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 Remove hair, nail, hooves and other keratinous matters.

 Remove some of the non collageneous proteins like MUCINs etc.

 Swell up and Split up the fibres to the desired extent.

 Remove the natural Fat and grease.

 Bring the collagen to a proper condition for satisfactory tannage.

Chemistry of Unhairing

Chemical Requirements for Liming

1) Lime [𝐶𝑎(𝑂𝐻)2 ]
2) Sodium sulphide [𝑁𝑎2 𝑆]
Reaction Mechanism
The first condition is the pH must be 12-13. if the pH is lower unhairing chemistry does not work.
Moreover the liming rate would be slow because of the hydroxyl ion concentration is reduced. At
higher pH, Liming rate is faster but danger of over swelling is greater
𝑁𝑎2 𝑆 + 𝐻2 𝑂 = 𝑁𝑎𝑂𝐻 + 𝑁𝑎𝑆𝐻

𝑁𝑎𝑆𝐻 = 𝑁𝑎+ + 𝑆𝐻 −

𝑁𝑎𝑂𝐻 = 𝑁𝑎+ + 𝑂𝐻 −

Enzymes in Unhairing (Sweating Process)

Specially for sheep skins
As per the survey conducted by ENS on 2012, leather industry is ranked as the fourth most
polluting industry in the world. This is because of the generation of huge amount of liquid and
solid wastes, out of which 60 to 70% pollutant is contributed by the effluent that is let out of after
pre-tanning operations. Out of which, the conventional liming process accounts to most of
chemical wastes both in gaseous and liquid form
Condition for Sweating Process
 15 to 20 degree Celsius temperature.
 Very humid condition @ 48 hrs exposure to bacteria.
Advantages of enzymatic treatments

 Cleaner grain, better for dyeing. @ More opening …Leather is softer.

 Remove the need for bating steps. @ Green technology.

Immunization of Keratin

Under condition of moderate alkalinity @ pH around 11and above ( in Lime solution only without sodium

sulphide)a peculiar phenomenon will take place. The alkali will disintegrate only 50% of keratin and the

remaining 50% keratin will become so much resistant to chemical action that removal of them will

become a problem. This phenomenon is technically called Immunization of Keratin.

Mechanism of Immunization

Oxidative Unhairing

Unhairing is done by strong oxidizing medium under acid condition. Chlorine Dioxide breaks the disulphur bonds

producing Keratin sulphonic acid and free chlorine. Keratin sulphonic acid portion is then converted into water

soluble material, in weakly acid media the hair and the epidermis are removed by the mechanical action of the

drum itself. The liberated Chlorine absorbed by collagen. Best results obtained at a buffered pH between 3 – 3.5

is maintained by using glycolic and slight sulphuric acid solution.

𝟒 𝐑 − 𝐒 − 𝐒 − 𝐑 + 𝟏𝟎𝐂𝐥𝐎𝟐 + 𝟒𝐇𝟐 𝐎 = 𝟖𝐑 − 𝐒𝐎𝟑− + 𝟖𝐇 + + 𝟓𝐂𝐥𝟐

 Lime Blast

 The heterogeneous reaction between solid lime, which has been driven into the grain surface of the pelt. The

gaseous carbon dioxide in the atmosphere, resulting in the formation of solid crystals of Calcium carbonate.

 𝐶𝑎(𝑂𝐻)2 + 𝐶𝑂2 = 𝐶𝑎𝐶𝑂3 + 𝐻2 𝑂

 At high pH, insoluble Calcium carbonate is formed, potentially creating lime blast.

 At lower pH (during deliming), with continuous addition of 𝐶𝑂2 , soluble calcium bicarbonate is formed.

 𝐶𝑎𝐶𝑂3 + 𝐶𝑂2 + 𝐻2𝑂 = [{𝐶𝑎(𝐻𝐶𝑂)3 }2]

Cow Raw Hide

Structure of Hides and skins

Hide/Skin Morphology.

The primary morphological function of the hide or skin during the life of the animal is to allow for thermo-regulation,

gaseous exchange, protection & provide cover.

(1) Chemical structure

(2) Anatomical structure


The chemical composition of fresh hides and skins falls approximately within the following limits:

• Water 60%-65%

• Protein 25%-30%

• Fats 5%-10%

ANATOMICAL STRUCTURE-: The hides and skins are mainly consists of three layers.

i) Epidermis or Outer layer

ii) Dermis or Corium layer

iii) Hypodermis or Flesh layer

(i) Epidermis or Outer layer-

It is comparatively thinner than corium. Its thickness is only 1—2% of the total thickness of the entire skin. It divided itself into two layer

of cells – the Outer layer and inner or soft layer.

The inner layer takes their food in the form of blood with corium layer. When thin food transferred to outer layer is late and all the cells

become dead as the form of Dandruff.

(ii) Dermis- This layer consists of two layer. (a) Grain layer (b) Corium layer.

(a) Grain layer-: Grain layer is also known as corium minor. It is top of the corium about one fifth of the total thickness. This layer has a

characteristic, grain pattern due to the presence of hair follicles. The grain pattern depends upon the density and structure of the hair


(b) Corium layer-: This is the main layer of hides or skins constituting about 98% of its thickness. The hair papilla contains nerves and

blood vessels. Due to the blood circulations of animals body a lot of cells are produced. As new cells are formed the older ones are

pushed upward through the follicles forming the hair. The rate of growth of the hair is determined by the rate at which the cell

surrounding the papilla reproduce. The newly formed cell of the hair substance are soft and slowly moving upward become elongated

and hardened. In forming the hair they take the shape of the follicle. At the bottom of the hair follicle the hair root is expanded and

has a bulb like shape. The portion of the hair above the surface of the skin is called shaft and lower portion the root.

The hair is also divided into three layers.

(i) Hair cuticle-: Upper hair.

(ii) Medulla -: This is surrounded by spindle-shaped cells which contains cortex and it has pigment colour. The pigment gives colour to

the hair.

iii)Fat Glands -: The fat glands are made of cells having nucleus and are arranged like grapes in a bunch. The oil present can act as a

barrier to water penetration during the soaking operation.

The fat glands on the other hand, maintain the body temp. by covering the body with a film of oils and thus regulate the surface

evaporation of water. In structure corium is entirely different from epidermis.

Hair is the typical epidermis structure and is entirely a product of the epidermis. The cell of the epidermis dip down into the body of

the dermis and form a hair pocket, in which the hair grows
(c) Hypodermis or Flesh layer-: This layer is found below the dermis layer. It is the loose connective tissue lying between the hide

or skin and the actual body of the animal. At the time of flaying a part of this tissue remain attached to the hide or skin.

The flesh is removed in fleshing operation after liming.

Defects of Hides and Skins-: Very few hides and skins are free from defects. Defects which occur in hides and skins can be many and

each defects is due to a specific cause originating either when the animals were alive or after their death. The former is called anti-

mortem and the later post-mortem defects.

Proteins-: Proteins are structural units of living thing containing carbon, hydrogen, oxygen and sulphare

(a) Structural protein-: (Fibrous proteins) are four types.

(i) Keratin (ii) Collagen (iii) Elastin (iv) Reticulin

(i) Keratin -: it is dissolved with lime liquor and Na2S it will be loose and when we apply the mechanical operation in pelt it will be totally

removed by the pelt.

(ii) Collagen -: This is the most important proteins in hides and skins and occurs in them in the largest amount. It is the protein constituents of the

white fibres of the corium and forms about 30.33% of the weight of the whole fresh skins.

Composition of dried collagen is----

Carbon—50.2%, Hydrogen – 6.4%, Nitrogen – 17.8%, Oxygen and Sulphur – 25.4%

Collagen is a complex protein containing various amino-acids. It is insoluble in organic solvent, water and dilute acids and alkalis at ordinary

temp. Collagen which combines with tanning substances and is converted into leather.

(iii)Elastin -:The elastin is removed by enzymatic treatment in the bating operation.

(iv) Reticuline-: Reticuline is attached by strong alkali treatment and may be removed by sodium sulphide.

(b) Non structural protein-: These are three types-

(i) Albumins-: soluble in water and remove during the time of Soaking.

(ii) Globulins-: When salt is added in raw skin it is present in skin but when we wash it for removal of salt in soaking operation it is automatically

removed with skin fibres.

(iii) Mucins-; It is soluble in diluted alkali and it is removed in living process with addition of lime.
Collagen is the most abundant protein in our bodies, especially type 1 collagen. It's found in muscles, bones, skin, blood vessels, digestive system

and tendons. It's what helps give our skin strength and elasticity, along with replacing dead skin cells. The collagen protein is composed of a

triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). The

amino acid composition of collagen is a typical for proteins, particularly with respect to its high hydroxyproline content. All amino acids found

in proteins have this basic structure, differing only in the structure of the R-group or the side chain.. The simplest, and smallest, amino acid found

in proteins is glycine for which the R-group is a hydrogen (H).

All amino acids found in proteins have this basic structure, differing only in the structure of the R-group or the side chain.. The simplest, and

smallest, amino acid found in proteins is glycine for which the R-group is a hydrogen (H).

Zwitterions :

The α-carboxylic acid group of amino acids is a weak acid, meaning that it releases a hydrogen (such as a proton) at

moderate pH values. In other words, carboxylic acid groups (−CO2H) can be deprotonated to become

negative carboxylates (−CO2− ). The negatively charged carboxylate ion predominates at pH values greater than the pKa of

the carboxylic acid group (mean for the 20 common amino acids is about 2.2, see the table of amino acid structures above).

In a complementary fashion, the α-amine of amino acids is a weak base, meaning that it accepts a proton at moderate pH

values. In other words, α-amino groups (NH2−) can be protonated to become positive α-ammonium groups (+NH3−). The

positively charged α-ammonium group predominates at pH values less than the pKa of the α-ammonium group (mean for the

20 common α-amino acids is about 9.4).

Because all amino acids contain amine and carboxylic acid functional groups, they share amphiproteic properties. Below

pH 2.2, the predominant form will have a neutral carboxylic acid group and a positive α-ammonium ion (net charge +1), and

above pH 9.4, a negative carboxylate and neutral α-amino group (net charge −1). But at pH between 2.2 and 9.4, an amino

acid usually contains both a negative carboxylate and a positive α-ammonium group, as shown in structure, so has net zero

charge. This molecular state is known as a zwitterion, from the German Zwitter meaning hermaphrodite or hybrid

AMINO ACIDs An amino acid is a type of organic acid that contains a carboxyl functional group (-COOH) and an amine

functional group (-NH2) as well as a side chain (designated as R) that is specific to the individual amino acid. Amino acids are considered to be the building

blocks of polypeptides and proteins. The elements found in all amino acids are carbon, hydrogen, oxygen, and nitrogen.
Amino acids may contain other elements on their side chains. Shorthand notation for amino acids may be either a three-letter abbreviation or a single

letter. For example, valine may be indicated by V or val; histidine is H or his.

Amino acids may function on their own, but more commonly act as monomers to form larger molecules. Linking a few amino acids forms peptides. A chain

of many amino acids is called a polypeptide. Polypeptides may become proteins.

The process of producing proteins based on an RNA template is called translation. Translation occurs in ribosomes of cells.


The amino acids most commonly memorized and encountered in biochemistry are:

 * Glycine, Gly, G * Valine, Val, V *Leucine, Leu, L *Isoeucine, Leu, L *Proline, Pro, P *Threonine, Thr, T *Cysteine, Cys, C

*Methionine, Met, M * Phenylalanine, Phe, F *Tyrosine, Tyr, Y * Tryptophan, Trp, W *Arginine, Arg, R *Aspartate, Asp, D

Glutamate, Glu, E *Aparagine, Asn, N *Glutamine, Gln, Q *Aparagine, Asn, N

An amino acid is a type of organic acid that contains a carboxyl functional group (-COOH) and an amine functional group (-NH2) as well as a side chain

(designated as R) that is specific to the individual amino acid. Amino acids are considered to be the building blocks of polypeptides and proteins. The

elements found in all amino acids are carbon, hydrogen, oxygen, and nitrogen.