Table 2.

Physical-chemical status of cows’ milk.

Average Emulsion type Colloidal solution/ True

composition % oil/water suspension solution

Moisture 87,5

Fat 3,9 X

Proteins 3,4 X

Lactose 4,8 X

Minerals X
0,8
(Ash)

Source: https://dairyprocessinghandbook.tetrapak.com/chapter/chemistry-milk

Table 2.2
Relative sizes of particles in milk.

Size (mm) Type of particles

10-2 to 10-3 Fat globules

10-4 to 10-5 Casein-calcium phosphates

10-5 to 10-6 Whey proteins

10-6 to 10-7 Lactose, salts and other substances in true

solutions
Milk contains two types of protein: whey (20%) and casein (80%). Both are high-quality proteins,
according to science-based rating scales, and both contain all essential amino acids in amounts sufficient
to support the multiple roles of protein in the body.1,2

Source:https://www.dairynutrition.ca/nutrients-in-milk-products/protein/milk-products-source-of-high-q

u ality-protein

Structure: The Casein Micelle

Most, but not all, of the casein proteins exist in a colloidal particle known as the casein micelle . Its
biological function is to carry large amounts of highly insoluble CaP to mammalian young in liquid form
and to form a clot in the stomach for more efficient nutrition. Besides casein protein, calcium and
phosphate, the micelle also contains citrate, minor ions, lipase and plasmin enzymes, and entrapped milk
serum. These micelles are rather porous structures, occupying about 4 mL/g and 6-12% of the total
volume fraction of milk. Size ranges from 50-250 nm in diameter.
Casein micelle image from Dalgleish, D. G., P. Spagnuolo and H. D. Goff. 2004. A possible structure of
the casein micelle based on high-resolution field-emission scanning electron microscopy. International
Dairy Journal. 14: 1025-1031. This micelle is 120 nm in diameter.
There have been many models developed over the years to explain the structure of the casein micelle,
based on all of the information available about its composition and reactivity. The casein sub-micelle
model was prominent for many years, but there is sufficient evidence now to conclude that there is not a
defined sub-micellar structure to the micelle at all. More recent models suggest a more open structure
composed of aggregates of protein around calcium phosphate nanoclusters. Each of the casein proteins
has unique abilities to either bind with CaP or with other caseins, which give rise to the aggregates. The
nanoclusters provide regions of more or less density. The structure is sufficiently porous to hold a
considerable amount of water, and for the surface, and even part of the interior, to be reactive to other
substances. All models agree that the k-casein is mostly present as a stabilizing layer around the exterior
of the micelle. Please see any of the following references for great detail about micelle structures and
models.

Source: https://www.uoguelph.ca/foodscience/book/export/html/160 8

Rennin, also known as chymosin, is an enzyme that can be

easily found in the rennet. It is usually produced by the 4th stomach chamber of the cows,
called
abomasum. Infants have gastric chief cells that produce rennin in order to clot the milk and
promote much better absorption. Alternatively, the bovine rennin is produced in K. lactis,
Aspergillus niger var awamori and E. coli. Although it’s not active, this enzyme can also be
found
in the human body on chromosome 1.

Rennin enzyme is included in the protease family and along with pepsin, it’s the only enzyme
that can be found in the stomach. In its inactive form, rennin is known as prorennin. When
milk
is consumed, the stomach produces hydrochloric acid. This immediately connects with the
prorennin and activates it, forcing the enzyme to produce beneficial rennin. Milk contains the
caseinogen protein that includes TEKLYNX product identification software
● kappa-casein
● beta-casein
● alpha-s2
● alpha-s1 molecules
The last 3 molecules catalyze the interaction between calcium and milk. Kappa-casein doesn’t
have any activity on milk and calcium, but it can put an end to the other molecules from
precipitating. This is when the rennin enzyme becomes effective. It hides the kappa-casein,
allowing the precipitation of beta-casein, alpha-s2 and alpha-s1 and the absorption of milk.

Therefore, rennin is beneficial for coagulating or curdling the milk. It breaks down the milk
into
whey or liquid and semisolid substance. Thus, the stomach can digest and absorb milk
proteins,
which is extremely important for the human body. In case the stomach doesn’t produce enough
rennin, the milk is not digested properly and the calcium cannot be absorbed in the bones and
body.

So, young mammals are the only ones that can produce rennin enzymes. Immediately after
birth, their stomach secrets high doses of rennin, but with age, the production ends and the
pepsin enzyme becomes more active and important. Rennin is also used in the dairy industry
for
the making of cheese.
Source: https://worldofenzymes.info/enzymes-introduction/rennin /