About Dairy Market

Milk Protein

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 productiom.

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 phsyical properties 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, the6-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.

The serum (whey) protein family consists of approximately 50% ß-lactoglobulin, 20% α-lactalbumin, blood serum albumin, immunoglobulins, lactoferrin, transferrin, and many minor proteins and enzymes. Like the other major milk components, each whey protein has its own characteristic composition and variations. Whey proteins do not contain phosphorus, by definition, but do contain a large amount of sulfur-containing amino acids. These form disulfide bonds within the protein causing the chain to form a compact spherical shape. The disulfide bonds can be broken, leading to loss of compact structure, a process called denaturing. Denaturation is an advantage in yogurt production because it increases the amount of water that the proteins can bind, which improves the texture of yogurt. This principle is also used to create specialized whey protein ingredients with unique functional properties for use in foods. One example is the use of whey proteins to bind water in meat and sausage products.

The functions of many whey proteins are not clearly defined, and they may not have a specific function in milk but may be an artifact of milk synthesis. The function of ß-lactoglobulin is thought to be a carrier of vitamin A. It is interesting to note that ß-lactoglobulin is not present in human milk. α-Lactalbumin plays a critical role in the synthesis of lactose in the mammary gland. Immunoglobulins play a role in the animal’s immune system, but it is unknown if these functions are transferred to humans. Lactoferrin and transferrin play an important role in iron absorption and there is interest in using bovine milk as a commercial source of lactoferrin.

Milk Protein Physical Properties

The caseins in milk form complexes called micelles that are dispersed in the water phase of milk. The casein micelles consist of subunits of the different caseins (α-s1, α-s2 and ß) held together by calcium phosphate bridges on the inside, surrounded by a layer of 6-casein which helps to stabilize the micelle in solution.

Casein micelles are spherical and are 0.04 to 0.3 µm in diameter, much smaller than fat globules which are approximately 1 µm in homogenized milk. The casein micelles are porous structures that allow the water phase to move freely in and out of the micelle. Casein micelles are stable but dynamic structures that do not settle out of solution. They can be heated to boiling or cooled, and they can be dried and reconstituted without adverse effects. ß-casein, along with some calcium phosphate, will migrate in and out of the micelle with changes in temperature, but this does not affect the nutritional properties of the protein and minerals.

The whey proteins exist as individual units dissolved in the water phase of milk.

Deterioration of Milk Protein

Proteins can be degraded by enzyme action or by exposure to light. The predominant cause of protein degradation is through enzymes called proteases. Milk proteases come from several sources: the native milk, airborne bacterial contamination, bacteria that are added intentionally for fermentation, or somatic cells present in milk. The action of proteases can be desirable, as in the case of yogurt and cheese manufacture, so, for these processes, bacteria with desirable proteolytic properties are added to the milk. Undesirable degradation (proteolysis) results in milk with off-flavors and poor quality. The most important protease in milk for cheese manufacturing is plasmin because it causes proteolysis during ripening which leads to desirable flavors and texture in cheese.

Two amino acids in milk, methionine and cystine are sensitive to light and may be degraded with exposure to light. This results in an off-flavor in the milk and loss of nutritional quality for these 2 amino acids.

Influence of Heat Treatment on Milk Proteins

The caseins are stable to heat treatment. Typical high temperature short time (HTST) pasteurization conditions will not affect the functional and nutritional properties of the casein proteins. High temperature treatments can cause interactions between casein and whey proteins that affect the functional but not the nutritional properties. For example, at high temperatures, ß-lactoglobulin can form a layer over the casein micelle that prevents curd formation in cheese.

The whey proteins are more sensitive to heat than the caseins. HTST pasteurization will not affect the nutritional and functional properties of the whey proteins. Higher heat treatments may cause denaturation of ß-lactoglobulin, which is an advantage in the production of some foods (yogurt) and ingredients because of the ability of the proteins to bind more water. Denaturation causes a change in the physical structure of proteins, but generally does not affect the amino acid composition and thus the nutritional properties. Severe heat treatments such as ultra high pasteurization may cause some damage to heat sensitive amino acids and slightly decrease the nutritional content of the milk. The whey protein α-lactalbumin, however, is very heat stable.

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