The protein from smp also contributes to some extent to the stability, but as this is present in micellar form, it is not optimum for emulsifying properties. Also, it is known that calcium may negatively influence the binding properties of meat proteins (3). Therefore Ca-reduced smp has found quite some application in meat products.

Milk Protein

The application of milk protein in the form of sodium casemate has found broad acceptance in the meat industry (4). The functional properties of milk protein can be explained from its molecular structure (5) (Fig. 1).

Due to the high proline and the low sulfuric amino acids content, caseinates will have a random coil structure with a low percent helix. As a consequence, caseinates will show no heat gelation and denaturation and will have a high viscosity in solution.

Caseinates have a high electrical charge and have several very hydrophobic groups. This makes them perfect

£ Very hydrophobic residues £ Charged residues

Hydrophobic residues 1 Proline o Hydrophilic residues 1 ■ Crysteine emulsifiers, with a strong preference for interfaces fat/ water or air/water. The high charge makes them perfectly soluble in water.

Caseinates build strong, flexible membranes that will hardly be influenced by heat. Whey proteins show a different pattern (Fig. 2). They are low in proline and have many S-S bonds, leading to a globular, strongly folded and organized structure. Whey proteins are sensitive to heat. During heating they unfold and, depending on pH and concentration, they will build intermolecular disulfide bonds resulting in gelation. The globular form is also the reason for the low viscosity in solution.

Whey proteins have a rather high hydrophobicity, which is more evenly distributed than in caseinate. Because of this structure, the application possibilities of whey proteins in meat products are very limited and will not be discussed in this article.

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