Physics and Chemistry of Hide Protein

Post
Pre-tanning Tanning tanning and
Finishing

Remove unwanted Putrescible(decay)

material and prepare to • Flexibility
suitable for tanning non-putrescible • Softness
(non-decay) • Toughness
• Strength
• Water proofness
• Abrasive resistance
• Resiliency
• Perspiration resistance
• Resistance to scratch and rubbing
• Attractive look etc
 Marie Curie (1867-1934)

 Discovers the radiation phenomenon with Antonie

Henrie Bequerel and husband Pierre Curie and
receives Nobel Prize in Physics in 1903
 Discovers radium and polonium and studies radium
and receives Nobel Prize in Chemistry in 1911
 Designs the first mobile X-ray machine
 Amazing memory and diligent work ethic
 Neglected food and sleep while at work
 Carried test tube full of radioactive isotopes in her
pocket; Stores them in desk drawer, resulting in
exposure to radiation
 Polish-French physicist and chemist
 Dies from aplastic anaemia due to massive
exposure to radiation
 PROTEIN = -amino acid -peptide bond-amino acid-

 Amino acids are the organic compounds that

is the primary unit of protein

 There are 25 different amino acids present

 Amino acids join together by a bond called as
polypeptide bond
 By using peptide bonds, amino acids join
unit by unit and form polypeptide chain
 Many such polypeptide chain is joined
together and they coil up as a single structure
called PROTEIN
 65%-95% of solid matter of hides and skins are PROTEINS

Fibrous proteins Non fibrous proteins

 Keratin  Albumin
 Collagen  Globulin
 Reticulin  Mucin
 Elastin
Character:
 Fills the interfibrillary spaces in
hides and skins
 Semi-liquid substances /
cementing substances
 Coagulated by heat
 Different techniques used to study collagen are X –ray analysis, Infra red
Spectroscopy etc

Collagen Keratin
In Greek is glue former

 Hairs, nails, hooves, horns, feathers etc
Constitutes major portion of hides and skins

Forms the
 derma or corium of hides and skins  Character
The hydrogen bond of collagen is ruptured and
  Insoluble in water
 Insoluble in dilute acids
converted into glue when digested with water at
above 60 degree celsius  Attacked slowly by strong solution of

Character:
 alkali in cold
Insoluble in organic solvent
Insoluble in water
Insoluble in dilute acid and alkali
Swells up in acid or alkali and this swelling can
be repressed by addition of common salt
Enzyme pepsin digests collagen at pH 2.0
When collagen is boiled and treated for long
time in nickel nitrate , the individual chains in
triple chain are separated
 Quite resistant to enzymes like pepsin
and trypsin (though not applicable to
softer keratins at the hair roots)
 In presence of alkali, unhairing agents
like sulphide, cyanide, amines etc can
react and dissolve keratins (this
principle is used to remove hair, nails
etc in tannery)
 Isoelectric point is pH 2.4 in acetate buffer
 Swells little over whole pH range
 Reticulin Elastin
Surrounds the collagen fibre bundles and

 Yellow connective tissue found in the
protects the collagen fibre bundles from
the chemical and physical actions of nature grain surface
Very resistant to action of boiling water
 Character
 Insoluble in organic and aqueous
and chemical reagents such as acids and solvents
alkali  Highly resistant to boiling water
Pespin can digest reticulin tissues  Digested by trypsin and unattacked by
Largely found in grain surface pepsin)
Special property to fix colloidal silver
 Mainly composed on non-polar amino
acids (elastic nature)
(argyrophylic property)
 Optically isotropic in unstretched
Roddy and O’Flaherty says
condition
reticulin = union of collagen with  Astbury says, intermediate state of
polysaccharides and other proteins like collagen and keratin
albumin, globulin and mucoids
 Acidulation:- treatment of bones with cold, dilute acid solutions to remove the
mineral matters like Calcium phosphate from bone; 18-20% of solid matter of bone
is collagen; The demineralized bone protein obtained from bone is called Ossein

 Analysis of proteins

S.No. To estimate Name of the test

1. Total nitrogen Micro Kjeldahl method
2. Amino nitrogen Van-Slyke’s method
3. Amino acid composition Paper chromatography
 Degradation of protein:-
Protein is denatured when subjected to heat at a temperature above its shrinkage
temperature; the final product is insoluble
 Chemical degradation:
• When treated with nitric acid, nitrogen gas evolves due to denaturation of
amino groups in the £-position of proteins
• C-Terminal degradation (Schlack and kumpf in 1926)
• N-Terminal degradation (Edman in 1950)
• DNP method (Sanger in 1945)

 Inactivation and removal of specific groups of collagen for the study of its
reactivity
• Deamination or diazotization (nitrous acid is used)
• Inactivation of amino group by Sangers reagent, Dinitro fluoro benzene
(DNFB)
• Inactivation of £-NH2 group by acetylation (ketene/carbon suboxide/acetic
anhydride)
• Inactivation of guanidyl group of arginine (sodium hypochlorite, acetic acid
& acetone are used)
• Inactivation of carboxyl group (by esterification)
• Inactivation of amide group (dodecyl sulphate is used to hydrolyse)
• Inactivation of hydroxyl groups (by acetylation – Greens method / sulpation
– by Frankel Conrat)
 Things to remember!

 Higher value of pK1 means weaker acidic solution

 Higher value of pK2 means stronger basic solution
(K =ionization constant of an electrolyte)
 Amino acids are +vely charged in acid media
 Amino acids are –vely charged in alkaline media

 Isoelectric point: Intermediate pH at which amino acids are electrically neutral

• Chemically inactive
• =1/2(pK1 + pK2)
• At isoelectric point the added acid or alkali changes the pH of
the solution very rapidly. The pH range where this rapid
change in pH is observed is the isoelectric point for the
protein
• The pH at which gelatin shows maximum turbidity is the
isoelectric point of gelatin
• The pH at which minimum fixation of dye to collagen is
considered as isoelectric point