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extracting the enzyme rennet (chymosin and pepsin) from the fourth stomach of the milk-fed calf.
Milk proteins
Caseins comprise about 80% of milk proteins, the remainder being associated with the whey fraction of milk i.e. that fraction remaining after removal of casein curds following coagulation of casein.
1) Caseins.
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Caseins are the phosphoproteins that can be precipitated from milk at pH 4.6 at 0ºC. These caseins are present in milk as macromolecular aggregates or micelles of diameter 0-00 nm. They belong to four genetic families; as1- (8%),as -(10%), b- (1%) and k- caseins (6%). These percentages refer to bovine milk in human milk there are no as1-caseins.
as1-caseins contain 1 amino acids, of which 17 are prolyl residues and 8 are phosphoseryl residues. Several genetic variants are known.
as- caseins contain 07 amino acids and 10-1 phosphoseryl residues. These are the most hydrophilic caseins but they have a hydrophobic C-terminal region. Several genetic variants are known.
b- caseins contain 0 amino acids, over 0 prolyl residues and are the most hydrophobic of the caseins. The g-caseins are believed to be hydrolysis products of b-casein, formed just prior to, or just following, milking.
k- caseins contain 16 amino acids and one phosphoseryl residue. These caseins are amphiphilic containing a charged tri or tetrasaccharide unit attached in the C-terminal region whilst the remainder of the molecule is fairly hydrophobic.
The different molecular properties of the caseins and their affinity for calcium and their phosphate content contributes to the formation of the complex casein micelle, the structure of which is not fully understood. The casein micelle is primarily protein but it also contains calcium, magnesium and citrate.
It is the k- caseins which are specifically hydrolysed by the exogenous enzyme rennet. The latter protease hydrolyses the Phe105-Met106 bond in k- casein, releasing two polypeptides, the longer being referred to as para k-casein. The action of rennet destabilises the casein micelle and causes the coagulation and formation of the casein curds.
Purpose To investigate the dependence of the coagulation of milk protein on the presence of calcium ions.
Background The coagulation of milk to make a cheese product is a process in which a soluble milk protein caseinogen is converted to the insoluble protein paracasein, which clumps or coagulates. This process involves an enzyme called rennet and this enzyme needs calcium ions to act. As the protein is coagulated it contracts and squeezes out the liquid whey.
Rennet can be found in a product available in grocery stores called Junket™. A 1% calcium chloride solution is needed and some solid sodium citrate. The citrate ion will precipitate calcium ions effectively removing them from solution and unavailable for the rennet. Fresh mild is also required.
Since calcium is required for the operation of the enzyme rennet, the milk in tube does not coagulate because the citrate ion has removed the calcium ions from solution. Addition of calcium chloride solution back to tube two should cause the coagulation of the milk.
Cows milk is rich in a wide range of chemical compounds that can be processed into various dairy products such as cheese, butter, and yogurt. Specifically the milk component involved in cheese production is a soluble protein called casein. The enzyme rennet can be used to catalyze the conversion of casein in milk to para-casein by removing a glycopeptide from the soluble casein. Para-casein further clots, i.e. coagulates, in the presence of calcium ions to form white, creamy lumps called the curd, leaving behind the supernatant called the whey.
rennet Ca++
casein ------- para-casein (aq.) -------- para-casein (ppt)
The precipitate is soft at this point and can be separated from the whey by the use of cheese cloth. Filtration does not work very well; filter paper clogging is a recurrent problem.
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