食品科学 ›› 2021, Vol. 42 ›› Issue (8): 67-73.doi: 10.7506/spkx1002-6630-20191018-183

• 食品化学 • 上一篇    下一篇

芦丁诱导猪肉肌原纤维蛋白结构变化对蛋白凝胶特性的改善作用

贾娜,林世文,刘丹,刘登勇   

  1. (渤海大学食品科学与工程学院,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,辽宁省食品安全重点实验室,辽宁 锦州 121013)
  • 出版日期:2021-04-25 发布日期:2021-05-14
  • 基金资助:
    辽宁省重点研发计划项目(2017205003);辽宁省高等学校产业技术研究院重大应用研究项目(041804)

Improvement Effects of Structural Changes of Pork Myofibrillar Protein Induced by Rutin on Its Gel Properties

JIA Na, LIN Shiwen, LIU Dan, LIU Dengyong   

  1. (National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, Food Safety Key Lab of Liaoning Province, College of Food Science and Technology, Bohai University, Jinzhou 121013, China)
  • Online:2021-04-25 Published:2021-05-14

摘要: 向猪肉肌原纤维蛋白氧化体系(40?mg/mL蛋白、10?μmol/L?FeCl3、100?μmol/L?VC和1?mmol/L?H2O2)中添加不同量的芦丁(0、10、50、100、150?μmol/g,以蛋白计),测定蛋白质的巯基含量、表面疏水性、电泳、溶解度、凝胶强度和保水性、流变特性,研究芦丁对肌原纤维蛋白结构和凝胶特性的影响。结果表明,添加芦丁使肌原纤维蛋白的巯基含量显著下降(P<0.05),表面疏水性先下降后上升;芦丁使肌球蛋白重链(myosin heavy chain,MHC)强度减弱,肌动蛋白条带强度在其较高含量下(100?μmol/g和150?μmol/g)降低,添加β-巯基乙醇后,MHC和肌动蛋白条带大部分被还原;溶解度随着芦丁添加量的增加而降低;芦丁用量增加,蛋白的凝胶强度与保水性显著增强(P<0.05),凝胶最终形成阶段的储能模量(G’)提高。因此,芦丁可通过与肌原纤维蛋白的共价交联或适度增加蛋白的表面疏水性而改善蛋白的凝胶特性。

关键词: 芦丁;肌原纤维蛋白;结构;凝胶特性;交联

Abstract: Different concentrations of rutin (0, 10, 50, 100 and 150 μmol/g protein) was added to Fenton oxidation system containing pork myofibrillar protein (40 mg/mL protein, 10 μmol/L FeCl3, 100 μmol/L VC and 1 mmol/L H2O2). To study the effects of rutin on the structure and gel properties of myofibrillar protein, we determined the sulfhydryl content, surface hydrophobicity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) pattern, solubility, gel strength, water-holding capacity and rheological properties of the protein. The results showed that the addition of rutin significantly decreased the sulfhydryl content of myofibrillar protein (P < 0.05), and first decreased and then increased the surface hydrophobicity. Rutin addition reduced the intensity of myosin heavy chain (MHC). The intensity of actin band was decreased at higher concentrations of rutin (100 and 150 μmol/g). Most of the MHC and actin bands were restored after adding β-mercaptoethanol. The solubility was decreased with increasing rutin concentration, and the gel strength and water-holding capacity were increased significantly (P < 0.05). Similarly, the storage modulus (G’) in the final stage of gel formation was increased. Therefore, rutin can improve the gel properties of myofibrillar protein by covalent crosslinking with it or moderately increasing its surface hydrophobicity.

Key words: rutin; myofibrillar protein; structure; gel properties; crosslinking

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