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中国精品科技期刊2020
黄馨禾,王长艳,范龙彬,等. 燕麦蛋白耦合异源共架技术对大米蛋白水溶性的影响[J]. 食品工业科技,2024,45(7):134−141. doi: 10.13386/j.issn1002-0306.2023100090.
引用本文: 黄馨禾,王长艳,范龙彬,等. 燕麦蛋白耦合异源共架技术对大米蛋白水溶性的影响[J]. 食品工业科技,2024,45(7):134−141. doi: 10.13386/j.issn1002-0306.2023100090.
HUANG Xinhe, WANG Changyan, FAN Longbin, et al. Effect of Oat Protein-coupled Co-assemble Hybridization Technology on Water Solubility of Rice Protein[J]. Science and Technology of Food Industry, 2024, 45(7): 134−141. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023100090.
Citation: HUANG Xinhe, WANG Changyan, FAN Longbin, et al. Effect of Oat Protein-coupled Co-assemble Hybridization Technology on Water Solubility of Rice Protein[J]. Science and Technology of Food Industry, 2024, 45(7): 134−141. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023100090.

燕麦蛋白耦合异源共架技术对大米蛋白水溶性的影响

Effect of Oat Protein-coupled Co-assemble Hybridization Technology on Water Solubility of Rice Protein

  • 摘要: 为了通过燕麦蛋白耦合异源共架技术提升大米蛋白在水中的溶解特性,本研究以不同比例的大米蛋白和燕麦蛋白为原料,将两种蛋白在pH12的环境下混合,再恢复至中性进行共架。测定蛋白的溶解性并通过分析十二烷基磺酸钠-聚丙烯酰胺凝胶电泳、粒径、微观形态、乳化特性、起泡特性、傅里叶红外光谱等探究其作用机理。结果显示,大米-燕麦蛋白的溶解度显著高于大米蛋白(8.49%±1.53%)(P<0.05),两者比例为1:0.6时达到最大值93.07%±2.15%。经过异源共架处理的大米-燕麦蛋白复合物粒径为0.1 μm左右,同时结构更加松散,大米蛋白和燕麦蛋白之间的疏水相互作用和氢键也发生了变化,使得大米蛋白的溶解度增加,进一步提升乳化特性和起泡特性。综上,燕麦蛋白耦合异源共架技术是一种可以解决大米蛋白水溶性差的可靠手段。

     

    Abstract: In order to improve the solubility of rice protein in aqueous solutions by using oat protein-coupled co-assemble hybridization technology, in this study, different ratios of rice protein and oat protein were used as raw materials, and the two proteins were mixed at pH12, and then restored to neutrality for the co-assemble hybridization. The solubility of the protein was determined and the mechanism of action was explored by analyzing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, particle size, microscopic morphology, emulsification characteristics, foaming characteristics, and Fourier transform infrared spectrometer. The results indicated that the solubility of rice protein-oat protein was higher than that of rice protein (8.49%±1.53%), and the highest solubility 93.07%±2.15% was achieved at the ratio of 1:0.6 (rice protein/oat protein). The particle size of the rice protein-oat protein after co-assemble hybridization was about 0.1 μm, while the structure became looser and hydrophobic interaction and hydrogen bond between rice protein and oat protein were changed, which increased the solubility of rice protein and further improved the emulsification and foaming characteristics. In conclusion, the oat protein-coupled co-assemble hybridization technology is a robust method that can solve the poor water solubility of rice protein.

     

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