微酸性电解水协同超声波杀菌对金枪鱼肌动蛋白结构及组织蛋白酶活性的影响  

Effects of Slightly Acidic Electrolyzed Water Combined with Ultrasonic Sterilization on Actin Structure and Cathepsin Activity of Tuna Meat

作　　者：孙协军 刘孝芳 李秀霞 王珍 励建荣 SUN Xiejun;LIU Xiaofang;LI Xiuxia;WANG Zhen;LI Jianrong(College of Food Science and Technology,Bohai University;National&Local Joint Engineering Research Center of Storage,Processing of Fresh Agricultural Products and Safety Control Technology;Liaoning Weiheng Testing Technology Co.,LTD,Jinzhou 121013,China)

机构地区：[1]渤海大学食品科学与工程学院 [2]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 [3]辽宁卫衡检测科技有限公司,辽宁锦州121013

出　　处：《广东海洋大学学报》2025年第1期77-85,共9页Journal of Guangdong Ocean University

基　　金：国家重点研发计划(2019YFD0901702);渤海大学海洋研究院开放课题(BDHYYJY2023001)。

摘　　要：【目的】分析微酸性电解水协同超声波杀菌对0℃冷藏大眼金枪鱼(Thunnus obesus)肌动蛋白结构和组织蛋白酶活性的影响,并进一步探究组织蛋白酶B对鱼肉肌动蛋白的降解机制。【方法】以未经处理的金枪鱼为对照组,用55.0 mg/mL微酸性电解水协同280 W超声波对金枪鱼进行杀菌处理5 min后,采用差示扫描量热法、傅里叶变换红外光谱、内源荧光光谱对金枪鱼肉肌动蛋白组成进行分析,结合组织蛋白酶B、L、D活性与分子对接技术,研究金枪鱼肉经协同杀菌处理后,0℃冷藏期间鱼肉的肌蛋白结构及相关组织蛋白酶活性变化。【结果】处理组变性焓值降低速度低于对照组,对照组α-螺旋相对占比降低69.09%,而处理组只降低41.33%。处理组色氨酸残基的稳定性更高。对照组肌动蛋白电泳条带更浅。分子对接结果表明,肌动蛋白-组织蛋白酶B结合时极性溶剂化能达-2179.70 kJ/mol,两者间氢键出现频率较高。【结论】55.0 mg/mL微酸性电解水和280 W超声波协同杀菌处理5 min处理后,金枪鱼肌动蛋白热稳定性更高,肌动蛋白的二级与三级结构得到较好保持。组织蛋白酶B在鱼肉肌动蛋白降解中发挥关键作用,肌动蛋白与组织蛋白酶B结合驱动力为极性溶剂化能,氢键在两者结合中起主导作用。本实验结果为微酸性电解水协同超声波杀菌在金枪鱼贮藏保鲜中的应用提供了理论参考。【Objective】To study the effect of slightly acidic electrolyzed water and ultrasonic sterilization on the actin structure and cathepsin activity of Thunnus obesus during storage at 0℃,and further expolore the effect of cathepsin B on its actin degradation.【Methods】Untreated tuna was used as control,the tuna was sterilized with 55 mg/mL slightly acidic electrolytic water and 280 W ultrasonic treatment for 5 min.The changes of actin structure and related cathepsin activity of the refrigerated fish meat were analyzed by Differential Scanning Calorimetry(DSC),Fourier Transform Infrared Spectroscopy(FTIR),and endogenous fluorescence spectroscopy.Combined with the activities of cathepsins B,L,and D and molecular docking techniques,the changes in myosin structure and related cathepsin activities in tuna meat during storage at 0℃after sterilization were investigated.【Results】The electrophoretic bands of actin in control group were shallower,the decrease rate of enthalpy of denaturation in the treatment group was lower than that in the control group,α-helix decreased by 69.09%in the control group and 41.33%in the experimental group.The stability of tryptophan residues in the treatment group was higher.Molecular docking showed that the polar solvation energy of actin-cathepsin B could reach-2179.70 kJ/mol,and the hydrogen bond between the two was more frequent.【Conclusion】Actin in the treatment group has better thermal stability and can better protect the secondary and tertiary structure of actin.Cathepsin B plays a key role in the degradation of actin in fish.The driving force of the binding of actin and cathepsin B is polar solvation energy,and hydrogen bond plays a major role in the binding of both.The study can provide a theoretical reference for the application of weakly acidic electrolytic water in tuna storage and fresh keeping.

关 键 词：金枪鱼 肌动蛋白结构 微酸性电解水 超声波 肌动蛋白降解 组织蛋白酶 

分 类 号：TS254.4[轻工技术与工程—水产品加工及贮藏工程]