Milk Composition - Proteins
Milk Composition
There are several types of proteins in milk.
The major milk proteins are unique to milk.
- not found in any other tissue
Milk proteins, particularly caseins, have an appropriate amino            acid composition for growth and development of the young.
Other proteins in milk include an array of enzymes, proteins involved          in transporting nutrients, proteins involved in disease resistance (antibodies          and others), growth factors, etc.
 
The          total protein component of milk is composed of numerous specific proteins.          The primary group of milk proteins are the caseins. There are 3          or 4 caseins in the milk of most species; the different caseins are distinct          molecules but are similar in structure. All other proteins found in milk          are grouped together under the name of whey proteins. The major whey proteins          in cow milk are beta-lactoglobulin and alpha-lactalbumin.
The major milk proteins, including the caseins, ß-lactoglobulin          and a-lactalbumin, are synthesized in the mammary          epithelial cells and are only produced by the mammary gland. The immunoglobulin          and serum albumin in milk are not synthesized by the epithelial cells.          Instead, they are absorbed from the blood (both serum albumin and the          immunoglobulins). An exception to this is that a limited amount of immunoglobulin          is synthesized by lymphocytes which reside in the mammary tissue (called          plasma cells). These latter cells provide the mammary gland with local          immunity.
Caseins have an appropriate amino acid composition that is important for        growth and development of the nursing young. This high quality protein in        cow milk is one of the key reasons why milk is such an important human food.
Caseins are highly digestible in the intestine and are a high quality          source of amino acids. Most whey proteins are relatively less digestible          in the intestine, although all of them are digested to some degree. When          substantial whey protein is not digested fully in the intestine, some          of the intact protein may stimulate a localized intestinal or a systemic          immune response. This is sometimes referred to as milk protein allergy          and is most often thought to be caused by ß-lactoglobulin. Milk          protein allergy is only one type of food protein allergy.
Caseins is composed of several similar proteins which form a multi-molecular,          granular structure called a casein micelle. In addition to casein          molecules, the casein micelle contains water and salts (mainly calcium          and phosphorous). Some enzymes are associated with casein micelles, too.          The micellar structure of casein in milk is an important part of the mode          of digestion of milk in the stomach and intestine, the basis for many          of the milk products industries (such as the cheese industry), and the          basis for our ability to easily separate some proteins and other components          from cow milk. Casein is one of the most abundant organic components of          milk, in addition to the lactose and milk fat. Individual molecules of casein alone are not very soluble in the aqueous environment of milk.          However, the casein micelle granules are maintained as a colloidal suspension          in milk. If the micellar structure is disturbed, the micelles may come          apart and the casein may come out of solution, forming the gelatinous          material of the curd. This is part of the basis for formation of          all non-fluid milk products like cheese.
A couple of types of Cheddar cheese, with a cheese lover.
Centrifugation of the skim milk in an ultracentrifuge (usually about 50,000         x g or greater) results in pelleting of the casein and in a supernatant          called whey (also sometimes called the serum phase of milk) which          contains         the water, lactose and soluble non-casein proteins. Once casein is removed,                  then by definition every other protein left in the milk preparation is          a whey          protein.
Casein molecules can also be separated from the whey by precipitation          of the casein with acid (similar to what happens in the stomach when milk          is consumed) or by disrupting the micellar structure by partial hydrolysis          of the protein molecules with a proteolytic enzyme. In the stomach of          the young of many species is an enzyme called rennin which specifically          hydrolyzes part of the casein micelle resulting in formation of a curd.          A classic precipitation method for casein in cow milk which is done in          the laboratory is to slowly add HCl (0.1 N) to lower the milk pH to 4.6.          The casein will gradually form a precipitate while relatively little of          the other milk proteins will precipitate. Different combinations of controlled          acid precipitation and enzymatic hydrolysis of casein are the foundation          of the cheese industries. Often specific bacterial cultures are used to          establish the conditions for lowered pH and secretion of proteolytic enzymes          which form the different types of cheese.
Because the casein micelle is in suspension, it can be separated from        the rest of milk by centrifugation at a very high speed. Generally the milk        is first defatted (the cream is removed) from whole milk by low speed        centrifugation (at about 5,000 to 10,000 x g), resulting in the cream layer        at the top, the aqueous supernatant, and a small pellet of leukocytes and        other debris. The aqueous supernatant is the skim milk (sometimes        called the plasma phase of milk).
There are many whey proteins in milk and the specific set of whey proteins          found in mammary secretions varies with the species, the stage of lactation,          the presence of an intramammary infection, and other factors. The major          whey proteins in cow milk are ß-lactoglobulin and a-lactalbumin. a-Lactalbumin is an important protein in the          synthesis of lactose and its presence is central to the process of milk synthesis. ß-Lactoglobulin's function is not known. Other whey proteins          are the immunoglobulins (antibodies; especially high in colostrum)          and serum albumin (a serum protein). Whey proteins also include          a long list of enzymes, hormones, growth factors, nutrient transporters,          disease resistance factors, and others.
Milk proteins can be separated and identified by molecular mass              (Mol. Weight; in kiloDaltons). One method of separating proteins is              by polyacrylamide gel electrophoresis. This method essentially separates              the proteins by molecular mass, with the lagest proteins migrating              more slowly in the gel and remaining nearer the top and the smaller              protiens migrating more rapidly toward the bottom of the gel. In the              gel at right, mammary secretions from several species are compared.              Note the relative size of the caseins (~25-35 kDa) vs the major whey              proteins ß-lactoglobulin (18 kDa) and a-lactalbumin              (14 kDa). Others include primarily lactoferrin (~80 kDa) and serum              albumin (~66 kDa).
Caseins have an appropriate amino acid composition that is important for        growth and development of the nursing young. This high quality protein in        cow milk is one of the key reasons why milk is such an important human food.
Caseins are highly digestible in the intestine and are a high quality          source of amino acids. Most whey proteins are relatively less digestible          in the intestine, although all of them are digested to some degree. When          substantial whey protein is not digested fully in the intestine, some          of the intact protein may stimulate a localized intestinal or a systemic          immune response. This is sometimes referred to as milk protein allergy          and is most often thought to be caused by ß-lactoglobulin. Milk          protein allergy is only one type of food protein allergy.
Study          Questions
A. Address the following items, then consider the question below:
What did you learn from the above about the function of a-lactalbumin?
What did you learn from the Lactose page about the function of lactose in the precess of milk synthesis?
What did you learn about the function of water in milk from the Water page?
Considering these facts that you have learned, what would you expect          with regard to lactation in an animal that had a mutated a-lactalbumin          gene?
 
 
B. Little Miss Muffet was observed eating her curds and whey. What would          be the composition of her curds and what would be the composition of her          whey? Also, by what method by which those curds and whey most probably          were produced?