Effect of Casein on Whey Protein Concentrate Self-assembling to Form Nano-fibril Polymers

被引:0
作者
Xu H. [1 ]
Wang X. [1 ]
Ju T. [1 ]
Ma C. [1 ]
Guan C. [1 ]
机构
[1] College of Food Science, Northeast Agricultural University, Harbin
来源
Nongye Jixie Xuebao/Transactions of the Chinese Society for Agricultural Machinery | 2020年 / 51卷 / 10期
关键词
Casein; Nano-fibrils; Polymerization; Self-assembling; Whey protein concentrate;
D O I
10.6041/j.issn.1000-1298.2020.10.045
中图分类号
学科分类号
摘要
Proteins can self-assemble to form nano-fiber polymers under unconventional conditions. This kind of polymer structure given protein monomers and their conventional polymerization formed with high-level functional properties, but this self-assembly process was easily interfered by other proteins and destroyed the assembly and polymerization mode. The interaction of two main protein components in milk was explored, and the effect of casein (CN) on the self-assembly of whey protein concentrate (WPC) to form fibril polymers was studied, and the degree of interference of WPC by CN at different stages of self-assembly was analyzed. The results showed that incorporation of CN at different stages of fibril formation determined the structure and shape of the hybrid copolymer. The earlier CN was added, the more obvious the inhibitory effect on the fibril formation was. With the increase of CN concentration, the mixing time point of CN for the formation of fibril polymer was delated. Among them, the surface hydrophobic interaction and the formation of disulfide bonds promoted the polymerization of CN and WPC, which weakened the interaction between WPC itself, and then inhibited the self-assembly of WPC fibrils. This inhibition was particularly obvious when CN was mixed in the initial stage of fibril formation. The polymerization rate constant k and the polymerization ability of WPC and CN were increased and the polymerization between WPC was weakened. The formation of WPC fibril polymer was destroyed by the interference of CN. The results indicated that cow's milk protein cannot form nano-fibril polymers due to the effect of CN in cow's milk, but the casein in cow's milk was removed, and mixed in the middle and late stages of WPC self-assembly polymerization did not affect the formation of nano-fibril polymer structure. © 2020, Chinese Society of Agricultural Machinery. All right reserved.
引用
收藏
页码:395 / 402
页数:7
相关论文
共 25 条
  • [1] MICHAELS T C, DEAR A J, KIRKEGAARD J B, Et al., Fluctuations in the kinetics of linear protein self-assembly, Physical Review Letters, 116, 25, (2016)
  • [2] HE J S, GAO Q, MU T H, Et al., Molecular chaperone-like properties of sodium caseinate to suppress the pressure-induced aggregation of β-lactoglobulin, High Pressure Research, 39, 2, pp. 1-8, (2019)
  • [3] AROSIO P, KNOWLES T P J, LINSE S., On the lag phase in amyloid fibril formation, Physical Chemistry Chemical Physics, 17, 12, pp. 7606-7618, (2015)
  • [4] DANIELA O, WANG L., Fibrillization of whey proteins improves foaming capacity and foam stability at low protein concentrations, Journal of Food Engineering, 121, pp. 102-111, (2014)
  • [5] XU H H, WANG J, DONG S R, Et al., Acid-responsive properties of fibrils from heat-induced whey protein concentrate, Journal of Dairy Science, 99, 8, pp. 6052-6060, (2016)
  • [6] SUZANNE G B, ASTRID J V, LEONARD M C S., Heat-induced whey protein isolate fibrils: conversion, hydrolysis, and disulphide bond formation, International Dairy Journal, 17, 7, pp. 846-853, (2007)
  • [7] TOYAMA B H, WEISSMAN J S., Amyloid structure: conformational diversity and consequences, Annual Review of Biochemistry, 80, 1, pp. 557-585, (2011)
  • [8] NELSON R, EISENBERG D., Recent atomic models of amyliid fibril structure, Current Opinion in Structural Biology, 16, 2, pp. 260-265, (2006)
  • [9] GAO Y Z, XU H H, JU T T, Et al., The effect of limited proteolysis by different proteases on the formation of whey protein fibrils, Journal of Dairy Science, 96, 12, pp. 7383-7392, (2013)
  • [10] LIU Y, GUO R., pH-dependent structures and properties of casein micelles, Biophysical Chemistry, 136, 2-3, pp. 67-73, (2008)