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典型碱性蛋白质基异蛋白复合凝聚物的形成与应用

Formation and Applications of Typical Basic Protein-Based Heteroprotein Complex Coacervations.

作者信息

Xie Yufeng, Liu Qingchen, Ge Yubo, Liu Yongqi, Yang Rui

机构信息

College of Food Science and Engineering, Harbin University, Harbin 150086, China.

Tianjin Key Laboratory of Food Quality and Health, Tianjin University of Science and Technology, Tianjin 300457, China.

出版信息

Foods. 2024 Oct 16;13(20):3281. doi: 10.3390/foods13203281.

DOI:10.3390/foods13203281
PMID:39456343
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11508135/
Abstract

Lactoferrin, lysozyme, and gelatin are three common basic proteins known for their ability to interact with acidic proteins (lactoglobulin, ovalbumin, casein, etc.) and form various supramolecular structures. Their basic nature makes them highly promising for interaction with other acidic proteins to form heteroprotein complex coacervation (HPCC) with a wide range of applications. This review extensively examines the structure, properties, and preparation methods of these basic proteins and delves into the internal and external factors influencing the formation of HPCC, including pH, ionic strength, mixing ratio, total protein concentration, temperature, and inherent protein properties. The applications of different HPCCs based on these three basic proteins are discussed, including the encapsulation of bioactive molecules, emulsion stabilization, protein separation and extraction, nanogel formation, and the development of formulas for infants. Furthermore, the challenges and issues that are encountered in the formation of heteroprotein complexes are addressed and summarized, shedding light on the complexities and considerations involved in utilizing HPCC technology in practical applications. By harnessing the basic proteins to interact with other proteins and to form complex coacervates, new opportunities arise for the development of functional food products with enhanced nutritional profiles and functional attributes.

摘要

乳铁蛋白、溶菌酶和明胶是三种常见的碱性蛋白质,它们以能够与酸性蛋白质(如乳球蛋白、卵清蛋白、酪蛋白等)相互作用并形成各种超分子结构而闻名。它们的碱性性质使其在与其他酸性蛋白质相互作用以形成具有广泛应用的异源蛋白质复合凝聚物(HPCC)方面极具潜力。本综述广泛研究了这些碱性蛋白质的结构、性质和制备方法,并深入探讨了影响HPCC形成的内部和外部因素,包括pH值、离子强度、混合比例、总蛋白质浓度、温度和蛋白质固有性质。讨论了基于这三种碱性蛋白质的不同HPCC的应用,包括生物活性分子的包封、乳液稳定、蛋白质分离和提取、纳米凝胶形成以及婴儿配方奶粉的开发。此外,还阐述并总结了在形成异源蛋白质复合物过程中遇到的挑战和问题,揭示了在实际应用中利用HPCC技术所涉及的复杂性和注意事项。通过利用碱性蛋白质与其他蛋白质相互作用并形成复合凝聚物,为开发具有增强营养成分和功能特性的功能性食品带来了新机遇。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/42d2817312dc/foods-13-03281-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/c40ccc15c938/foods-13-03281-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/4a283e2a2ffb/foods-13-03281-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/607d804c0f06/foods-13-03281-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/2931d158421d/foods-13-03281-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/ad3fffeca469/foods-13-03281-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/42d2817312dc/foods-13-03281-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/c40ccc15c938/foods-13-03281-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/4a283e2a2ffb/foods-13-03281-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/607d804c0f06/foods-13-03281-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/2931d158421d/foods-13-03281-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/ad3fffeca469/foods-13-03281-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/509b/11508135/42d2817312dc/foods-13-03281-g006.jpg

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本文引用的文献

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