Research Progress of Heteroprotein Complex Coacervation

被引:0
作者
Zhang Y. [1 ]
Peng S. [1 ]
Wang Q. [1 ]
Guo Q. [1 ]
Zhao M. [1 ]
Fang Y. [2 ]
机构
[1] Hubei University of Technology, Hubei International Scientific and Technological Cooperation Base of Food Hydrocolloids, Wuhan
[2] Department of Food Science and Technology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai
关键词
Environmental factors; Food application; Heteroprotein complex coacervation; Typical systems;
D O I
10.16429/j.1009-7848.2021.12.033
中图分类号
学科分类号
摘要
Heteroprotein complex coacervation is a phase separation phenomenon that occurs between two oppositely charged proteins, and it has attracted increasing attention from food researchers. This review first introduced the definition and characteristics of the heteroprotein complex coacervation. Then, the typical systems of heteroprotein complex coacervation and the influences of the environmental factors on the coacervation process were summarized. Also, the applications of heteroprotein complex coacervation in the delivery of small molecule bioactives, the probiotic encapsulation, the separation and purification of proteins and the stabilization of emulsions were introduced in detail. Finally, the research direction of heteroprotein complex coacervation was prospected. © 2021, Editorial Office of Journal of CIFST. All right reserved.
引用
收藏
页码:302 / 310
页数:8
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共 68 条
[11]  
EGHBAL N, YARMAND M S, MOUSAVI M, Et al., Complex coacervation for the development of composite edible films based on LM pectin and sodium caseinate, Carbohydrate Polymers, 151, pp. 947-956, (2016)
[12]  
CHEN L, REMONDETTO G E, SUBIRADE M., Food protein-based materials as nutraceutical delivery systems, Trends in Food Science & Technology, 17, 5, pp. 272-283, (2006)
[13]  
GORDEEV A B, KARGATOV A M, EFIMOV A V., PCBOST: Protein classification based on structural trees, Biochemical and Biophysical Research Communications, 397, 3, pp. 470-471, (2010)
[14]  
SALVATORE D B, DURAFFOURG N, FAVIER A, Et al., Investigation at residue level of the early steps during the assembly of two proteins into supramolecular objects, Biomacromolecules, 12, 6, pp. 2200-2210, (2011)
[15]  
DESFOUGEERES Y, CROGUENNEC T, LECHEVALIER V R, Et al., Charge and size drive spontaneous self-assembly of oppositely charged globular proteins into microspheres, The Journal of Physical Chemistry B, 114, 12, pp. 4138-4144, (2010)
[16]  
WANG B, TIMILSENA Y P, BLANCH E, Et al., Lactoferrin: Structure, function, denaturation and digestion, Critical Reviews in Food Science and Nutrition, 59, 4, pp. 580-596, (2019)
[17]  
JIANG R L, LIU L, DU X G, Et al., Evaluation of bioactivities of the bovine milk lactoferrin-osteopontin complex in infant formulas, Journal of Agricultural and Food Chemistry, 68, 22, pp. 6104-6111, (2020)
[18]  
LIU L, JIANG R L, LONNERDAL B., Assessment of bioactivities of the human milk lactoferrin-osteopontin complex in vitro, Journal of Nutritional Biochemistry, 69, pp. 10-18, (2019)
[19]  
LIN L F, XU W, LIANG H S, Et al., Construction of pH-sensitive lysozyme/pectin nanogel for tumor methotrexate delivery, Colloids and Surfaces B-Biointerfaces, 126, pp. 459-466, (2015)
[20]  
SAHOO N, SAHOO R K, BISWAS N, Et al., Recent advancement of gelatin nanoparticles in drug and vaccine delivery, International Journal of Biological Macromolecules, 81, pp. 317-331, (2015)