The Food Safety Key Laboratory of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou, 310018, P.R. China.
The National Center of Meat Quality and Safety Control, Synergetic Innovation Center of Food Safety and Nutrition, College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, P.R. China.
J Food Sci. 2021 Jan;86(1):68-77. doi: 10.1111/1750-3841.15556. Epub 2020 Dec 17.
Currently, there has been a surge of interest in revealing the interactions between plasma and food matrices. In this study, we investigated the impacts of atmospheric cold plasma (ACP) treatment on the structural, physicochemical and allergenic characteristics of soybean protein isolate (SPI). SPI dispersions were subjected to ACP treatments at different frequencies (80 to 100 Hz) and durations (1 to 10 min) to investigate the effects of exposing conditions. Results showed that ACP induced reactive oxygen species-mediated oxidation of soy proteins, resulting in modifications in the secondary and ternary structures of SPI. As a consequence, functional properties of SPI, such as emulsifying (56 to 168%, compared with control) and foaming properties (60 to 194%) were influenced by varying degrees. In addition, under certain circumstance (120 Hz, 5 min), the IgE-binding level of SPI was decreased by up to 75%, when compared to the control. Moderate treatment yielded products with improved functionality and reduced allergenicity, while extensive exposure induced a loss of vendibility due to protein aggregation. PRACTICAL APPLICATION: In this study, we demonstrated for the first time, that plasma species reacted with soybean proteins, resulting in spatial structural changes which are closely related with protein functionality and allergenicity. ACP interacts with macromolecules in aqueous systems and thus can be an alternative and promising nonthermal approach in modifying soybean proteins, whereas the exact role of different processing parameters needs to be well-elaborated.
目前，人们对揭示等离子体与食物基质之间的相互作用产生了浓厚的兴趣。在本研究中，我们研究了大气压冷等离子体（ACP）处理对大豆分离蛋白（SPI）结构、物理化学和变应原特性的影响。SPI 分散体在不同频率（80 至 100 Hz）和时间（1 至 10 分钟）下进行 ACP 处理，以研究暴露条件的影响。结果表明，ACP 诱导活性氧介导的大豆蛋白氧化，导致 SPI 二级和三级结构的修饰。因此，SPI 的功能特性，如乳化（与对照相比，增加 56%至 168%）和起泡特性（增加 60%至 194%）受到不同程度的影响。此外，在某些情况下（120 Hz，5 分钟），与对照相比，SPI 的 IgE 结合水平降低了 75%。适度处理可产生功能改善和变应原性降低的产品，而广泛暴露会因蛋白质聚集而导致产品失去销售价值。实际应用：在这项研究中，我们首次证明了等离子体与大豆蛋白相互作用，导致空间结构发生变化，这与蛋白质功能和变应原性密切相关。ACP 与水系统中的大分子相互作用，因此可以作为一种替代的、有前途的非热方法来修饰大豆蛋白，而不同处理参数的确切作用需要进一步阐明。
