Spontaneous interaction of lactoferrin with casein micelles or individual caseins

被引:29
作者
Anema, Skelte G. [1 ,2 ]
机构
[1] Fonterra Res & Dev Ctr, Palmerston North, New Zealand
[2] Massey Univ, Riddet Inst, Palmerston North, New Zealand
关键词
Casein; casein micelles; coacervation; electrostatic interaction; lactoferrin; milk; spontaneous interaction; HETEROPROTEIN COMPLEX COACERVATION; BOVINE BETA-LACTOGLOBULIN; AMYLOID FIBRIL FORMATION; ALPHA-LACTALBUMIN; PHASE-SEPARATION; KAPPA-CASEIN; SUPRAMOLECULAR STRUCTURES; POLYELECTROLYTE SYSTEMS; PROTEIN-COMPOSITION; LYSOZYME;
D O I
10.1080/03036758.2018.1439846
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The spontaneous self-assembly of biological macromolecules is of great scientific interest and of significant importance in biological as well as industrial processes. Interestingly, proteins have the ability to self-associate with other macromolecules including polysaccharides and other proteins. Food proteins such as those from milk, egg and plant sources have shown the ability to spontaneously self-associate into supra-molecular structures, and these associations have the potential to offer unique functionalities in food and technical applications. This review summarises the research our group has conducted on the spontaneous self-association of lactoferrin, a large milk-derived basic protein, with the casein micelles in milk, and with individual isolated casein proteins.
引用
收藏
页码:89 / 110
页数:22
相关论文
共 107 条
[61]   Transfer matrix theory of polymer complex coacervation [J].
Lytle, Tyler K. ;
Sing, Charles E. .
SOFT MATTER, 2017, 13 (39) :7001-7012
[62]   The physics of protein self-assembly [J].
McManus, Jennifer J. ;
Charbonneau, Patrick ;
Zaccarelli, Emanuela ;
Asherie, Neer .
CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 2016, 22 :73-79
[63]   Theory and recent applications of coacervate-based extraction techniques [J].
Melnyk, A. ;
Namiesnik, J. ;
Wolska, L. .
TRAC-TRENDS IN ANALYTICAL CHEMISTRY, 2015, 71 :282-292
[64]   The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions [J].
Mezzenga, Raffaele ;
Fischer, Peter .
REPORTS ON PROGRESS IN PHYSICS, 2013, 76 (04)
[65]   Design of bio-based supramolecular structures through self-assembly of α-lactalbumin and lysozyme [J].
Monteiro, Adenilson A. ;
Monteiro, Marcia R. ;
Pereira, Ricardo N. ;
Diniz, Renata ;
Costa, Angelica R. ;
Malcata, F. Xavier ;
Teixeira, Jose A. ;
Teixeira, Alvaro V. ;
Oliveira, Eduardo B. ;
Coimbra, Jane S. ;
Vicente, Antonio A. ;
Ramos, Oscar L. .
FOOD HYDROCOLLOIDS, 2016, 58 :60-74
[66]   Biopolymer-based coacervates: Structures, functionality and applications in food products [J].
Moschakis, Thomas ;
Biliaderis, Costas G. .
CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 2017, 28 :96-109
[67]  
Nieuwenhuijse J.A., 2003, Advanced Dairy Chemistry, V1B., P947
[68]   Formation and stability of α-lactalbumin-lysozyme spherical particles: Involvement of electrostatic forces [J].
Nigen, Michaeel ;
Croguennec, Thomas ;
Bouhallab, Said .
FOOD HYDROCOLLOIDS, 2009, 23 (02) :510-518
[69]   Apo α-lactalbumin and lysozyme are colocalized in their subsequently formed spherical supramolecular assembly [J].
Nigen, Michael ;
Croguennec, Thomas ;
Madec, Marie-Noelle ;
Bouhallab, Said .
FEBS JOURNAL, 2007, 274 (23) :6085-6093
[70]   Temperature affects the supramolecular structures resulting from α-lactalbumin-lysozyme interaction [J].
Nigen, Michael ;
Croguennec, Thomas ;
Renard, Denis ;
Bouhallab, Said .
BIOCHEMISTRY, 2007, 46 (05) :1248-1255