食品科学 ›› 2019, Vol. 40 ›› Issue (20): 21-27.doi: 10.7506/spkx1002-6630-20181105-059

• 食品化学 • 上一篇    下一篇

氧化强度对肌原纤维蛋白结构及凝胶性能的影响

曹云刚,马文慧,艾娜丝,闫林林,赵倩倩,闵红卫,白雪,黄峻榕   

  1. (1.陕西科技大学食品与生物工程学院,陕西 西安 710021;2.北京工商大学 北京食品营养与人类健康高精尖创新中心,北京市食品添加剂工程技术研究中心,北京 100048;3.中国林业科学研究院林产化学工业研究所,江苏 南京 210042)
  • 出版日期:2019-10-25 发布日期:2019-10-25
  • 基金资助:
    国家自然科学基金青年科学基金项目(31801480;31501502);陕西省科技厅自然科学基础研究计划项目(2019JQ-397); 北京市食品添加剂工程技术研究中心开放课题(210170094)

CAO Yungang, MA Wenhui, AI Nasi, YAN Linlin, ZHAO Qianqian, MIN Hongwei, BAI Xue, HUANG Junrong

CAO Yungang, MA Wenhui, AI Nasi, YAN Linlin, ZHAO Qianqian, MIN Hongwei, BAI Xue, HUANG Junrong   

  1. (1. School of Food and Biological Engineering, Shaanxi University of Science & Technology, Xi’an 710021, China;2. Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University, Beijing 100048, China;3. Institute of Chemical Industry of Forest Products,?Chinese Academy of Forestry, Nanjing 210042, China)
  • Online:2019-10-25 Published:2019-10-25

摘要: 采用模拟氧化体系(10 μmol/L FeCl3,100 μmol/L抗坏血酸,0、0.5、1、3、5、10 mmol/L H2O2),研究不同氧化程度对猪肌原纤维蛋白(myofibrillar protein,MP)结构及凝胶性质的影响。结果表明:随H2O2浓度升高,蛋白羰基含量上升,总巯基含量、自由氨基含量及内源荧光强度下降,十二烷基硫酸钠-聚丙烯酰胺凝胶电泳表明氧化诱导二硫键的形成引起蛋白质交联聚集加剧,进而导致蛋白表面疏水性和溶解度降低;当H2O2浓度小于1.0 mmol/L时,MP热诱导凝胶性能无明显变化,当H2O2浓度大于1.0 mmol/L时,热诱导凝胶蒸煮损失显著增强(P<0.05),凝胶强度明显降低(P<0.05),但凝胶白度无明显变化。总体来说,H2O2浓度越高蛋白氧化程度越严重,凝胶强度越低。

关键词: 氧化, 肌原纤维蛋白, 结构变化, 十二烷基硫酸钠-聚丙烯酰胺凝胶电泳, 凝胶性能

Abstract: In this research, porcine myofibrillar protein (MP) was artificially oxidized in simulated oxidation systems (containing 10 μmol/L FeCl3, 100 μmol/L ascorbic acid, and 0, 0.5, 1, 3, 5 or 10 mmol/L H2O2) with a view to investigating the effects of different oxidation degrees on the structural characteristics and gel properties of myofibrillar protein. The results showed that the protein carbonyl content increased, while the contents of sulfhydryl groups and free amino groups and the endogenous fluorescence intensity decreased with the increase of H2O2 concentration. SDS-PAGE indicated that oxidative disulfide bond formation resulted in protein cross-linking and aggregation, and consequently a decrease of protein surface hydrophobicity and solubility. When the concentration of H2O2 was lower than 1.0 mmol/L, no significant change was observed in the heat-induced gel properties of MP. However, when the H2O2 concentration was higher than 1.0 mmol/L, the cooking loss increased significantly (P < 0.05) and the gel strength decreased obviously (P < 0.05), while the whiteness changed barely. Overall, H2O2 concentration was positively correlated with protein oxidation degree, but negatively correlated with gel strength.

Key words: oxidation, myofibrillar protein, protein structure change, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel properties

中图分类号: