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大豆分离蛋白-胶原蛋白自组装纳米胶束的制备与表征

Preparation and characterization of soy protein isolate-collagen self-assembled nanomicelles.

作者信息

Wang Ruirui, Wang Hongru, Yao Yijun, Chai Yong

机构信息

College of Bioresources Chemical and Materials Engineering, Key Laboratory of Leather Cleaner Production, China National Light Industry, Shaanxi University of Science & Technology Xi'an 710021 Shaanxi China

College of Chemistry and Chemical Engineering, Qinghai Normal University Xining 810008 Qinghai China.

出版信息

RSC Adv. 2018 Oct 31;8(64):36879-36885. doi: 10.1039/c8ra08030e. eCollection 2018 Oct 26.

DOI:10.1039/c8ra08030e
PMID:35558906
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9089279/
Abstract

This paper describes the preparation and characterization of soy protein isolate (SPI)-collagen self-assembled nanomicelles. Novel SPI-collagen self-assembled nanomicelles hydrogen bonding and electrostatic interactions were developed. SPI-collagen soluble complexes were formed at pH 6.4, which was lower than the isoelectric point of collagen (pI = 7.8) and higher than that of SPI (pI = 4.5). This research mainly focuses on the intermolecular force between the SPI and collagen. The diameter distribution, critical association concentration, and stability of the SPI-collagen self-assembled nanomicelles were investigated in this research. It was found that the SPI and collagen had hydrogen bonding and electrostatic interactions, and then formed natural complex nanomicelles in a weakly acidic environment. The preparation of SPI-collagen self-assembled nanomicelles was performed in an aqueous environment without surfactants or toxic agents. As a fixing agent, transglutaminase (TGase) promoted the intra- and intermolecular cross-linking of the nanomicelles, which improved the stability of the self-assembled nanomicelles. The SPI-collagen nanomicelles had a good stability. This research may provide a reference for the utilization of SPI-collagen self-assembled nanomicelles.

摘要

本文描述了大豆分离蛋白(SPI)-胶原蛋白自组装纳米胶束的制备与表征。通过氢键和静电相互作用制备了新型的SPI-胶原蛋白自组装纳米胶束。在pH 6.4时形成了SPI-胶原蛋白可溶性复合物,该pH低于胶原蛋白的等电点(pI = 7.8)且高于SPI的等电点(pI = 4.5)。本研究主要聚焦于SPI与胶原蛋白之间的分子间作用力。研究了SPI-胶原蛋白自组装纳米胶束的粒径分布、临界缔合浓度和稳定性。结果发现,SPI与胶原蛋白存在氢键和静电相互作用,并在弱酸性环境中形成天然复合纳米胶束。SPI-胶原蛋白自组装纳米胶束的制备是在无表面活性剂或有毒试剂的水性环境中进行的。作为一种固定剂,转谷氨酰胺酶(TGase)促进了纳米胶束的分子内和分子间交联,提高了自组装纳米胶束的稳定性。SPI-胶原蛋白纳米胶束具有良好的稳定性。本研究可为SPI-胶原蛋白自组装纳米胶束的应用提供参考。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/c8e6293aba04/c8ra08030e-f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/cface151dfc2/c8ra08030e-f1.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/3d8076160390/c8ra08030e-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/1238698451c0/c8ra08030e-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/b7bedbe51ecb/c8ra08030e-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/2c157c581db6/c8ra08030e-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/b060ce0df36f/c8ra08030e-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/c8e6293aba04/c8ra08030e-f8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/cface151dfc2/c8ra08030e-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/f4025e74ad2a/c8ra08030e-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/3d8076160390/c8ra08030e-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/1238698451c0/c8ra08030e-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/b7bedbe51ecb/c8ra08030e-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/2c157c581db6/c8ra08030e-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/b060ce0df36f/c8ra08030e-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ebc/9089279/c8e6293aba04/c8ra08030e-f8.jpg

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