食品科学 ›› 2021, Vol. 42 ›› Issue (5): 46-54.doi: 10.7506/spkx1002-6630-20200924-292

• 基础研究 • 上一篇    下一篇

基于同位素标记相对和绝对定量技术研究藏香猪冷鲜肉冰温保鲜分子机制

杨飞艳,辜雪冬,孙术国,罗章,谢司伟,黄文阳   

  1. (1.中南林业科技大学食品科学与工程学院,湖南 长沙 410004;2.西藏农牧学院食品科学学院,西藏 林芝 860000)
  • 出版日期:2021-03-15 发布日期:2021-03-29
  • 基金资助:
    西藏中央支持地方高校发展专项(503118004);西藏自治区重点科研项目(XZ201901NA04); 长沙市食品贮藏保鲜工程技术研究中心项目(kq1901146)

Isobaric Tags for Relative and Absolute Quantitation (iTRAQ)-Based Quantitative Proteomics Analysis of the Molecular Mechanism by Which Superchilling Preserves the Quality of Chilled Tibetan Fragrant Pig Meat

YANG Feiyan, GU Xuedong, SUN Shuguo, LUO Zhang, XIE Siwei, HUANG Wenyang   

  1. (1. College of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China; 2. Food Science College, Tibet Agricultural and Animal Husbandry University, Nyingchi 860000, China)
  • Online:2021-03-15 Published:2021-03-29

摘要: 本研究基于同位素标记相对和绝对定量技术研究冰温-2 ℃和冷藏4 ℃条件下,藏香猪冷鲜肉蛋白质组变化及其与微生物指标(菌落总数)、理化品质(总挥发性盐基氮(total volatile base nitrogen,TVB-N)含量、弹性)、蛋白质二级结构(β-折叠和β-转角相对含量)变化的关系。结果表明:与4 ℃贮藏条件相比,-2 ℃贮藏条件下猪肉菌落总数、TVB-N含量、弹性以及蛋白质二级结构变化速率相对较低。蛋白质组学分析结果表明,在-2 ℃和4 ℃贮藏条件下,猪肉中共179 个蛋白发生了明显变化,其中,丰度显著差异蛋白143 个。-2 ℃下16 d/0 d和4 ℃下16 d/0 d相比较有丰度差异蛋白97 个,其中共有丰度差异蛋白61 个。这些差异蛋白主要涉及结构蛋白、代谢酶、应激蛋白和钙调节蛋白等。差异表达蛋白的表达量与菌落总数、理化品质(TVB-N含量、弹性)、蛋白质二级结构(β-折叠和β-转角相对含量)之间的相关性分析表明,肌球蛋白、原肌球蛋白、钙蛋白酶抑制蛋白表达量均与肉弹性、β-折叠相对含量呈极显著正相关(P<0.01),与菌落总数、TVB-N含量、β-转角相对含量呈显著或极显著负相关(P<0.05,P<0.01),相对于这3 类蛋白,热休克蛋白与肉理化品质、蛋白质二级结构呈现相反的相关关系。结论:冰温贮藏能有效抑制腐败微生物增殖和猪肉蛋白质降解,降低藏香猪冷鲜肉TVB-N含量和减少蛋白质二级结构变化,维持肉弹性,进而达到冷鲜肉贮藏保鲜效果。本研究为深入理解冰温保鲜的分子机制、合理设计冰温贮藏条件提供了参考。

关键词: 藏香猪肉;同位素标记相对和绝对定量;蛋白质组学;品质特征;相关性

Abstract: Changes in the proteomic profile of chilled Tibetan fragrant pig meat during superchilling (–2 ℃) and cold (4 ℃) storage were investigated by isobaric tags for relative and absolute quantitation (iTRAQ), and its relationship with changes in total aerobic count (TAC), physicochemical properties (total volatile base nitrogen (TVB-N) content and elasticity), and protein secondary structures (β-sheet and β-turn relative content) were evaluated. The results showed a slower rate of changes in TVB-N content, springiness, and the relative contents of β-sheet and β-turn in meat was found during storage for 16 days at –2 ℃ than at 4 ℃. Proteomic analysis showed that a total of 179 differentially expressed proteins were identified between meats stored at the two temperatures. Among these proteins, 143 were found to significantly differ in abundance. In total, 97 proteins with differential abundance were found between meats stored at the two temperatures for 0 and 16 days, 61 out of which were found to be shared. The differentially expressed proteins mainly included structural proteins, metabolic enzymes, stress proteins and calmodulins. The correlation analysis indicated that myosin, tropomyosin and calpastatin expression level were significantly negatively correlated with TAC, TVB-N content and β-turn relative content (P < 0.05 or P < 0.01), and significantly positively correlated with springiness and β-sheet relative content (P < 0.01), while heat shock protein expression level had opposite correlations with the physicochemical properties and protein secondary structures. Therefore, we conclude that superchilling can effectively inhibit the growth of spoilage microorganisms and protein catabolism in pig meat, reduce the changes in TVB-N and protein secondary structure, and maintain elasticity, thereby preserving meat quality. This study provides a reference for in-depth understanding of the molecular mechanism for quality preservation in pig meat by superchilling and exploring reasonable storage conditions.

Key words: Tibetan fragrant pig meat; isobaric tags for relative and absolute quantitation; proteomics; quality characteristics; correlation

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