院,浙江 宁波 315800;3.湖北周黑鸭企业发展有限公司,湖北 武汉 430040)
  • 出版日期:2020-07-15 发布日期:2020-07-29
  • 基金资助:
    宁波市公益性项目(2019C10017);浙江省重点研发计划项目(2019C02085); 国家水禽产业技术体系加工与副产物综合利用岗位科学家基金项目(CRAS-42-25)

Effect of Heating Temperature on Myofibrillar Protein Structure and Gel Properties of Sheldrake Breast Muscle

WANG Zhengwen, TIAN Hongwei, ZHOU Fuyu, ZHANG Zhifang, HE Jun, SUN Yangying, CAO Jinxuan, PAN Daodong   

  1. (1. Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province, Ningbo University, Ningbo 315800, China; 2. College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo 315800, China;3. Hubei Zhouheiya Enterprise Development Co. Ltd., Wuhan 430040, China)
  • Online:2020-07-15 Published:2020-07-29

摘要: 为研究不同加热温度(50~100 ℃)对麻鸭胸脯肉肌原纤维蛋白凝胶结构及其特性的影响,测定凝胶保水性、质构、表面疏水性,观察凝胶的微观结构并结合拉曼光谱分析蛋白二级结构变化,探讨加热温度、蛋白结构和凝胶特性的相关性。结果表明:50 ℃时麻鸭胸脯肉肌原纤维蛋白凝胶保水性最低,60 ℃时蛋白开始变性并发生聚集,70 ℃时形成结构紧密细腻的凝胶;随着加热温度升高,凝胶网络孔径变大,保水性显著降低(P<0.05);拉曼光谱位于545、760、1 340 cm-1处特征峰的归一化强度随加热温度升高整体呈现下降趋势,说明二硫健伸缩振动发生变化,色氨酸从包埋态逐渐暴露,蛋白表面疏水性增强;50 ℃时,α-螺旋相对含量为66.95%,随着加热温度升高显著下降(P<0.05),100 ℃时下降至19.73%,加热过程中β-折叠、β-转角、无规卷曲相对含量升高。综上所述,70 ℃时形成的麻鸭肌原纤维蛋白热诱导凝胶均匀致密,且保水性达到最大。

关键词: 麻鸭, 肌原纤维蛋白, 二级结构, 热诱导凝胶, 拉曼光谱

Abstract: In order to investigate the effect of heating temperature (50–100 ℃) on myofibrillar protein (MP) structure and gel properties of sheldrake breast muscle, water-holding capacity (WHC), texture, surface hydrophobicity, microstructure and secondary structure were determined. Correlation analysis was performed to establish relationships among heating temperature, protein structure and gel properties. Results showed that the lowest WHC was obtained by heating at 50 ℃, heating at 60 ℃ could result in MP denaturation and aggregation, and a compact and exquisite gel structure was formed at 70 ℃. As the heating temperature increased, the pore size of the gel network became larger and the WHC decreased significantly (P < 0.05). The normalized strength of the characteristic absorption peaks at 545, 760 and 1 340 cm-1 in the Raman spectral showed a downward trend with increasing heating temperature, indicating changes in the disulfide stretching vibration together with gradual exposure of buried tryptophan residues and increased surface hydrophobicity. The α-helix content decreased significantly (P < 0.05) from 66.95% to 19.73% when the heating temperature increased from 50 to 100 ℃, while the contents of β-sheet, β-turn, and random coil increased. In summary, a homogeneous sheldrake MP gel microstructure was formed by heating at 70 ℃ and the formed gel had the maximum WHC .

Key words: sheldrake, myofibrillar protein, secondary structure, heat-induced gelation, Raman spectroscopy

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