食品科学 ›› 2023, Vol. 44 ›› Issue (1): 239-245.doi: 10.7506/spkx1002-6630-20211210-126

• 包装贮运 • 上一篇    下一篇

鲈鱼在4 ℃冷藏过程中的肌肉品质变化

杨汝晴,陈玉磊,孙乐常,张凌晶,刘光明,曹敏杰   

  1. (1.集美大学海洋食品与生物工程学院,福建 厦门 361021;2.大连工业大学海洋食品深加工协同创新中心,辽宁 大连 116034)
  • 出版日期:2023-01-15 发布日期:2023-01-31
  • 基金资助:
    国家重点研发计划项目(2018YFD0901004);国家自然科学基金面上项目(31772049)

Quality Change of Sea Bass (Lateolabrax japonicas) Muscle during Cold Storage at 4 ℃

YANG Ruqing, CHEN Yulei, SUN Lechang, ZHANG Lingjing, LIU Guangming, CAO Minjie   

  1. (1. College of Food and Biological Engineering, Jimei University, Xiamen 361021, China;2. Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China)
  • Online:2023-01-15 Published:2023-01-31

摘要: 目的:探究4 ℃冷藏过程中鲈鱼肌肉品质的变化。方法:测定4 ℃冷藏过程中鲈鱼肌肉pH值、菌落总数、总挥发性盐基氮(total volatile base nitrogen,TVB-N)含量、K值和质构等指标,综合评价鲈鱼生理生化品质的变化,采用Masson染色和免疫组化分析评价组织形态学变化,利用酶解荧光肽底物测定特异性酶解胶原蛋白的基质金属蛋白酶(matrix metalloproteinases,MMPs)活力变化。结果:鲈鱼在贮藏期间pH值呈先下降后升高趋势,菌落总数、TVB-N含量和K值随贮藏时间的延长而增加,并在第8天超过临界值。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析结果显示,贮藏至6 d鲈鱼肌肉蛋白组成没有明显变化,而在第8天肌球蛋白重链降解明显。Masson染色和I型胶原免疫组化分析结果显示,随贮藏时间的延长,肌内膜逐渐被降解,至第12天,肌膜I型胶原蛋白和肌纤维之间出现明显间隙。MMPs活力随贮藏时间的延长而明显增加,而鱼肉硬度不断下降。结论:鱼类冷藏期间肌肉的软化与胶原蛋白分解密切相关,而MMPs对I型胶原蛋白的降解可能是鱼死后肌肉软化的主要原因。

关键词: 鲈鱼;基质金属蛋白酶;质构;Masson染色;免疫组化

Abstract: This study was conducted in order to explore the changes in muscle quality of sea bass during cold storage. The physiological and biochemical changes of fish meat during storage at 4 ℃ were evaluated in terms of its pH, total bacterial count, total volatile basic nitrogen (TVB-N) content, K value and texture. Morphological changes of muscle were evaluated by Masson staining and immuno-histochemical staining. The enzymatic activity of matrix metalloproteinases (MMPs) was determined by hydrolyzing fluorescent peptide substrates. The results showed that the pH of sea bass muscle decreased firstly and then increased during cold storage. The total bacterial count, TVB-N content and K value increased with storage time, and exceeded the threshold on the 8th day. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that there was little change in the protein composition in sea bass muscle after 6 days of storage, while the myosin heavy chain was significantly degraded on the 8th day. Masson staining and immuno-histochemical staining of type I collagen showed that the endomysium was gradually degraded during storage. On the 12th day, an evident gap between type I collagen and muscle fibers was observed. The activity of MMPs increased significantly with storage time while the hardness of fish muscle decreased gradually. Hence, the softening of fish muscle during cold storage is closely related to collagen decomposition, and type I collagen degradation by MMPs may be the major reason for muscle softening after fish death.

Key words: sea bass; matrix metalloproteinase; texture; Masson staining; immuno-histochemical

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