食品科学 ›› 2021, Vol. 42 ›› Issue (5): 68-76.doi: 10.7506/spkx1002-6630-20200221-226

• 食品工程 • 上一篇    下一篇

超声辅助解冻对秘鲁鱿鱼胴体蛋白氧化与品质的影响

朱文慧,宦海珍,李月,步营,李学鹏,励建荣   

  1. (渤海大学食品科学与工程学院,生鲜农产品贮藏加工及安全控制技术国家地方联合工程研究中心,辽宁 锦州 121013)
  • 出版日期:2021-03-15 发布日期:2021-03-29
  • 基金资助:
    国家自然科学基金青年科学基金项目(31901763);辽宁省“兴辽英才计划”项目(XLYC1807133)

Effect of Ultrasound-Assisted Thawing on Protein Oxidation and Quality of Frozen Jumbo Squid (Dosidicus gigas)

ZHU Wenhui, HUAN Haizhen, LI Yue, BU Ying, LI Xuepeng, LI Jianrong   

  1. (National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Products, College of Food Science and Engineering, Bohai University, Jinzhou 121013, China)
  • Online:2021-03-15 Published:2021-03-29

摘要: 本研究旨在探讨超声辅助解冻过程中蛋白质氧化、肌肉结构变化与秘鲁鱿鱼胴体品质的关系。采用不同梯度的超声功率(100、300、500 W),在不同温度(5、10 ℃)下对秘鲁鱿鱼胴体进行超声辅助解冻处理。经U5-5(5 ℃、500 W)超声解冻处理的鱿鱼解冻和蒸煮质量损失最少,低场核磁共振实验结果也显示,U5-5超声解冻处理可以降低汁液流失。7 种不同解冻方式的鱿鱼羰基含量、总巯基含量、二聚酪氨酸含量和表面疏水性差异显著(P<0.05)。U5-3(5 ℃、300 W)、U5-5超声解冻处理对肌原纤维蛋白羰基含量影响小,U5-3超声解冻组的总巯基含量最高,二聚酪氨酸含量最低,冷藏解冻和U5-1(5 ℃、100 W)超声解冻组蛋白质表面疏水基团暴露最少。拉曼光谱分析结果表明,超声辅助解冻可以延缓α-螺旋向β-折叠、β-转角和无规卷曲结构转化。综上,5 ℃超声辅助解冻(U5-3、U5-5)可以改善秘鲁鱿鱼产品品质,延缓蛋白氧化。

关键词: 超声辅助解冻;秘鲁鱿鱼;蛋白氧化;品质;结构变化

Abstract: The objective of the present study was to explore the relationship of protein oxidation, muscle structural changes and jumbo squid mantle quality during ultrasound-assisted thawing. Frozen jumbo squid mantles were thawed by ultrasonic treatment using different power gradients (100, 300, and 500 W) at different temperatures (5 and 10 ℃). The U5-5 treatment (5 ℃, 500 W) caused the smallest thawing and cooking loss. Low-field nuclear magnetic resonance (LF-NMR) suggested that U5-5 could reduce juice loss. The seven different thawing methods showed significant differences in carbonyl content, total sulfhydryl content, dityrosine content and surface hydrophobicity (P < 0.05). U5-3 (5 ℃, 300 W) and U5-5 had little effect on the carbonyl content of myofibrillar protein. U5-3 caused the highest total sulfhydryl content and the smallest dityrosine content, while refrigerator thawing and U5-1 (5 ℃, 100 W) caused the least exposure of hydrophobic groups on the protein surface. Raman spectroscopy showed that ultrasonic-assisted thawing could retard the conversion of α-helices to β-sheets, β-turns and random coils. These results demonstrate that ultrasonic-assisted thawing at 5 ℃ (U5-3 and U5-5) can improve product quality and defer protein oxidation.

Key words: ultrasonic-assisted thawing; jumbo squid; protein oxidation; quality; structural transformation

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