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用三聚磷酸钠磷酸化的小麦面筋蛋白:结构变化以改善功能特性从而扩大应用范围。

Wheat gluten proteins phosphorylated with sodium tripolyphosphate: Changes in structure to improve functional properties for expanding applications.

作者信息

Hu Fei, Zou Peng-Ren, Zhang Fan, Thakur Kiran, Khan Mohammad Rizwan, Busquets Rosa, Zhang Jian-Guo, Wei Zhao-Jun

机构信息

School of Food and Biological Engineering, Hefei University of Technology, Hefei, 230601, China.

School of Biological Science and Engineering, Collaborative Innovation Center for Food Production and Safety, North Minzu University, Yinchuan, 750021, China.

出版信息

Curr Res Food Sci. 2022 Aug 28;5:1342-1351. doi: 10.1016/j.crfs.2022.08.014. eCollection 2022.

DOI:10.1016/j.crfs.2022.08.014
PMID:36082141
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9445281/
Abstract

Poor solubility of wheat gluten proteins (WG) has negative impact on functional attributes such as gelation and emulsification, which limits it use in the food industry. In this study, WG underwent different degrees of phosphorylation using sodium tripolyphosphate (STP). Phosphoric acid groups were successfully incorporated in the WG via covalent bonding (C-N-P and C-O-P) involving hydroxyl and primary amino groups from WG. The introduction of phosphoric acid groups increased the negative charge of phosphorylation-WG, which caused the enhancement of electrostatic repulsion between proteins and reduced the droplet size in emulsions, thereby allowing proteins to be more efficiently dispersed in the solution system. The change of structure induced with phosphorylation improved hydration of protein, making the WG with higher solubility, thereby resulting in the improvement of its emulsification, foaming, thermal stability, and rheological properties. Therefore, WG can be modified by phosphorylation which caused an overall improvement of functional properties, thus facilitating the expansion of WG applications.

摘要

小麦面筋蛋白(WG)的低溶解度对其凝胶化和乳化等功能特性具有负面影响,这限制了它在食品工业中的应用。在本研究中,使用三聚磷酸钠(STP)对WG进行了不同程度的磷酸化处理。磷酸基团通过涉及WG中的羟基和伯氨基的共价键(C-N-P和C-O-P)成功地引入到WG中。磷酸基团的引入增加了磷酸化-WG的负电荷,这导致蛋白质之间的静电排斥增强,并减小了乳液中的液滴尺寸,从而使蛋白质能够更有效地分散在溶液体系中。磷酸化诱导的结构变化改善了蛋白质的水合作用,使WG具有更高的溶解度,从而导致其乳化、起泡、热稳定性和流变学性质得到改善。因此,WG可以通过磷酸化进行改性,这会导致其功能特性的全面改善,从而促进WG应用范围的扩大。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/cb0648b3293e/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/5800d82f3f3f/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/9ef227221749/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/00b46d972fe2/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/471e6239b06e/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/cfe88e8c8803/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/cb0648b3293e/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/5800d82f3f3f/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/9ef227221749/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/00b46d972fe2/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/471e6239b06e/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/cfe88e8c8803/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d222/9445281/cb0648b3293e/gr5.jpg

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