Surfaces containing casein

Like as2-casein, /e-casein has two disulfide bonds which can form cross-links with /3-lactoglobulin. The N-terminal two-thirds of the molecule is hydrophobic and contains the two disulfide bonds. The C-termi-nal end is hydrophilic, polar, and charged. It varies in the number of attached carbohydrate moieties and has only one phosphate group. These characteristics make /c-casein ideal for the surface of casein micelles, where it is most often found. It is not susceptible to calcium ion binding, as the other caseins are, and when present on the surface of micelles, it protects the other caseins from calcium (McMahon and Brown 1984A Swaisgood 1982). 

Safety matches incorporating red P were first introduced by J.E. Lundstrom in 1885. The match heads contain an oxidising agent, sulphur, ground glass and glue or casein, while the striking surface contains red phosphorus. A typical formulation is... 

Milk is a natural colloidal dispersion that contains casein micelles, self-assembled protein associates with a diameter of about 200 nm [20]. The casein micelles are protected against flocculation by an assembly of dense hairs (often called a brush ) at their surfaces. Polymer brushes can thus provide steric stabilization of colloids. For millennia, man used the fact that milk flocculates and gels when it is acidified, as in yogurt production. Below pH = 5 macroscopic flocculation of the casein micelles in milk is observed [21]. This means that the interactions between casein micelles change from repulsive to attractive. The explanation is that acidification leads to collapse of the casein brushes [22]. In cheese-making the steric stabilization is removed by enzymes, which induce gelation into cheese curd. 

Tooth remineralization products contain casein-derived compounds that stabilize amorphous calcium phosphate (AGP) and release the AGP onto tooth surfaces, where it can facilitate remineralization [134, 135]. 

Dalgleish DG, Srinivasan M, Singh M. 1995. Surface properties of oil-in-water emulsion droplets containing casein and Tween-60. J Agric Food Chem 43 2351-2355. 

Avseenko et al. (2001) immobilized antigens onto aluminum-coated Mylar films by electrospray (ES) deposition. Various surface modifications of the metallized films were studied to determine their abilities to enhance sensitivity. The plastic surfaces were firsf cleaned by plasma discharge treatment, followed by coating with proteins (BSA and casein) or polymers such as poly (methyl methacrylate) or oxidized dextran, or they were exposed to dichlorodimethyl silane to create hydrophobic surfaces. Protein antigen was prepared in 10-fold excess sucrose and sprayed onto the surfaces to form arrays with spot diameters between 7 and 15 pm containing 1 to 4 pg protein. 

Dickinson, E., Golding, M. (1998). Influence of calcium ions on creaming and rheology of emulsions containing sodium caseinate. Colloids and Surfaces A Physicochemical and Engineering Aspects, 144, 167-177. 

Pugnaloni, L.A., Matia-Merino, L., Dickinson, E. (2005). Microstructure of acid-induced caseinate gels containing sucrose quantification from confocal microscopy and image analysis. Colloids and Surfaces B Biointerfaces, 42, 211-217. 

An ELISA (enzyme-linked immunosorbent assay) allows for rapid screening and quantification of the presence of an antigen in a sample (Fig. 5-28b). Proteins in a sample are adsorbed to an inert surface, usually a 96-well polystyrene plate. The surface is washed with a solution of an inexpensive nonspecific protein (often casein from nonfat dry milk powder) to block proteins introduced in subsequent steps from also adsorbing to these surfaces. The surface is then treated with a solution containing the primary antibody—an antibody against the protein of interest. Unbound antibody is washed away and the surface is treated with a solution containing antibodies against the primary antibody. These secondary antibodies have been linked to an enzyme that catalyzes a reaction that forms a colored product. After unbound secondary antibody is washed away, the substrate of the antibody-linked enzyme is added. Product formation (monitored as color intensity) is proportional to the concentration of the protein of interest in the sample. 

Lactic streptococci initiate casein degradation through the action of cell wall-associated and cell membrane-associated proteinases and peptidases. Small peptides are taken into the cell and hydrolyzed to their constituent amino acids by intracellular peptidases (Law and Sharpe 1978). Peptides containing four to seven residues can be transported into the cell by S. cremoris (Law et al. 1976B). S. lactis and S. cremoris have surface-bound peptidases and thus are not totally dependent on peptide uptake for protein use (Law 1979B). Some surface peptidases of S. cremoris are located in the cell membrane, whereas others are located at the cell wall-cell membrane interface (Exterkate 1984). Lactic streptococci have at least six different aminopeptidase activities, and can be divided into three groups based on their aminopeptidase profiles (Kaminogawa et al 1984). 

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