食品科学 ›› 2021, Vol. 42 ›› Issue (9): 206-213.doi: 10.7506/spkx1002-6630-20200419-250

• 包装贮运 • 上一篇    下一篇

反复冻融过程中开背调味鱼品质及蛋白特性的变化

吴晨燕,杨梅,王珂莉,刘鑫洁,刘思佳,马俪珍   

  1. (1.天津农学院食品科学与生物工程学院,国家大宗淡水鱼加工技术研发分中心(天津),天津 300384;2.天津市强源食品有限公司,天津 301700)
  • 出版日期:2021-05-15 发布日期:2021-06-02
  • 基金资助:
    天津市水产品加工及质量安全校企协同创新实验室建设项目(17PTSYJC00140)

Changes in the Quality and Protein Properties of Seasoned Fish during Repeated Freeze-Thaw Cycles

WU Chenyan, YANG Mei, WANG Keli, LIU Xinjie, LIU Sijia, MA Lizhen   

  1. (1. National Research and Development Sub-center of Freshwater Fish Processing Technology (Tianjin), College of Food Science and Biological Engineering, Tianjin Agricultural University, Tianjin 300384, China; 2. Tianjin Qiangyuan Food Co. Ltd., Tianjin 301700, China)
  • Online:2021-05-15 Published:2021-06-02

摘要: 为研究反复冻融过程对超高压(ultra high pressure,UHP)和滚揉(tumbling,TB)两种腌制方式制得的开背调味鱼品质及蛋白特性的影响,分别通过UHP和TB腌制加工出两种开背调味鱼,将其先在-35 ℃速冻后再于-18 ℃冷库中冻藏,期间每隔20 d进行解冻-再冷冻的循环过程,分析鱼肉在5 次冻融循环过程中菌落总数、硫代巴比妥酸反应物(thiobarbituric acid reaction substances,TBARS)值、总挥发性盐基氮(total volatile basic nitrogen,TVB-N)含量、蛋白氧化相关指标(总巯基、二硫键含量)的变化;同时,通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析鱼肉的蛋白组成变化,并通过扫描电子显微镜、紫外分光光度计、傅里叶变换红外光谱仪对肌原纤维蛋白的结构进行分析。结果表明:随着冻融循环次数的增加,UHP和TB样品的菌落总数一直维持在较低水平,TVB-N含量、TBARS值呈逐渐上升趋势,但整体也维持在较低水平;肌原纤维蛋白总巯基含量显著降低(P<0.05),二硫键含量显著升高(P<0.05),蛋白二级结构α-螺旋和β-转角相对含量降低,β-折叠和无规卷曲相对含量增加,肌球蛋白重链、肌动蛋白电泳条带变淡变细,冻融循环过程中,样品表面逐渐出现明显的孔洞、褶皱,表面结构变粗糙。其中UHP样品的品质变化明显低于TB样品,说明UHP腌制方式可以延缓开背调味鱼在反复冻融过程的品质变化。

关键词: 反复冻融;调味鱼;鱼肉品质;蛋白特性;超高压;滚揉

Abstract: In order to explore the effects of repeated freeze-thaw cycles on the quality and protein properties of seasoned split fish prepared by ultra-high pressure (UHP) or tumbling (TB) marination, after being quickly frozen at ?35 ℃, the two fish samples were stored at ?18 ℃ for 20 days and then thawed and the freeze-thaw process was repeated five times consecutively. Changes in total bacterial count (TBC), thiobarbituric acid reaction substances (TBARS) value, total volatile basic nitrogen (TVB-N) content and protein oxidation indexes (sulfhydryl group and disulfide bond contents) were determined as well as in protein composition analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The microstructure, functional groups and secondary structure of myofibrillar proteins were evaluated by scanning electron microscopy (SEM), ultraviolet (UV) spectroscopy and Fourier transform infrared (FTIR) spectroscopy. The results showed that TBC in both samples remained at low levels, TVB-N content and TBARS value in both samples increased but also remained at low levels with increasing number of freeze-thaw cycles. Moreover, the sulfhydryl group content of myofibrillar proteins decreased significantly (P < 0.05), while the disulfide bond content increased significantly (P < 0.05); the relative contents of α-helix and β-turn decreased, whereas the relative contents of β-sheet and random coil increased. The electrophoretic bands of myosin heavy chain and actin became thinner and lighter. SEM observation revealed that the surface of the samples became wrinkled and rough with cavity after repeated freeze-thaw cycles. The quality change of UHP samples was significantly lower than that of TB samples, indicating that the UHP marination could delay the quality changes of seasoned split fish during repeated freeze-thaw process.

Key words: repeated freeze-thaw; seasoned fish; fish quality; protein characteristics; ultra-high pressure; tumbling

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