Types of Casein protein

This page describes the properties of milk protein. There is a brief introduction to, followed by sections on, , , and the. For more details on milk protein properties see references by Fox and McSweeney (1998), Jelen and Rattray (1995), Singh (1995), and Walstra et al. (1999).

General Protein Definition & Chemistry

Proteins are chains of amino acid molecules connected by peptide bonds.

There are many types of proteins and each has its own amino acid sequence (typically containing hundreds of amino acids). There are 22 different amino acids that can be combined to form protein chains. There are 9 amino acids that the human body cannot make and must be obtained from the diet. These are called the essential amino acids.

The amino acids within protein chains can bond across the chain and fold to form 3-dimensional structures. Proteins can be relatively straight or form tightly compacted globules or be somewhere in between. The term “denatured” is used when proteins unfold from their native chain or globular shape. Denaturing proteins is beneficial in some instances, such as allowing easy access to the protein chain by enzymes for digestion, or for increasing the ability of the whey proteins to bind water and provide a desirable texture in yogurt production.

Milk Protein Chemistry

Milk contains 3.3% total protein. Milk proteins contain all 9 essential amino acids required by humans. Milk proteins are synthesized in the mammary gland, but 60% of the amino acids used to build the proteins are obtained from the cow's diet. Total milk protein content and amino acid composition varies with cow breed and individual animal genetics.

There are 2 major categories of milk protein that are broadly defined by their chemical composition and physical properties. The casein family contains phosphorus and will coagulate or precipitate at pH 4.6. The serum (whey) proteins do not contain phosphorus, and these proteins remain in solution in milk at pH 4.6. The principle of coagulation, or curd formation, at reduced pH is the basis for cheese curd formation. In cow's milk, approximately 82% of milk protein is casein and the remaining 18% is serum, or whey protein.

The casein family of protein consists of several types of caseins (α-s1, α-s2, ß, and 6) and each has its own amino acid composition, genetic variations, and functional properties. The caseins are suspended in milk in a complex called a micelle that is discussed below in the section. The caseins have a relatively random, open structure due to the amino acid composition (high proline content). The high phosphate content of the casein family allows it to associate with calcium and form calcium phosphate salts. The abundance of phosphate allows milk to contain much more calcium than would be possible if all the calcium were dissolved in solution, thus casein proteins provide a good source of calcium for milk consumers. The 6-casein is made of a carbohydrate portion attached to the protein chain and is located near the outside surface of the casein micelle (see Figure 2 below). In cheese manufacture, the 6-casein is cleaved between certain amino acids, and this results in a protein fragment that does not contain the amino acid phenylalanine. This fragment is called milk glycomacropeptide and is a unique source of protein for people with phenylketonuria.