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中文摘要：
为探究奥尼罗非鱼片在冰藏期间组织蛋白酶活性与质构及肌原纤维蛋白降解的相关性,实验测定了冰藏期间的组织蛋白酶B、H、L、D的活性、鱼片质构和肌原纤维蛋白随冰藏时间的变化趋势及其相关性。结果显示,组织蛋白酶B、D的活性整体呈波动式上升趋势,组织蛋白酶L、B＋L活性均呈先下降后上升的变化趋势,组织蛋白酶B、B＋L的活性与冰藏时间呈显著正相关。组织蛋白酶H的活性在贮藏期间变化较小。肌原纤维蛋白含量在冰藏第2天最高,整体变化趋势与冰藏时间呈显著负相关;SDS-PAGE图谱表明肌球蛋白重链发生了显著的降解,肌动蛋白和原肌球蛋白变化不显著,α-辅肌动蛋白在冰藏前4 d逐渐降解;质构指标硬度、胶黏性、咀嚼性3者整体均呈波动变化趋势,凝聚性和弹性在整个冰藏期间变化不显著,黏附性和黏附力在冰藏2 d后逐渐上升。组织蛋白酶活性与质构和肌原纤维蛋白含量的相关性分析表明,组织蛋白酶B活性与弹性和肌原纤维蛋白含量显著相关,组织蛋白酶L、D与硬度、胶黏性和咀嚼性呈显著相关性,组织蛋白酶L和D是最有可能直接参与宰后冰藏期间奥尼罗非鱼片肌肉软化的组织蛋白酶。溶酶体组织蛋白酶可能共同参与鱼肉的自溶。
英文摘要：
To inquire the correlation of cathepsins activities and texture and myofibrillar protein degradation of tilapia fillets during iced storage,the changes of cathepsins B,H,L and D activities over a period of iced storage were measured. And these variation trends of texture of fillets as well as myofibrillar protein with iced time and correlation among them were also determined. The results showed that cathepsins B and D activities presented a fluctuatingly upgraded tendency on the whole, and cathepsins L, sum of B and L activities presented a first descending and then upgraded tendency. A highly significant positive correlation was observed between cathepsins B and sum of B and L activities and iced storage period. Through the duration of storage,changing scale of cathepsin H activity was small. Myofibrillar protein had a maximum content on the iced 2nd day,and its overall variation trend showed a significant negative correlation with iced time. The SDS-PAGE pattern showed that myosin heavy chain degraded obviously, while actin and tropomyosin had no remarkable changes, and a-actinin degraded gradually in the first iced four days. Texture indices including hardness, gumminess and chewiness on the whole presented a fluctuating tendency, and cohesiveness as well as springiness did not change remarkably through the iced storage, whereas adhesiveness and adhesive force increased gradually two days after iced storage. The correlation analysis of cathepsins activities and texture as well as myofibrillar protein content indicated that cathepsin B activity was largely related to springiness and myofibrillar protein content, and cathepsins L and D presented a significant correlation with hardness,gumminess and chewiness. Cathepsins L and D were the most likely to be directly involved in the postmortem softening of tilapia fillets muscle during iced storage. Lysosomal cathepsins may have participated jointly in autolysis of fish.
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