Relationship between the Structure and Solubility of Nano-Soybean Peptides Revealed by Infrared Spectroscopy and Atomic Force Microscopy
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摘要: 以大豆分离蛋白为原料进行胃蛋酶水解,得到大豆肽。通过红外光谱、原子力显微镜对大豆蛋白和大豆肽的二级结构及微观结构进行分析,揭示结构与溶解性之间的关系。结果表明,与大豆分离蛋白相比,大豆肽二级结构主要以无规则卷曲为主,其α-螺旋和β-折叠结构含量低16.38%,而无序结构的β-转角和无规则卷曲含量高15.37%。大豆肽表面较平滑颗粒较分散,以单个分子状态存在,粒径为大豆分离蛋白的50%,在pH为4.0时,其溶解性为大豆分离蛋白的4.43倍。Abstract: Using the soy protein isolate after hydrolysis by pepsin as the substrate to obtain soybean peptides,the effects of secondary structure of soybean protein isolate and soybean peptide on the solubility of soy protein isolate were studied. The structure and microstructure of the two classes were analyzed by infrared spectroscopy and atomic force microscopy. The relationship between structure and function was analyzed by the functional analysis of the changes. The results showed that a-helix and β-sheet of the secondary structure of soybean peptide was 16.38% lower than that of soybean protein isolate,while the β-turn and random coil is about 15.37% higher than one. The surface of soybean peptide was smooth and the particle was dispersed,existing in single molecule state. The particle size was 50% of soybean protein isolate,and the solubility of soybean protein was 4.43 times of that of soybean protein isolate at pH4.0.
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期刊类型引用(4)
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4. 林展拓，高志明，杜徐楠，陈改亭，胡猛，方亚鹏，汤虎. 热聚集对β-乳球蛋白消化行为及消化产物的抗氧化性的影响. 食品科学. 2019(23): 52-59 . 百度学术
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