Self-assembly of β-lactoglobulin and egg white lysozyme as a potential carrier for nutraceuticals

被引:57
作者
Diarrassouba, Fatoumata [1 ]
Remondetto, Gabriel [2 ]
Garrait, Ghislain [3 ]
Alvarez, Pedro [1 ]
Beyssac, Eric [3 ]
Subirade, Muriel [1 ]
机构
[1] Univ Laval, INAF STEIA, Chaire Rech Canada Prot Biosyst & Aliments Fonct, Quebec City, PQ G1V 0A6, Canada
[2] Agropur Cooperat, Ctr Rech & Dev, St Hubert, PQ, Canada
[3] EA CIDAM, Fac Pharm, Lab Biopharm, F-63001 Clermont Ferrand, France
基金
加拿大自然科学与工程研究理事会;
关键词
beta-Lactoglobulin; Lysozyme; Self-assembly; Proteins; Bioactives; Delivery vehicle; ALPHA-LACTALBUMIN; WHEY PROTEINS;
D O I
10.1016/j.foodchem.2014.10.009
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Self-assembly structures of p-lactoglobulin (beta lg) and egg protein lysozyme (Lyso) were developed, using electrostatic interactions between the two oppositely charged proteins. Different beta lg/Lyso concentration ratios were essayed at pH 6.8 to select the optimal ratio for the proteins co-precipitation, which behaviour was then studied at varying pH values. Optimal beta lg/Lyso concentration ratio, prepared at pH 7.5, was selected for protein co-precipitation. As a result, a structure with a mean diameter of 7.1 +/- 2.5 mu m was formed, as indicated by static light scattering. Furthermore, the SEM images showed that beta lg and Lyso self-assembled to form a microsphere. Vitamin D-3, used as a model nutraceutical, was successfully entrapped in the beta lg/Lyso microspheres with an encapsulation efficiency of 90.8 +/- 4.8%. Therefore, the beta lg/Lyso microspheres can serve as a potential food-grade vehicle for bioactives in the formulation of food products and pharmaceuticals. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:203 / 209
页数:7
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