MILK COMPOSITION

KMK33803 MEAT AND DAIRY TECHNOLOGY

• Dr Mohd Asraf Bin Mohd Zainudin

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 Importance to learn Dairy Science and
Technology; Why should I learn dairy science?
• Milk is one of the major nutritious food/almost complete food
• Expanding the production to cater human needs on food
• Creating new product based from dairy
• Produce safe dairy product for human
• New technologies continue to provide nutritional products that allow
the nutritionists to increase the limits of a well-balanced ration for
production and improved well-being for cows and the environment

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• Milk is classified as an oil-in-water (O/W) emulsion (polar and non polar
component co-exist in a homogenous solution)
• The liquid contained micro size particles and this system showed that;
• (1) chemical components are present in separate compartments, which can
greatly affect their reactivity;
• (2) the presence of particles greatly affects some physical properties, like viscosity
and optical appearance;
• (3) interaction forces between particles generally determine the physical stability
of the system;
• (4)the separation of some components (fat and casein) is relatively easy.
• The chemical composition of milk largely determines
• its nutritional value;
• The extent to which microorganisms can grow in it (Shelf-life)
• its flavor and taste
• the chemical reactions that can occur in milk.
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Milk Structure
• This emulsion system consist of ;
• Casein micelles (protein)=Milk-(FG+S)
• Casein, salt, water
• Fat globule= Milk –CM+S
• Milk Serum= Milk-FG+CM
• Each compartment have their own composition
• Give distinct characteristic
• Physicochemical properties

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Milk Composition

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Water
• Largest portion
• The water activity (aw) of milk is 0.993 on average.
• Small percentage water bound to the protein and liposome*

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 Carbohydrate
• Lactose- disaccharide consisting of a galactose molecule and a molecule of
glucose joined together with a beta 1–4 glycosidic bond.
• lactose is a reducing sugar
• hydrolyzed by the enzyme lactase, more precisely, β-galactosidase(EC
3.2.1.23), which is secreted in the small intestine.
• Sweetness: a lactose solution is approximately 0.3 times as sweet as a
sucrose solution of the same concentration. The present of protein, casein
further masked the sweet taste from lactose.
• heat treatment caused caramelization and Maillard reactions
• Maillard reaction occur in the presence of amino groups, especially the ε-
amino group of lysine residues in proteins
• Crystallization of lactose can occurred especially in concentrated or dry
milk product
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• Lactose intolerant cause by lack of lactase that function to breakdown
this 1-4 beta glycosidic bond.
• Unable to process the sugar lead to diarrhea, gases and bloating after
dairy product consumption.
• How to solve this problem?

1-4 beta glycosidic bond

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• Besides lactose (main carbohydrate in milk), other carbohydrates can also
be found in milk, such as some monosaccharides and oligosaccharides
• glucose (Glc),
• galactose (Gal),
• N-acetylglucosamine (GlcNAc),
• N-acetylgalactosamine,
• fucose
• the sialic acids
• N-acetylneuraminic acid and N-glycolylneuraminic acid

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Lipid
• The triacylglycerols, generally called triglycerides, make up over 98% of the milk lipids
• Milk contains a relatively high proportion (15 to 20 mol %) of short-chain fatty acid
residues, with 4 to 10 C atoms (Table
• The proportion of saturated fatty acid residues is high; for example, 70 mol % (≈ 63%
w/w).
• Oleic acid is the most abundant of the unsaturated fatty acid residues (about 70%).
• The other unsaturated fatty acid residues are present in a wide variety of chain length
as well as in number, position, and configuration of the double bonds.
• Factors affect milk fat composition
• Species and breed
• Animal feed

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Milk fat distribution and composition

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SALTS
• Milk contains inorganic and organic salts.
• The concept of ‘salts’ thus is not equivalent to ‘mineral substances.’
• Salts are by no means equivalent to ‘ash’ because ashing of milk
causes loss of organic acids including citrate and acetate and because
organic phosphorus and sulfur are transferred to inorganic salts
during ashing.
• Not all of the salts are dissolved, and not all of the dissolved salts are
ionized. (E.g salts in casein micelles is insoluble)

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• A very important nutrient in milk is calcium phosphate, which is
needed for growth and maintenance of bones.
• calcium phosphates are poorly soluble in water but ruminant milk
especially cow can solved this problem.
1. cows’ milk has a relatively high casein content, and casein can
accommodate large quantities of undissolved calcium phosphate by
forming casein micelles.
2. the concentration of citrate in milk is high, and it strongly associates
with calcium, which means that the calcium ion activity in milk is quite
low.
3. part of the phosphate is esterified and thereby kept in the casein
micelles or in solution

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 Protein
• Important component in milk that will determine the quality of the milk
• Few important term when discussing about protein;
• Primary structure (amino acid composition)
• Conformation
• (alpha-helix, beta sheet, disulphide bond S-S, hydrophobic group, hydrophilic group)
• Denaturation
• (Factor that can affect denaturation- pH, Temperature, Pressure, Chemical reagants)-what will
happens if protein undergo denaturation??
• Solubility
• (Factor affecting the solubility- intermolecular electrostatic and hydrophobic interactions, and
molar mass)

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Milk Protein nutritional value
• digestibility of milk protein is close to 100%
• best estimator may be the protein efficiency ratio (PER), the ratio of
weight gain of a growing animal to its protein intake
• PER value of
• Casein is ∼2.5,
• serum protein ∼3.0,
• of whole milk protein ∼3.3

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• About 95% of the nitrogen in milk is in the form of proteins
• Which type of analysis that suitable to determine protein content in
milk?
• Multiplication factor of 6.38 is generally accepted for milk
• Protein in milk composed of two major group
• Casein- Casein is a mixture of several components that form a bulk
micelles structure called casein micelles.
• Serum protein/Whey protein
• α-lactalbumin, β-globulin, Immunoglobulin (Ig)

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 • Caseins are hydrophobic;
• they have a fairly high charge,
• Many prolines, and few cysteine residues.
• They do not form anything more than short lengths of α-helix and
have little tertiary structure
• 4 type of casein- αs1-, αs2-, β-, κ-, γ- casein*
• the molar ratio of αs1-, αs2-, β-, κ-casein is about 11:3:10:4.
• γ-Casein is a degradation product of β-casein.

Amino acid sequence

MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSEST
EDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIV
PNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQ
YTDAPSFSDIPNPIGSENSEKTTMPLW
24-05-2022 Source; https://www.uniprot.org/uniprot/P02662 αs1-casein 22
Caseine micelles

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• Electron micrographs show roughly spherical particles, average size
on the order of 0.1 μm, with a marked spread in size.
• The core of a micelle consists of roughly equal amounts of αs- and β-
casein, with very little κ-casein.
• The outer layer appears to consist of about equal amounts of κ- and
αs-casein, with very little β-casein.
• Existence of a ‘hairy layer,’ consisting of the C-terminal of κ-casein.
hairs are quite hydrophilic and are negatively charged.
• Nanoclusters of calcium phosphate of about 3-nm diameter. These
contain the inorganic phosphate and much of the calcium in the
micelles.
• Hydrodynamic voluminosity of casein micelles is considerable, about
4 ml per gram of dry casein, implying that the casein micelles must
contain a lot of water.
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Function properties of casein
Solubility A typical solubility-pH profile of casein shows that close to its isoelectric pH, i.e. pH 4.0-5.0,

Water-holding Casein micelles bind large amount of (2-4 g/g protein) water as compared to globular protein (50 g/100 g of
capacity protein). This is due to the mechanical entrapment of water in the micellar matrix (via colloidal calcium
phosphate). The k-casein 'hairs' (having carbohydrate moiety) that protrude from the surface of the micelles
also contribute to the large amount of water associated with the micelles. So casein can modify the texture
of dough or baked products, serve as the matrix former in cheese-type products, produce specialised plastic
materials, or increase the consistency of solutions such as soups.

Gelation Gel-like structures are formed at > 5% protein at temperatures < 40°C, which may be exploited in the
preparation of milk protein-containing fruit gels.
Cheese production also application from this properties after partially hydrolyzed by rennet.

Emulsification Casein forms complexes with milk fats and other lipids and acts as emulsifier by forming a stable coating
around fat globules.
Foaming Caseinates generally give higher foam overruns, but produce less stable foams than egg white or whey
protein concentrates. The excellent surfactant property of the amphiphillic casein is also responsible for its
use in whipped toppings, cake mixes, and ice-cream.
Viscosity Caseinates from highly viscous solution at concentration greater than 15% and even at high temperatures
containing greater than 20% protein is so high as to make them difficult to process.
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Serum Protein
• typically are globular proteins: they have relatively high
hydrophobicity and compactly folded peptide chains.
• become insoluble at pH values below 6.5 if milk is heated
• α-lactalbumin
• protein is a small, compactly folded, more or less spherical molecule. It does
• not associate, except at low ionic strength.
• β-lactoglobulin
• major serum protein, and its properties tend to dominate the properties of
whey protein preparations
• solubility strongly depends on pH and ionic strength
• The protein is subject to a number of changes in tertiary and quaternary
structure with changes in pH or temperature.

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• Immunoglobulins are antibodies synthesized in response to stimulation by specific
antigens.
• Immunoglobulins are large glycoprotein molecules of heterogeneous composition
• classes of immunoglobulins are distinguished, including G (gammaglobulins), A, and
M (macroglobulins)
• The concentrations are highly variable. Concentrations in colostrum can be 30 to
100 times as high, whereas very little is present in late-lactation milk

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Enzymes
• The native enzymes can be present at different locations in the milk

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 Group of enzyme and their function
Group Type of enzymes Function
Antimicrobial 1. Lactoperoxidase (EC 1.11.1.7) Mechanism of action
2. Lysozyme (EC 3.2.1.17) 1. Oxidized reaction involving H2O2
2. hydrolyzes polysaccharides of bacterial cell walls,
eventually causing lysis of the bacteria
Oxidation-reduction 1.Xanthine oxidase (EC 1.1.3.22) 1. catalyze oxidation of various substances
2. Superoxide dismutase (EC 1.15.1.1) 2. superoxide anion, O2− to hydrogen peroxide
3. Sulfhydryl oxidase (EC 1.8.?) 3. Catalyzes oxidation of sulfhydryl groups to
4.Catalase disulfides
5. Lactoperoxidase
Phosphatase alkaline phosphatase (EC 3.1.3.1) hydrolysis of certain phosphoric esters in milk.
acid phosphatase (EC 3.1.3.2) Important enzyme as a marker for pasteurization
Lipolytic enzyme lipoprotein lipase (EC 3.1.1.34) liberates fatty acids from tri- and diglycerides
and is only active at the oil–water interface
Proteinases 1. Plasmin (EC 3.4.21.7) or alkaline milk Hydrolyzed protein
proteinase
2. Acid proteinases or cathepsin D (EC
3.4.23.5),
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Other natural components
• Organic acids: small quantities of other organic acids (e.g., trace amounts of lactic
and pyruvic acid) occur in milk serum.
• Nitrogenous compounds: On average, about 5% of total nitrogen in milk is
nonprotein nitrogen (NPN). partly intermediate products of the protein
metabolism of the animal (e.g., ammonia, urea, creatine, creatinine, and uric
acid)
• Vitamins: All known vitamins are present in milk.
• Ribonucleic acids and their degradation products, e.g., phosphate esters and
organic bases.
• Sulfuric acid esters: Only indoxyl sulfate has been found in milk.
• Carbonyl compounds: An example is acetone; more of it occurs if the cow suffers
from ketosis.
• Gases: In milk the amount of nitrogen is about 16 mg⋅kg−1, that of oxygen about
6 mg⋅kg−1, or about 1.3% and 0.4% by volume, respectively
• Hormones: Several hormones are present in trace quantities in milk. Examples are
prolactin, somatotropin, and steroids
• Somatic cells

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Vitamins

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Factors affecting Milk Composition
• Genetic factors: Breed and individual.
• The stage of lactation: This can have a significant effect. Especially
the milk obtained within 2 or 3 d after parturition tends to have a very
different composition; it is called colostrum or beestings.
• Illness of the cow: Especially severe mastitis (inflammation of the udder)
can have a relatively large effect. The milk tends to have an increased
content of somatic cells.
• Feed: The amount and the quality of the feed given strongly affect milk
yield. However, the effect of the cow’s diet on milk composition is fairly
small, except for milk fat content and composition.

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Milk Dairy Sources
• Animal
• Cow
• Sheep
• Buffalo
• Goat
• Camel
• Horse

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 Question
• Which type of cow suitable for dairy production??
• Criteria for breed selection.

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Cow breed for milk

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Lactation stage

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Illness
• pathogenic bacteria enter a mammary gland, a severe inflammation
can result, called mastitis.
• somatic cell count (number of cells per milliliter) is often taken as a
measure of the severity of the mastitis and of the change in milk
composition
• Although the correlations are far from perfect.
• Other factors also affect the cell count: for healthy cows it increases
with age and with stage of lactation, and it varies significantly among
individuals. But if the reading of cells is too high, e.g 3 x 106, it is
almost certain that this quarter suffers from severe mastitis.

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Feed

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Milking period
• The shorter the time elapsed after the previous milking, the lower the
milk yield and the higher the fat content will be.
• Hence, evening milk usually has a higher fat content than morning
milk, the difference amounting to, say, 0.25% fat. During milking the
fat content of milk increases (e.g., from 1 to 10%), but the difference
varies markedly among cows.

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• Thank you

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