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膜形成性能和大豆蛋白的机制:从β-伴球蛋白和大豆球蛋白得到的启示。

Film-forming properties and mechanisms of soy protein: Insights from β-conglycinin and glycinin.

机构信息

College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China.

College of Food Science and Engineering, Northwest A&F University, Yangling 712100, China.

出版信息

Int J Biol Macromol. 2023 Dec 31;253(Pt 8):127611. doi: 10.1016/j.ijbiomac.2023.127611. Epub 2023 Oct 23.

DOI:10.1016/j.ijbiomac.2023.127611
PMID:37879573
Abstract

Extensive research has been conducted on soy protein films; however, limited information is available regarding the influence of the major components, β-conglycinin (7S) and glycinin (11S), on the film-forming properties of soy protein. This study aimed to isolate the 7S and 11S fractions in order to prepare films and investigate the impact of varying 7S/11S ratios on the film-forming solutions (FFS) and film properties. The findings revealed that higher 11S ratios led to increased protein aggregation, consequently elevating the storage modulus (G') of the FFS. Notably, an optimal 7S/11S ratio of 7S1:11S2 (CF3) significantly enhanced the film's water resistance. Specifically, it enhanced the water contact angle by an impressive 17.44 % and reduced the water vapor transmission rate by 27.56 %. These improvements were attributed to intermolecular interactions, involving hydrogen bonds and salt bridges, between the amino acid residues of 7S and 11S. As a result, a more uniform and dense microstructure was achieved. Interestingly, the mechanical and optical properties of the film were maintained by the different protein fractions examined. In summary, this study contributes to the understanding of the film-forming properties of soy protein, particularly the role of 7S and 11S.

摘要

已经对大豆蛋白膜进行了广泛的研究;然而,关于主要成分β-伴球蛋白(7S)和大豆球蛋白(11S)对大豆蛋白成膜性能的影响,信息有限。本研究旨在分离 7S 和 11S 级分,以便制备薄膜并研究不同 7S/11S 比例对成膜溶液(FFS)和薄膜性能的影响。研究结果表明,较高的 11S 比例导致蛋白质聚集增加,从而提高 FFS 的储能模量(G')。值得注意的是,7S/11S 比例为 7S1:11S2(CF3)时,可显著提高薄膜的耐水性。具体而言,它将水接触角提高了令人印象深刻的 17.44%,水蒸气透过率降低了 27.56%。这些改进归因于 7S 和 11S 氨基酸残基之间的分子间相互作用,包括氢键和盐桥。结果,形成了更均匀和致密的微观结构。有趣的是,不同蛋白质级分检查的薄膜的机械和光学性能得以保持。总之,本研究有助于理解大豆蛋白的成膜性能,特别是 7S 和 11S 的作用。

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