In vitro interactions between probiotic bacteria and milk proteins probed by atomic force microscopy

被引:51
作者
Burgain, J. [1 ]
Gaiani, C. [1 ]
Francius, G. [2 ]
Revol-Junelles, A. M. [1 ]
Cailliez-Grimal, C. [1 ]
Lebeer, S. [3 ,4 ]
Tytgat, H. L. P. [3 ,4 ]
Vanderleyden, J. [3 ]
Scher, J. [1 ]
机构
[1] Univ Lorraine, LIBio, Lab Ingn Biomol, F-54505 Vandoeuvre Les Nancy, France
[2] Univ Lorraine, LCPME, UMR 7564, F-54505 Vandoeuvre Les Nancy, France
[3] Katholieke Univ Leuven, Ctr Microbial & Plant Genet, Louvain, Belgium
[4] Univ Antwerp, Dept Biosci Engn, B-2020 Antwerp, Belgium
关键词
Probiotic; Interactions; Milk proteins; Adhesion; LACTIC-ACID BACTERIA; RAY PHOTOELECTRON-SPECTROSCOPY; CASEIN MICELLES; FUNCTIONAL-ANALYSIS; LACTOCOCCUS-LACTIS; SURFACE-PROPERTIES; REUTERI RC-14; ADHESION; CHEESE; YOGURT;
D O I
10.1016/j.colsurfb.2012.11.032
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Interactions between microbial cells and milk proteins are important for cell location into dairy matrices. In this study, interactions between two probiotic strains, Lactobacillus rhamnosus GG and Lactobacillus rhamnosus GR-1, and milk proteins (micellar casein, native and denatured whey proteins) were studied. The bacterial surface characterization was realized with X-ray photoelectron spectroscopy (XPS) to evaluate surface composition (in terms of proteins, polysaccharides and lipid-like compounds) and electrophoretic mobility that provide information on surface charge of both bacteria and proteins along the 3-7 pH range. In addition, atomic force microscopy (AFM) enabled the identification of specific interactions between bacteria and whey proteins, in contrast to the observed nonspecific interactions with micellar casein. These specific events appeared to be more important for the GG strain than for the GR-1 strain, showing that matrix interaction is strain-specific. Furthermore, our study highlighted that in addition to the nature of the strains, many other factors influence the bacterial interaction with dairy matrix including the nature of the proteins and the pH of the media. (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:153 / 162
页数:10
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