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中國精品科技期刊2020
黃馨禾,王長艷,范龍彬,等. 燕麥蛋白耦合異源共架技術對大米蛋白水溶性的影響[J]. 食品工業科技,2024,45(7):134?141. doi: 10.13386/j.issn1002-0306.2023100090.
引用本文: 黃馨禾,王長艷,范龍彬,等. 燕麥蛋白耦合異源共架技術對大米蛋白水溶性的影響[J]. 食品工業科技,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.

燕麥蛋白耦合異源共架技術對大米蛋白水溶性的影響

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

  • 摘要: 為了通過燕麥蛋白耦合異源共架技術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麥蛋白為原料,將兩種蛋白在pH12的環境下混合,再恢復至中性進行共架。測定蛋白的溶解性并通過分析十二烷基磺酸鈉-聚丙烯酰胺凝膠電泳、粒徑、微觀形態、乳化特性、起泡特性、傅里葉紅外光譜等探究其作用機理。結果顯示,大米-燕麥蛋白的溶解度顯著高于大米蛋白(8.49%±1.53%)(P<0.05),兩者比例為1:0.6時達到最大值93.07%±2.15%。經過異源共架處理的大米-燕麥蛋白復合物粒徑為0.1 μm左右,同時結構更加松散,大米蛋白和燕麥蛋白之間的疏水相互作用和氫鍵也發生了變化,使得大米蛋白的溶解度增加,進一步提升乳化特性和起泡特性。綜上,燕麥蛋白耦合異源共架技術是一種可以解決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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