食品科学 ›› 2025, Vol. 46 ›› Issue (20): 268-276.doi: 10.7506/spkx1002-6630-20250417-135

• 食品工程 • 上一篇    下一篇

真空低温烹饪对南美白对虾肌原纤维蛋白结构的影响

冯洁,费雨萱,周锦均,林慧敏,张宾   

  1. (浙江海洋大学食品与药学学院,浙江 舟山 316022)
  • 出版日期:2025-10-25 发布日期:2025-09-17
  • 基金资助:
    国家自然科学基金项目(U23A20263);浙江省杰出青年项目(LRG25C200001)

Effect of Sous Vide on the Structure of Myofibrillar Protein from Penaeus vannamei

FENG Jie, FEI Yuxuan, ZHOU Jinjun, LIN Huimin, ZHANG Bin   

  1. (Food and Pharmacy College, Zhejiang Ocean University, Zhoushan 316022, China)
  • Online:2025-10-25 Published:2025-09-17

摘要: 为探究真空低温烹饪(sous vide,SV)对南美白对虾肌原纤维蛋白(myofibrillar protein,MP)结构的影响,提取对虾MP后,在设定的不同加工温度(40、50、60、70、80 ℃)下各加热5、10、15 min,以新鲜的南美白对虾MP为对照,测定其十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)、溶解度、表面疏水性、羰基和总巯基含量、傅里叶变换红外光谱(Fourier transform infrared spectroscopy,FTIR)、拉曼光谱。结果显示,随着加工温度升高和时间延长,南美白对虾MP总体表现出羰基和总巯基含量、表面疏水性和粒径增加,而溶解度下降的趋势。表明虾MP在SV加工过程中发生了氧化变性,出现了解构、重组和聚集等结构上的变化,且在50 ℃-5 min条件下达到变性点。总巯基含量的增加和粒径的增大还说明二硫键在该过程中并非是引起MP聚集的主要作用。此外,SDS-PAGE中的肌球蛋白重链条带强度发生改变,FTIR和拉曼光谱表征的蛋白质二级结构中α-螺旋含量先减后增的趋势以及β-折叠含量增加的现象也进一步佐证了该结论。

关键词: 真空低温烹饪;南美白对虾;肌原纤维蛋白;结构特性

Abstract: This study aimed to investigate the effects of sous vide (SV) on the structure of myofibrillar protein (MP) in Penaeus vannamei. MP was subjected to SV cooking at different combinations of temperature (40, 50, 60, 70, and 80 ℃) and time (5, 10, and 15 min). Non-treated MP served as control. The samples were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and their solubility, surface hydrophobicity, carbonyl content, total sulfhydryl content, Fourier transform infrared spectroscopy (FTIR), and Raman spectra were evaluated. The results showed that with increasing processing temperature and time, the carbonyl and total sulfhydryl content, surface hydrophobicity, and particle size of MP increased, and the solubility decreased in general. This indicates that shrimp MP underwent oxidative denaturation during SV processing, with structural changes such as deconstruction, reorganization, and aggregation, and that the denaturation point was reached after 5 min at 50 ℃. The increase in total sulfhydryl contents and particle sizes together indicate that disulfide bonding was not the major cause of MP aggregation during the process. This conclusion was further supported by the altered intensity of myosin heavy chain bands in SDS-PAGE, as well as the initial increase and then decrease in α-helix content and the increase in β-sheet content as characterized by FTIR and Raman spectroscopy.

Key words: sous vide; Penaeus vannamei; myofibrillar protein; structural characteristics

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