食品科学 ›› 2018, Vol. 39 ›› Issue (7): 215-220.doi: 10.7506/spkx1002-6630-201807032

• 包装贮运 • 上一篇    下一篇

货架期冷藏过程中鳝鱼肉理化指标及蛋白质变化规律

郑 红1,苏现波2,马 良1,3,张晓洁1,马明思1,孙 艺1,张宇昊1,3,*   

  1. 1.西南大学食品科学学院,重庆 400715;2.邯郸学院生命科学与工程学院,河北 邯郸 056005;3.西南大学 食品科学与工程国家级实验教学示范中心,重庆 400715
  • 出版日期:2018-04-15 发布日期:2018-04-17
  • 基金资助:
    “十三五”国家重点研发计划重点专项(2016YFD0400200);国家自然科学基金面上项目(31671881);中国博士后科学基金特别资助项目(2015T80951);重庆市基础科学与前沿技术研究重点项目(cstc2015jcyjBX0116);第四批重庆市高等学校优秀人才支持计划项目

Changes in Physicochemical Properties and Proteins during Shelf Life of Cold Stored Swamp Eel (Monopterus albus)

ZHENG Hong1, SU Xianbo2, MA Liang1,3, ZHANG Xiaojie1, MA Mingsi1, SUN Yi1, ZHANG Yuhao1,3,*   

  1. 1. College of Food Science, Southwest University, Chongqing 400715, China; 2. School of Life Science and Engineering, Handan College, Handan 056005, China; 3. National Demonstration Center for Food Science and Engineering Education, Southwest University, Chongqing 400715, China
  • Online:2018-04-15 Published:2018-04-17

摘要: 本研究目的是探讨鳝鱼货架期冷藏过程中品质变化规律及原因。首先测定了鳝鱼肌肉的挥发性盐基氮(total volatile basic nitrogen,TVB-N)含量、K值和硫代巴比妥酸反应产物(thiobarbituric acid reactive substances,TBARS) 值等指标,明确在冷藏条件下货架期为4 d。冷藏货架期内鳝鱼肉的pH值、色泽和持水率等理化指标测定结果显 示,随着贮藏时间的延长,pH值呈先下降后上升的趋势,肉色由鲜红变为褐红色,持水力逐渐下降。三氯乙酸- 可溶性氮含量和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis, SDS-PAGE)的结果表明,货架期内随着冷藏时间的延长,肌球蛋白和肌动蛋白质逐渐发生降解。价键分析表明, 冷藏货架期内离子键和氢键总体呈下降趋势,二硫键和疏水作用含量呈现逐渐增加的趋势。红外光谱分析表明,冷 藏货架期内,酰胺A带吸收峰总体向高波数移动,这与氢键变化趋势一致。酰胺I带曲线拟合结果表明,冷藏前期 主要是β-组分间的相互转化,后期则由β-组分向α-螺旋和无规卷曲转化,蛋白无序程度增加。结合红外光谱和价键 分析表明氢键和离子键可能是冷藏初期维系鳝鱼蛋白二级结构的主要作用力,二者的破坏导致蛋白构象改变。

关键词: 鳝鱼, 冷藏, 货架期, 理化性质, 蛋白质

Abstract: The purpose of this study was to investigate the quality changes of cold stored Monopterus albus during shelf life. The results showed that the shelf life of Monopterus albus was 4 days during cold storage as determined by measuring total volatile basic nitrogen (TVB-N) content, K value (freshness index) and thiobarbituric acid reactive substances (TBARS). pH decreased firstly and then increased with storage time, color turned from bright red to brown red, and water-holding capacity decreased continuously. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and trichloroacetic acid (TCA)-soluble nitrogen measurement showed that myosin and actin were degraded gradually during storage. Chemical analysis indicated that ionic bonds and hydrogen bonds decreased, whereas disulfide bonds and hydrophobic interactions showed a gradually increasing trend. Fourier transform infrared spectroscopy analysis indicated that amide A band moved to high wavenumber, which was consistent with the changes of hydrogen bonds. Curve fitting of amide ? band indicated that interconversion between β-sheet and β-turn was dominant during the early storage period, and then the protein structural components were transformed to α-helix and random coil, indicating increased structural disorderliness. Overall, these results showed that hydrogen bonds and ionic bonds may be the major forces to maintain the secondary structure of protein during the early storage period. The destruction of hydrogen bonds and ionic bonds can cause changes in protein conformation.

Key words: Monopterus albus, cold storage, shelf life, physicochemical properties, protein

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