NATURAL POLYMERS MU SCI 9 2018
1
NATURAL POLYMERS

 FIBROUS PROTEINS I
COLLAGEN
Dr. Ladislav Pospíšil
January 9/2018

Time schedule
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
2
LECTURE
SUBJECT
1
Introduction to the subject – Structure & Terminology of nature polymers, literature
2
Derivatives of acids – natural resins, drying oils, shellac
3
Waxes
4
Plant (vegetable) gums, Polyterpene – natural rubber (extracting, processing and modification),
Taraxacum_kok-saghyz
5
Polyphenol  – lignin, humic acids
6
Polysaccharides I – starch
7
Polysaccharides II – celullose
8
Protein fibres I
9
Protein fibres II
10
Casein, whey, protein of eggs
11
Identification of natural polymers
Laboratory methods of natural polymers’ evaluation

1.Repeating of the Basic Terminology related to PROTEINS (Lecture 8)
2.FIBROUS PROTEINS
3.Manufacture of the Gelatine and Animal Glue
4.Tanning industry
§Skin (Hide) versus Leather
§Tanning Procedure
5.Leather and Conservator – Restorer
6.
1.
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
3

1.Repeating of the Basic Terminology related to PROTEINS (Lecture 8)
•
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
4

Structure Hierarchie of Peptides and Proteins
•Primary structure – the Amino acids Sequence of the Protein •Secondary structure – No covalent
Interactions in the Backbone of the one Polypeptide (Protein) Chain, usually the near Parte of the
Backbone (a – Helix and/or b - Sheet) •Tertiary structure – various Interactions between the
Backbones of more then the one Polypeptide (Protein) Chain of Chains or remote NO neighbouring)
Segments of one Chain •Quaternary structure – Interactions between the Chain Bundles, between the
Tertiary structures
•Tertiary & Quaternary Structures – we give attention to this in the next Lesson!
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
5

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
6
CAM00548.jpg

PRIMARY STRUKTURE of Proteine I
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
7
Protein_primary_structure_svg.png

PROTEIN SECONDARY STRUCTURE I
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
8
Hierarchie struktur bílkovin 001.jpg

PROTEIN SECONDARY STRUCTURE II A
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
9
Left-handed Helix
Sekundární struktura bílkovin 001.jpg

Proteins dividing – the Occurrence of other Components in Macromolecule accordingly
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
10
•Simple protein – they are broken by Hydrolysis to Amino acids only
•Compound protein – they are broken by Hydrolysis to Amino acids, Saccharides, Fats, …
–LIPOPROTEINE (Fats)
–GLYKOPROTEINE (Saccharides)
–FOSFOPROTEINE (Phosphate groups > KASEIN)
–CHROMOPEROTEINE (Colorants, e.g.  Haemoglobin, Melamine)
–
•

Proteins dividing – Macromolecules’ Solubility in Water of accordingly
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
11
•SOLUBLE (SFEROPROTEINE)
–HEAT > COAGULATION
–Albumin > Egg white
–Glutelin > Glutelin from Wheat
•UNSOLUBLE (SKLEROPROREINE)
–Keratin a and b
–Collagen
–
–
•

Proteins dividing – Macromolecules’ Shape and Supermolecular Structure accordingly
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
12
•FIBRILAR > natural/genuine Silk, Hair, animal Hair, Muscles, fibrous connective Tissue •GLOBULAR >
ENZYM, Egg white, Milk white, INSULIN, …
•

2.FIBROUS PROTEINS
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
13

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
14
Primary_and other structures bílkoviny 12102015.png
Interaction in ONE  MACROMOLECULE
Interaction between  MORE THEN ONE PROTEIN
Two possible  Structures
Interaction between  MORE THEN ONE MACROMOLECULE

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
15
Levels_of_structural_organization_of_a_protein_svg.png
Functional proteins have four levels of structural organization:
1) Primary Structure : the linear structure of amino acids in the polypeptide chain
2) Secondary Structure : hydrogen bonds between peptide group chains in an alpha helix or beta
3) Tertiary Structure : three-dimensional structure of alpha helixes and beta helixes folded
4) Quaternary Structure : three-dimensional structure of multiple polypeptides and how they fit
together
Interaction between  MORE THEN ONE MACROMOLECULE

DENATURATION and COAGULATION of Proteines
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
16
DENATURATION IS THE DISINTEGRATION OF THE PROTEIN STRUCTURE
COAGULATION is the Formation  of the UNSOLUBLE  Protein Form from the initially SOLUBLE Protein
Form by Influence of the Physical  Factors, e.g. Heat (e.g. Egg White at Cooking Egg) or by
Influence of the Chemical Reagents.
COAGULATION is one of the Forms of DENATURATION
COAGULATION BY HEAT IS USUALLY IRREVERSIBLE
Protein denaturation & Coagulation 001.jpg

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
17
Process_of_Denaturation_svg.png
Process of Denaturation:
1)Functional proteins showing a quaternary structure
2)When heat is applied it alters the intramolecular bonds of the Proteins’
3)Unfolding of the polypeptides (Proteins)
1
2
3

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
18
Denaturation is a process in which proteins or nucleic acids lose the quaternary structure,
tertiary structure and secondary structure which is present in their native state, by application
of some external stress or compound such as a strong acid or base, a concentrated inorganic salt,
an organic solvent (e.g., alcohol or chloroform), radiation or heat.[3] If proteins in a living
cell are denatured, this results in disruption of cell activity and possibly cell death. Denatured
proteins can exhibit a wide range of characteristics, from loss of solubility to communal
aggregation
Protein_Denaturation.png 290px-Chemical_precipitation_diagram_svg.png
COAGULATION BY HEAT
ANALOGY with paper Clips

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
19
IUPAC definition
Process of partial or total alteration of the native secondary, and/or tertiary, and/or quaternary
structures of proteins or nucleic acids resulting in a loss of bioactivity.
Note 1:
Denaturation can occur when proteins and nucleic acids are subjected to elevated temperature or to
extremes of pH, or to nonphysiological concentrations of salt, organic solvents, urea, or other
chemical agents.
Note 2:
An enzyme loses its catalytic activity when it is denaturized.[2]

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
20
DENATURATION CAN BE  REVERSIBLE > RENATURATION
denaturave X RENATURACE BÍLKOVIN 28052017.jpg
REVERSIBLE DENATURATION (=RENATURATION) of the Globular Protein with marked –S-S- Bonds
RENATURATION
DENATURATION

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
21
Reversibility and irreversibility
In very few cases, Denaturation is reversible (the proteins can regain their native state when the
denaturing influence is removed). This process can be called Renaturation.
This understanding has led to the notion that all the information needed for proteins to assume
their native state was encoded in the primary structure of the protein, and hence in the DNA that
codes for the protein, the so-called "Anfinsen's thermodynamic hypothesis".
One example of Renaturation is that an egg white can be uncooked using vitamin C or sodium
borohydride (VERY CURIOUS PROCEDURE).

EXAMPLES Reversibility and Irreversibility
COAGULATION
•REVERSIBLE
•GELLATINE (it is  COLLAGEN  with lower  MW) •Temperature Increasing > Dissolving > SOL
•Temperature Decreasing > Solidification > GEL •TEMPERATURE OF COAGULATION = TEMPERATURE, at which
(at given Concentration)  COAGULATION occurs, it is Transition  SOL >> GEL occurs by Temperature
Decreasing
•IRREVERSIBLE
•EGG WHITE
•Temperature Increasing (over approx. 60 °C) > Solidification > Transition SOL >> GEL •TEMPERATURE
OF COAGULATION = TEMPERATURE, at which (at given Concentration)  COAGULATION occurs, it is
Transition  SOL >> GEL occurs by Temperature Increasing
•
•
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
22

COLLAGEN as the EXAMPLE of
 the FIBROUS PROTEINS
•SKIN, BONES, CARTILAGE, TENDON, VASCULAR WALLS, CORNEA, …
•Glycine 27 % w/w, Proline 15 % w/w, Sequnce (GLY-X-Y)n
•15 Types of COLLAGENS have been described up to now, they are different as to the Occurence and
the Abundance of the particular Aminoacids
•TROPOCOLLAGEN –THREE mutually coiled Backbones
•TROPOCOLLAGEN > SELF ARRANGEMENT into  COLLAGEN FIBRILS > Crosslinking via Hydrogen Bonds  >
COLLAGEN FIBERS > BUNDLES of FIBERS •DEGRADATION of COLLAGEN by ENZYME COLLAGENASE > SKIN AGEIN
•
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
23

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
24
GLYCINE
 (Gly, G)
Amminoacido_glicina_formula.png
PROLINE (Pro, P)
800px-Amminoacido_prolina_formula_svg.png
LYSINE
 (Lys, L)
Amminoacido_lisina_formula.png
This Group of the Amino acids is important for the Hydrogen Bonds between the COLLAGEN Molecules

PRIMARY STRUCTURE Proteins II – COLLAGEN as the EXAMPLE (Numbers of particular Amino acids in the
 Macromolecules are given bellow )
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
25
AMK
Typ I
Typ II
Typ III
Typ IV
Typ V
alfa1
alfa2
A
B
3-Hyp
1,0
0,0
2,0
—
11
2,5
2,9
4-Hyp
96
86
99
125
130
109
109
Asp
46
44
42
42
51
51
50
Thr
20
20
20
13
23
26
19
Ser
42
43
27
39
37
31
26
Glu
74
66
89
71
84
84
91
Pro
129
113
121
107
61
97
118
Gly
330
336
333
350
310
319
322
Ala
112
102
100
96
33
52
46
Val
20
32
18
14
29
27
18
Gys 1
-
-
-
2
8
-
-
Met
8
6
9
8
10
11
8
Ile
6
16
9
13
30
16
19
Leu
18
32
26
22
54
35
39
Tyr
2
2
1
3
6
18
2,1
Xhe
12
10
13
8
27
14
12
Hyl
4,3
8
20
30
10
18
20
Lys
30
22
2
6
10
11
7,3
Arg
49
51
51
46
33
68
50

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
26
Type
Molecular  Composition
OCCURENCE
I
[alfa1(I)]2alfa2
SKIN, BONES, CARTILAGE, TENDON, VASCULAR WALLS, CORNEA
II
[alfa1(II)]3
Hyalin CARTILAGE
III
[alfa1(III)]3
The same as the Type I, formely called Retikuline
IV
[alfa1(IV)]3
Basal Membranes
V
Neoplasm etc.
VI
Interstitial Tissues
VII
Epithel Tissues
VIII
Some Endotel Cells
IX
CARTILAGE together with Type II
X
Part of the Hypertrofic and Mineralised CARTILAGE s
XI
CARTILAGE
XII
OCCURENCE together with Types I and III
COLLAGEN OCCURENCE IN HUMAN BODY

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
27
Glu-Met-Ser-Tyr-Gly-Tyr-Asp-Glu-Lys-Ser-Ala-Gly-Val-Ser-Val-Pro–
Gly-Pro-Met-Gly-Pro-Ser-Gly-Pro-Arg-Gly-Leu-Hyp-Gly-Pro-Hyp-Gly-Ala-Hyp-Gly-Pro-Gln-Gly-Phe-Gln-Gly
-Pro-Hyp-
Gly-Glu-Hyp-Gly-Glu-Hyp-Gly-Ala-Ser-Gly-Pro-Met-Gly-Pro-Arg-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly-Lys-Asn-Gly
-Asp-Asp-
Gly-Glu-Ala-Gly-Lys-Pro-Gly-Arg-Hyp-Gly-Gln-Arg-Gly-Pro-Hyp-Gly-Pro-Gln-Gly-Ala-Arg-Gly-Leu-Hyp-Gly
-Thr-AJa-
Gly-Leu-Hyp-Gly-Met-Hyl-Gly-His-Arg-Gly-Phe-Ser-Gly-Leu-Asp-Gly-Ala-Lys-Gly-Asn-Thr-Gly-Pro-AIa-Gly
-Pro-Lys-
Gly-Glu-Hyp-Gly-Ser-Hyp-Gly-Glx-Asx-Gly-Ala-Hyp-Gly-Gln-Met-Gly-Pro-Arg-Gly-Leu-Hyp-Gly-Glu-Arg-Gly
-Arg-Hyp-
Gly-Pro-Hyp-Gly-Ser-Ala-Gly-Ala-Arg-Gly-Asp-Asp-Gly-Ala-Val-Gly-Ala-Ala-Gly-Pro-Hyp-Gly-Pro-Thr-Gly
-Pro-Thr-
Gly-Pro-Hyp-Gly-Phe-Hyp-Gly-Ala-Ala-Gly-Ala-Lys-Gly-Glu-Ala-Gly-Pro-Gln-Gly-Ala-Arg-Gly-Ser-Glu-Gly
-Pro-Gln-
Gly-Val-Arg-Gly-Glu-Hyp-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Ala-Ala-Gly-Pro-Ala-Gly-Asn-Hyp-Gly-Ala-Asp-Gly
-Gln-Hyp-
Gly-Ala-Lys-Gly-Ala-Asn-Gly-Ala-Hyp-Gly-Ile-Ala-Gly-Ala-Hyp-Gly-Phe-Hyp-Gly-Ala-Arg-Gly-Pro-Scr-Gly
-Pro-Gln-
Gly-Pro-Ser-Gly-Ala-Hyp-Gly-Pro-Lys-Gly-Asn-Ser-Gly-Glu-Hyp-Gly-Ala-Hyp-Gly-Asn-Lys-Gly-Asp-Thr-Gly
-Ala-Lys-
Gly-Glu-Hyp-Gly-Pro-Ala-Gly-Val-Gln-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Glu-Glu-Gly-Lys-Arg-Gly-Ala-Arg-Gly
-Glu-Hyp-
Gly-Pro-Ser-Gly-Leu-Hyp-Gly-Pro-Hyp-Gly-Glu-Arg-Gly-Gly-Hyp-Gly-Ser-Arg-Gly-Phe-Hyp-Gly-Ala-Asp-Gly
-Val-Ala-
Gly-Pro-Lys-Gly-Pro-Ala-Gly-Glu-Arg-Gly-Ser-Hyp-Gly-Pro-Ala-Gly-Pro-Lys-Gly-Ser-Hyp-Gly-Glu-Ala-Gly
-Arg-Hyp-
Gly-Glu-Ala-Gly-Leu-Hyp-Gly-Ala-Lys-Gly-Leu-Thr-Gly-Ser-Hyp-Gly-Ser-Hyp-Gly-Pro-Asp-Gly-Lys-Thr-Gly
-Pro-Hyp-
Gly-Pro-Ala-Gly-Gln-Asp-Gly-Arg-Hyp-Gly-Pro-Ala-Gly-Pro-Hyp-Gly-Ala-Arg-Gly-Gln-Ala-Gly-Val-Met-Gly
-Phe-Hyp-
Gly-Pro-Lys-Gly-Ala-Ala-Gly-Glu-Hyp-Gly-Lys-AIa-Gly-Glu-Arg-Gly-Val-Myp-Gly-Pro-Hyp-Gly-Ala-Val-Gly
-Pro-Ala-
Gly-Lys-Asp-Gly-Glu-A]a-Gly-Ala-Gln-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Pro-A,.-Gly-Glu-Arg-Gly-Glu-Gln-Gly
-Pro-Ala-
Gly-Ser-Hyp-Gly-Phe-Gln-Gly-Leu-Hyp-GIy-Pro-Ala-Gly-Pro-Hyp-Gly-Glu-Ala-Gly-Lys-Hyp-Gly-Glu-Gln-Gly
-Val-Hyp-
Gly-Asp-Leu-Gly-Ala-Hyp-Gly-Pro-Ser-Gly-Ala-Arg-Gly-Glu-Arg-Gly-Phe-Hyp-Gly-Glu-Arg-Gly-Val-Glu-Gly
-Pro-Hyp-
Gly-Pro-Ala-GJy-Pro-Arg-Gly-Ala-Asn-Gly-Ala-Hyp-Gly-Asn-Asp-Gly-Ala-Lys-Gly-Asp-Ala-Gly-Ala-Hyp-Gly
-Ala-Hyp-
Gly-Ser-Gin-Gly-Als-Hyp-Gly-Leu-Gin-Gly-Met-Hyp-Gly-Glu-Arg-Gly-Ala-Ala-Gly-Leu-Hyp-Gly-Pro-Lys-Gly
-Asp-Arg-
Gly-Asp-Ala-Gly-Pro-Lys-Gly-Aln-Asp-Gly-Ala-Pro-Gly-Lys-Asp-Gly-Val-Arg-Gly-Leu-Thr-Gly-Pro-Ile-Gly
-Pro-Hyp-
Gly-Pro-Ala-Gly-Ala-Hyp-Gly-Asp-Lys-Gly-Glu-Ala-Gly-Pro-Ser-Gly-Pro-Ala-Giy-Thr-Arg-Gly-Ala-Hyp-Gly
-Asp-Arg-
Gly-Glu-Hyp-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Phe-Ala-Gly-Pro-Hyp-Gly-Ala-Asp-Gly-Gln-Hyp-Gly-Ala-Lys-Gly
-Glu-Hyp-
Gly-Asp-Ala-Gly-Ala-Lys-Gly-Asp-Ala-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Pro-Ala-Gly-Pro-Hyp-Gly-Pro-Ile-Gly
-Asn-Val-
Gly-Ala-Hyp-Gly-Pro-Hyl-Gly-Ala-Arg-Gly-Ser-Ala-Gly-Pro-Hyp-Gly-Ala-Thr-Gly-Phe-Hyp-Gly-Ala-Ala-Gly
-Arg-Val-
Gly-Pro-Hyp-Gly-Pro-Ser-Gly-Asn-Ala-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Lys-Glu-Gly-Ser-Lys-Gly
-Pro-Arg-
Gly-Glu-Thr-Gly-Pro-Ala-Gly-Arg-Hyp-Gly-Glu-Val-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly-Pro-Ala-Gly-Glu-Lys-Gly
-Ala-Hyp-
Gly-Als-Asp-Gly-Pro-Ala-Gly-Ala-Hyp-Gly-Thr-Pro-Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln-Arg-Gly-Val-Val-Gly
-Leu-Hyp-
Gly-Gln-Arg-Gly-Glu-Arg-Gly-Phe-Hyp-Gly-Leu-Hyp-Gly-Pro-Ser-Gly-Glu-Hyp-Gly-Lys-Gln-Gly-Pro-Ser-Gly
-Ala-Ser-
Gly-Glu-Arg-Gly-Pro-Hyp-Gly-Pro-Met-Gly-Pro-Hyp-Gly-Leu-AlarGly-Pro-Hyp-Gly-Glu-Ser-Gly-Arg-Glu-Gly
-Ala-Hyp-
Gly-Ala-Glu-Gly-Ser-Hyp-Gly-Arg-Asp-Gly-Ser-Hyp-Gly-Ala-Lys-Gly-Asp-Arg-Gly-Glu-Thr-Gly-Pro-Ala-Giy
-Ala-Hyp-
Gly-Pro-Hyp-Gly-Ala-Hyp-Gly-Ala-Hyp-Gly-Pro-Val-Gly-Pro-Ala-Gly-Lys-Ser-Gly-Asp-Arg-Gly-Glu-Thr-Gly
-Pro-Ala-
Gly-Pro-Ile-Gly-Pro-Val-Gly-Pro-Ala-Gly-AIa-Arg-Gly-Pro-Ala-Gly-Pro-Gln-Gly-Pro-Arg-Gly-Asx-Hyl-Gly
-Glx-Thr-
Gly-Glx-Glx-Gly-Asx-Arg-Gly-Ile-Hyl-Gly-His-Arg-Gly-Phe-Ser-Gly-Leu-Gln-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly
-Ser-Hyp-
Gly-Glu-Gln-Gly-Pro-Ser-Gly-Ala-Ser-Gly-Pro-Ala-GIy-Pro-Arg-Gly-Pro-Hyp-Gly-Ser-Ala-Gly-Ser-Hyp-Gly
-Lys-Asp-
Gly-Leu-Asn-Gly-Leu-Hyp-Gly-Pro-Ile-Gly-Hyp-Hyp-Gly-Pro-Arg-Gly-Arg-Thr-Gly-Asp-Ala-Gly-Pro-Ala-Gíy
-Pro-Hyp-
Gly-Pro-Hyp-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly-Pro-Pro-
Ser-Gly-Gly-Tyr-Asp-Leu-Ser-Phe-Leu-Pro-Gin-Pro-Pro-Gin-Gin-Glx-Lys-Ala-His-Asp-Gly-Gly-Arg-Tyr-Tyr
Amino acids Sequence alfa1 Chain of the Skin Collagen (N-terminal and C-terminal Regions are given
separately)

PROTEIN SECONDARY STRUCTURE II B
January 8/2018
NATURAL POLYMERS MU SCI 8 2018
28
img779.jpg
Left-handed a Helix
b Folded Sheet

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
29
Sekundární struktura bílkovin 018.jpg
b Folded Sheet

SECONDARY STRUCTURE of Proteins II
COLLAGEN as the EXAMPLE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
30
The Conformation of the SECONDARY STRUCTURE (a-Helix, b- Sheet, Statistic Coil) has the Influence
on the IR Wave Number of the Amide Group Peak in the IR Spectrum.
It is a bit unusual Wave Number Unit, but it is right!
It is the same Figure as the usual Unit cm-1.
COLLAGEN is the  a-Helix.
IR Spectrum (Wave Number) of the Amide Bond (102 m-1)
Structure
Amide I
Amide II
a - Helix
1650
1652
1515
1546
b-Structure
1630
1645
1530
1550
Statistic Coil
1656
1535

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
31
Sekundární struktura bílkovin 016.jpg
These Interactions are in the ONE MOLECULE, so it is SECONDARY STRUCTURE

TERTIARY STRUCTURE of Proteins II
 COLLAGEN as the EXAMPLE
 three Coils arranged to the next combined coiled Chain
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
32
http://www.hypro.cz/img/kolagen/molekula.gif http://www.hypro.cz/img/kolagen/model.gif

TERTIARY STRUCTURE of Proteins II
 COLLAGEN as the EXAMPLE
 three Coils arranged to the next combined coiled Chain
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
33
http://www.hypro.cz/img/kolagen/tropomol.gif
Schematic representation of the COLLAGEN Triple helix Molecule. The marked Intervals on the right
(a, b, c, d) are 67 nm, what is the Distance over which are the particular Molecules in the Triple
helix shifted each to another .

TERTIARY STRUCTURE of Proteins II
 COLLAGEN as the EXAMPLE
 three Coils arranged to the next combined coiled Chain
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
34
sekundární & terciární struktura KOLAGENU 002.jpg
SECUNDARY STRUCTURE

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
35
Sekundární struktura bílkovin 015.jpg
Sekundární struktura bílkovin 014.jpg Sekundární struktura bílkovin 013.jpg

TERTIARY STRUCTURE Proteins V
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
36
Sekundární struktura bílkovin 008.jpg

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
37
Sekundární struktura bílkovin 012.jpg Sekundární struktura bílkovin 011.jpg

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
38
Sekundární struktura bílkovin 010.jpg

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
39
Collagen_biosynthesis_(en).png
NON-HELIX Prolongation
= it is NOT  coiled to Helix
By NON-EZYMATIC Degradation of the NON-HELIX Prolongation
Is increased the BIOCOMPATIBILY, it is the ANTIGENITY is suppressed

QUOTERNARY STRUCTURE Proteins I
 CELULASE as the EXAMPLE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
40
The Interaction between  the folded up Fibrous Structures coiled to the Helix as the TERTIARY
STRUCTURE already.
An Example – COLLAGEN -   they are PARALEL BUNDLES of TERTIARY STRUCTURE.  It is called ASSOCIATES
ARISING sometimes.
It is typical for the ENZYME, where they are not PARALEL BUNDLES, but they are GLOBULAR STRUCTURES.
Cellulase_1JS4 PICTURE WIKI ENG.jpg
One Enzyme from the  „CELULASE“ Group

QUOTERNARY STRUCTURE Proteins I
 COLLAGEN as the EXAMPLE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
41
The Interaction between  the folded up Fibrous Structures coiled to the Helix as the TERTIARY
STRUCTURE already.
An Example – COLLAGEN -   they are PARALEL BUNDLES of TERTIARY STRUCTURE.
http://www.hypro.cz/img/kolagen/mikrofib.gif
The Microfibril Model created as the Consequence of Interaction polar an d hydrophobic Side Chains.
Five Tropocollag Molecules are shifted each to another 4 nm here and they are creating a Cylinder
Structure so.

 COLLAGEN – Hierarchy of the Structures
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
42
img799.jpg
SECONDARY
 = one Helix
TERTIARY – two different Representations
THREE HELIXES
Left Picture – SIMPLIFIED
RIGHT PICTURE - REALITY
QUOTERNARY

The EXAMPLE of Creation of the QUOTERNARY STRUCTURE
- HEMOGLOBINE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
43
img800.jpg img801.jpg
Three Parts -  Tertiary Structures, which create the QUOTERNARY STRUCTURE
QUOTERNARY STRUCTURE

QUOTERNARY STRUCTURE
Proteinů III COLLAGEN as the EXAMPLE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
44
The Interaction between  the folded up Fibrous Structures coiled to the Helix as the TERTIARY
STRUCTURE already.
An Example – COLLAGEN -   they are PARALEL BUNDLES of TERTIARY STRUCTURE.
These PARALEL BUNDLES of TERTIARY STRUCTURE form QUOTERNARY STRUCTURE
http://www.hypro.cz/img/kolagen/vlakna.jpg
COLLAGEN -   PARALEL BUNDLES of TERTIARY STRUCTURE

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
45
Sekundární struktura bílkovin 017.jpg

 COLLAGEN – Cross Bonds IN VIVO
•The Bonds are based on the Reactions of the  Oxidised – HN2 in Lysine with –OH Group and Reactions
between arisen Groups •Reactions are mainly INTRAMOLECULAR,  but also  INTERMOLECULAR •There is
less Cross Bonds in so called YOUNG  COLLAGEN  > Higher Solubility •There is more Cross Bonds in so
called OLD  COLLAGEN  > Lower Solubility
•Lysine
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
46
Amminoacido_lisina_formula.png

 COLLAGEN – REACTIONS IN VITRO 1
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
47
• ACYLATION using acetanhydride
• Esterification (various reagents)
• Deamination (-NH2 > -OH)
• Deguanidisation
(Removing the End from the Arginine
and cleavage H2N – CO – NH2)
141px-Guanidin_svg.png
guanidin
Amminoacido_arginina_formula.png

COLLAGEN – REACTIONS IN VITRO 2
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
48
SÍŤOVÁNÍ KOLAGENU 001.jpg
• Aldehydic Condensation
• Oxidation by Periodate >
  5-hydroxylysine > ALDEHYDE > REACTION

 COLLAGEN – Reaction with Synthetic Polymers IN VITRO 1
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
49
Effort to enhance the COMPATIBILITY of the NATURAL & SYNTHETIC POLYMERS

 COLLAGEN – Hierarchy of Structures & USE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
50
Structure Level
Branch of Use/Products
Fibres’ Tissue
Leather, Wounds’ Covering, Skin Implants, Vessels Substitutes,
Fibres
Casing for Meat Products, Packaging Films, Membranes, Powder for Wounds’ Covering, Capsule for
Medicines
Fibrils
Biocompatible Plastic or Ceramic Composites for Surgery
Macromolecules
Native Collagen, Derivatives of Collagen for Medicine & Cosmetic Use
Polypeptides
Animal Glue, Gelatine, Hydrolysate of Collagen, Capsule for Medicines, Thickener, Animal feed ...

 COLLAGEN – Medicine Use 1
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
51
COLLAGEN Medicine Preparations – Sort and Use accordingly
Products
Use
Catgut
Surgery Sewing, Wounds’ Covering, Wounds’ Covering
Fibres –
·From the Solutions
·From the Suspensions
·From the Membranes
Skin Implants, Haemostatics, Vessels Substitutes,
Collagen Sheets –
·Genuine skin
·Membranes
·Nonwoven Textiles
·Foams
·Sponge
Implants, Fillers for Implants
Vessels/Organs
Connective tissues healing (“Reparations”), Tissues’ Glue
Collagen Powder,  Glue, Sprays, Face Powder
Face Skin Care

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
52
CATGUT chirurgické nitě vstřebatelné z KOLAGENU 001.jpg
•  Resorption is controlled by chromium salts Crosslinking at Tanning > slower Biodegradation
(Resorption ) in living Organism
•  UNCROSSLINKED by chromium salts Crosslinking at Tanning > FASTER Biodegradation (Resorption ) in
living Organism

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
53
The Discussion is on stream now, if the COLLAGEN  degradated Chains are harmful for the Humans
Organism or not.
It is sought in some Sources now, that COLLAGEN „CATGUT“  is allowed for the Veterinary use only.
There are not any such bans for „CATGUT“ at the Internet pages of the „CATGUT“  Suppliers up to now
(year 2018).

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
54
Catgut Chromic Suture | Catgut suture
• Catgut or gut suture is an absorbable suture usually manufactured from the intestine of sheep or
goat.
• Catgut suture are composed of highly purified connective tissue derived from either beef or sheep
intestines. The membrane is chemically treated and slender strands are woven together to form a
suture. The grinding process creates a strand of uniform diameter. The suture strand is then
further polished to achieve maximum smoothness, for reliability and strength.
• Catgut suture are available in the form of plain catgut or chromic catgut.
• Plain catgut is usually having shorter absorption periods and is absorbed more rapidly in
infected areas.
• The percentage of collagen in the catgut suture often determines the quality of the suture.
Higher percentages of collagen allow for: superior tensile strength, longer absorption times, and
lower reactions in vivo. Plain catgut is available in ivory colour.

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
55
Catgut Chromic Suture | Catgut suture
•  Chromic catgut is treated with chromium salt solution to resist body enzymes and slower the
absorption process thus supporting the wound for longer periods.
• Chromic gut is chromicised before it is spun into strands. This allows control over the amount of
chromic content for an even absorption rate.
• The chromic content not only increases the tensile strength, but also reduces tissue irritation.
• Catgut sutures are sterilized by a sterilizing fluid containing EO (ethylenoxide), distilled
water and isopropyl alcohol.

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
56
Distinctive Characteristics of Catgut Chromic Sutures
•Absorption within 60-90 days for chromic suture and 60-70 days for plain gut suture.
•Allows for smooth passage through tissue.
•Packed in IPA to retain memory & increase pliability.
•Uniform chrome content provides required wound support and absorption.
•Catgut suture are available from U.S.P Sizes 5-0 to 2
•General closure, Ophthalmic, Orthopaedics, Obstetrics/Gynaecology and Gastro-intestinal Tract
Surgery.

 COLLAGEN – Solubility 1
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
57
Some cosmetics include soluble or hydrolyzed collagen. In this case, the collagen molecules have
been broken down into much smaller fragments, which are able to penetrate the skin’s surface.
COLLAGEN SOLUBILITY DEPENDS ON:
• MW >  hydrolysable Types are more soluble, even in the Water,
• pH,
• …………..

COLLAGEN – Solubility 2
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
58
ISOELECTRIC POINT of COLLAGEN: approx. pH7
 SOL               28 °C              GEL
 GEL               34 °C              SOL
Transition SOL               GEL is NOT the one POINT CHARACTERISTIC, it is NOT Reversible Process!
It is called „INVERS PROCESS“, because some Changes in the Macromolecular Conformations can occur
during this Process.

 COLLAGEN – Nanofibres 1
(Courtesy of the CONTIPRO Ltd.)
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
59
NANOVLÁKNO KOLAGEN vzorek_4_1kx.tiff

 COLLAGEN – Nanofibres 2
(Courtesy of the CONTIPRO Ltd.)
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
60
NANOVLÁKNO KOLAGEN vzorek_4_5kx.tiff

 COLLAGEN – Nanofibres 3
(Courtesy of the CONTIPRO Ltd.)
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
61
NANOVLÁKNO KOLAGEN vzorek_4_10kx.tiff

 COLLAGEN – Prices on the World Market Grades for Cosmetic, Water-soluble
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
62
US $12 - 18 / Kilogram
100% Soluble In Water Solubility Hydrolyzed Collagen For Hair
Supply Ability: 300 Ton/Tons per Month Fish Collagen
Country of Origin: China (PRC)
US $12 - 18 / Kilogram
FOOD GRADE
Supply Ability: 300 Ton/Tons per Month Fish Collagen
Country of Origin: China (PRC)

 COLLAGEN as the Basic Substance for   Chemical Reactions
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
63
• If possible – POLYMERANALOGIC CHANGES (REACTIONS), it is without changes of the MW,
• They were mostly the Modifications for Photographic Emulsions > PATENTS,
• The Substrates for Cultivation of the Cells’ Cultures are the main Subject now (Patents,
Publications etc.)
The Reaction point is the Amino-group (-NH2)
ARTICLE (e.g.):
Synthesis and properties of some GELATIN derivatives with substituents at the amino groups
J. Chem. Techn. and Biotechnology, 15, (1965), 479

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
64
 COLLAGEN as the Basic Substance for   Chemical Reactions
Chemical Modification (see Slide No. 47 also)
Reaction with monofunctional Reagents
• Acylation (acetanhydride + amino-groups)
• Esterification (dimethylsulphate, anhydrous methanol) – the Swelling Curve is changing, Structure
and Insolubility is remained
• Deaminace (Mixture of Sodium Nitrite and Ice acetic acid) – Amino-groups à Hydroxyl Groups; the
Swelling Curve is changing
• Deguanidinace – Arginine à Ornithine + Urea or Citrulline + Ammonium

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
65
Ornitine
Citrulline
335px-L-Citrullin2_svg WIKI CZ 30012018.png 266px-L-Ornithin2_svg WIKI CZ 30012018.png

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
66
 COLLAGEN as the Basic Substance for   Chemical Reactions
Chemical Modification
Reactions going to Crosslinked Gel Forming
• Higher Flexibility, Resistance to Enzymes Proteases, lower Swelling Degree à better Product
• Aldehyde Condensation (Glutaraldehyde forms Bridges) à Double Schiff Base – higher Resistance to
to Acid or Basic High temperature Hydrolysis
• Oxidation by Periodate (5-hydroxyproline à Aldehyde à + amino Groups of Lysines àNetwork �
higher  Mechanical Strength
•

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
67
 COLLAGEN as the Basic Substance for   Chemical Reactions
Chemical Modification
Reaction with Synthetic Polymers (Surface Immobilisation)
Covering of the Porous COPOLYMER of Polyethylene with Acrylic acid by COLLAGEN bond to the Surface
by the Covalent Bond  amide Bond (between Carboxylic Groups of the Acrylic acid and the Amino
groups of the COLLAGEN Molecule) à INCREASING OF THE IMPLANTATES’ BIOCOMPACTIBITY
AN  EXAMPLE
The Covering of the Vessels Substitutes knitted from PET Fibres

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
68
COLLAGEN Medical  Applications  1
• Catgut Chromic Suture – Resorption is controlled by the Chromium Salts crosslinking
• Split leather, Nonwoven Textiles, Fixed Foams à Radiation-Chemical Sterilisation à Wounds’ &
Burns Covering
• Spray Bandage on Wounds (COLLAGEN Powder )
• Blood Vessel Reparation, Tendon Replacement
•Cells’ Cultures Growing in vitro
• …………………

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
69
COLLAGEN Medical  Applications 2
• COLLAGEN inside covered Teflon hose > Blood Vessel Replacement
• Combination with Calcium Phosphate à Bones and Tooth Replacement
•Injection of the Microcapsules impregnated with effective Substance – Wound Healing
• COLLAGEN Glue in Surgery
• ………….
•

COLLAGEN based Articular Preparation
 NUTRITION & REGENERATION
of the Articular Cartilage
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
70
ORLING Company (Czech Republic) accordingly:
Pure native Collagen is as the Rope coiled from the Three Fibres, which is non-specifically split
during Digestion. The Results are split Chains, which are of various Length whenever.
Hydrolysed Collagen is called Collagen Peptides. If the Collagen is split by Enzymes COLLAGENASE,
the pure native Collagen is changed to the Collagen Peptides of the same Length every time.
The Biological Activity of the Pure native Collagen and of the Collagen Peptides is different, what
was proved by many scientific Studies.

3.Manufacture of GELATIN & ANIMAL GLUE
•TANEX Company, Czech Republic
•The Pictures were taken during Students’ Excursion to this Glue Plant Company
•
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
71

Manufacture of GELATIN & ANIMAL GLUE
The Raw Materials are not looking too atractive 1!
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
72
Suroviny TANEX IMAG0951.jpg Suroviny TANEX IMAG0943.jpg
Abattoir by-products from the Pig livestock
Skin, Ears etc.

Manufacture of GELATIN & ANIMAL GLUE
The Raw Materials are not looking too atractive 2!
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
73
Suroviny TANEX IMAG0942.jpg Suroviny TANEX IMAG0950.jpg
Abattoir by-products from the Pig livestock
Skin, Ears etc.

Manufacture of GELATIN & ANIMAL GLUE
BASIC SCHEMA
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
74
Přeměna kolagen - želatina
COLLAGEN
GELATIN

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
75
Example of the GELATIN & Animal Glue Making 1
Parameters
Sequence of Leaching (Lixiviating)
1
2
3
4
Product
Edible & Photographic GELATIN
GELATIN
1.Quality
GELATIN
2. Quality
Technical GELATIN & Animal Glue
Temperature (°C)
50 – 55
60 – 65
70 – 75
85 - 100
Time (hours)
5
pH
5 - 7
Concentration (% w/w)
3 - 8
3 - 8
10
> 12
Better Raw Material & Mild Manufacturing Conditions > GELATIN
Worse Raw Material & „Rough“ Manufacturing Conditions > Animal Glue

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
76
Example of the GELATIN & Animal Glue Making 2
Parameters
Sequence of Leaching (Lixiviating)
1
2
3
4
Product
Edible & Photographic GELATIN
GELATIN
1.Quality
GELATIN
1.Quality
Technical GELATIN & Animal Glue
Temperature (°C)
60 – 65
80 – 85
95 – 100
100
Time (hours)
8
pH
5 - 7
Concentration (% w/w)
8
Raw Materials:
1.Abattoir by-products from the Pig livestock (Animal Glue)
2.Bones from Abattoir (Bone Glue)
3.Wastes from the Tannery (Animal Glue)

Manufacture of GELATIN & ANIMAL GLUE
TECHNOLOGICAL STEPS
1.Washing of the Fleshings (Removing of the Preservatives, usually Ca(OH)2) and acidification to pH
= 6,2 – 6,5 using HCl or H2SO4
2.„Cooking“ of the GELALTIN & GLUE > transformation of the COLLAGEN  to so called GLUTINE SOLUTION
(NOT GLUTENE!) in several Stages, up to the Rest only about 2 – 5 % w/w of the original Charge
3.Filtration to remove the Impurities
4.Preservation  and Bleaching by SO2 or H2O2
5.Thickening in the Evaporator
6.Chilling and Forming
7.Drying to the Water Content 12 – 15 % w/w
8.Cutting to small Cubes od Milling to Powder
9.
9.
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
77

Manufacture of GELATIN & ANIMAL GLUE
TECHNOLOGICAL WASTES and their USE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
78
1.Skin Fat >  Refining (Purification) > Sale or use for the SOAK Manufacture
2.Impurities filtered out > Biogas or Burning or approved waste Dump

Bone & Animal Glue and GELATIN In the Work of the CONSERVATOR – RESTORER I
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
79

•Wood Gluing,
•Book Binding,
•Paints binding Agent,
•Undercoat  (Primer, Primer Coat) for Painting
•Binding Agent for the Nonwoven Textile
•
•Photographic Plates and Films (FORMELY)
•Casting Moulds
•Undercoat  for the Contact Gilding (Covering by very thin Gold Foils)
•

COLLAGEN and CONSERVATOR – RESTORER
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
80
Detail
Technická želatina

CUTGUT srtuna do smyčcových nástrojů 1280px-Violino_classico,_dettaglio WIKI ENG 09122017.jpg
Catgut (STRINGS) for the Bowed Instruments
are made of COLLAGEN forming the animal's gut (usually Sheep or Goat)

GELATIN - Clarifying of Wine and fruit Juice
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
81
želatina pH X izoelektrický bod 15012016.jpg
 Clarifying = the Measure to remove the Substances forming Wine lees (Haze)
The main Haze forming Substance in Wine is PEKTIN
PEKTIN 15012016.jpg
The Structure Formula of PECTIN
R = H or
–CH3
Isoelectric Point of GELATIN  the Manufacturing Technology accordingly:
• On the Left – acid catalysis
• On the Right – basic catalysis

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
82
From the QUALITY POINT OF WIEV,  the LOWEST MW HAS:
GLUE FOR THE Wall House Painting
For the Interior Painting is added go get for the Painting Cohesion
Because having the lowest MW, it is the most Degradated COLLAGEN, it is soluble even at room
Temperature in the cold Water

3.Tannery
–3.1 HIDE versus Leather
–3.2 Tanning of HIDE technology
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
83

3.1 Skin  versus Leather
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
84

HIDE versus Leather
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
85
Detail
Technická želatina

ŘEZ KŮŽÍ.jpg
HIDE = it is that, what is taken after the Slaughter of the Animal
LEATHER = it is that, what is gained after Tanning of the HIDE
True Inner HIDE is the principal Part of the the HIDE for the Manufacture of the LEATHER
Outer HIDE & Fleshings (Under HIDE connective Tissue are removed during Processing of the HIDE to
LEATHER
True inner HIDE
Outer HIDE
Fleshings (Under HIDE connective Tissue
RAW HIDE transversal sectional View

HIDE COMPOSITION - CROSSCUT
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
86
Detail
Technická želatina

ŘEZ KŮŽÍ.jpg
• Proteins
• FIBROUS (Collagen)
• Globularní (e.g. Albumine, they are removed before Tanning)
• Fats
• Water
• Inorganic Substances
Processing of the HIDE to LEATHER = HIDE TANNING
Outer HIDE
True inner HIDE
Fleshings (Under HIDE connective Tissue
RAW HIDE transversal sectional View

HIDE – Composition of the True Inner HIDE
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
87
Detail
Technická želatina

•COLLAGEN
–FIBRES FORM  THREEDIMENSIONAL STRUCTURE
•Outer HIDE = PAPILLARY LAYER
•True Inner HIDE = RETIKULARY LAYER
•Ratio of the PAPILARY LAYER versus RETIKULAR LAYER Thicknesses determines the HIDE QUALITY and is
different for various Animals
•

CONTRACTION TEMPERATURE
 HIDE VERSUS LEATHER
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
88
CONTRACTION TEMPERATURE is:
Release of the Hydrogen Bonds between COLLAGEN FIBERS caused by the increased Temperature and the
CONTRACTION (SHINKAGE) so released Fibres
This Process is IRREVERSIBLE
COLLAGEN CONTRACTION TEMPERATURE for various Tanning Procedures
Tanning Procedures
CONTRACTION TEMPERATURE (°C)
COLLAGEN  without Tanning
58 – 68
Fur Tawing
49 – 63
Formaldehyde Tanning
63 – 73
Tannine Tanning
70 – 87
Basic Tanning by Aluminium Salts
74 – 81
Basic Tanning by Chromium Salts
77 - 100

HIDE VERSUS LEATHER
•LEATHER is more resistant against to Microorganisms in the humid Conditions •LEATHER has the
higher chemical Resistance and lower Swelling in the Water •LEATHER has better and advantageous
mechanical Properties and is soft and pliable if it is Dry •LEATHER has higher CONTRACTION
TEMPERATURE
•
•
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
89
Detail
Technická želatina

3.2 Technology Steps at HIDE Tanning
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
90

Technology Steps at HIDE Tanning
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
91
1.Preservation
2.Soaking (Liming)
3.Leaching (Unhairing and scudding) in the Solution Sodium Sulfite and Lime (Ca(OH)2) to remove Fur
and the so called depilated raw Hide.
4.Piling of Hides
5.Scraping – connective Tissue and Muscles Rest are cut off
6.Decalcification of Clearings(Deliming) –see 3, Removing of the Ca Salts
7.Bating & Pickling– Preparation for Tanning
8.Tanning
9.Greasing
10.

COLLAGEN – Cross Bonds IN VITRO 1
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
92
COLLAGEN  modification Reactions are used in transformation of the HIDE  to LEATHER and GELATIN
Modification.
Irreversible Process occurs during forming of the Cross Bonds between COLLAGEN  Molecules. So
called TANNING AGENTS are necessary for this CROSSLINKING of the COLLAGENs Molecules.
TANNING AGENTS are the di or tri or multifunctional Substances.
The HIDE is changed (transformed) to LEATHER by Reaction of COLLAGENs Molecules with these TANNING
AGENTS.
The chemical and physical Changes occurred during TANNING.

 COLLAGEN – Cross Bonds IN VITRO 2
are the CHEMICAL BASIS of the
 Tanning of the HIDE to LEATHER
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
93
a)INORGANIC COMPOUNDS – coordination Compound (Complex) based on the Cr, Al, Zr, Fe etc. And
heteropolyacids of the Si, P, W, Mo
b)ORGANIC COMPOUNDS – Tannins of the Plant Origin, Aldehydes, Chinons, Syntanes, Fats,
Sulfochlorites,  some synthetic Polymers
Tanning by heavy Metals, Aldehydes, Chinons is possible to compare with the Cross Bonds IN VIVO.
The most important are Salts of Cr and Zr, Tannins of the Plant Origin, Aldehydes, Syntanes.

Tanning of the HIDE to LEATHER
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
94
Detail
Technická želatina

• HIDE Tanning is the CHEMICAL PROCESS,  when   functional Groups of the COLLAGEN react with
Tanning Substance (Reagent)
•Tanning Substances (Reagents)
1.TANNINS (HYDROLYSABLE OR CONDENSED) > Vegetable Tanning
2.POTASSIUM ALUMINIUM SULPHATE
3.CHROMIUM COMPOUNDS

Tanning of the HIDE to LEATHER
Similarity with Vulcanisation of the RUBBER to VULCANISED RUBBER
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
95
Detail
Technická želatina

•Tanning of the HIDE is the CHEMICAL REACTION,  when react COLLAGENs functional Group with the
Tanning Substances and forms NETWORK BETWEEN MACROMOLECULES OF COLLAGEN •VULCANISATION of Rubber to
VULCANISED RUBBER is the CHEMICAL REACTION  called VULCANISATION which forms NETWORK BETWEEN
MACROMOLECULES OF POLYIZOPRENE

Vegetable Tanning of the HIDE to LEATHER 1 A
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
96
•Basis is the  Interaction of  –OH or SO3-2 Groups of Tannin with side Chain Groups on the COLLAGEN
Chain forming the COVALENTN or HYDROGEN BOND
•
TŘÍSLOČINĚNÍ 001.jpg
------ OH -

Vegetable Tanning of the HIDE to LEATHER 1 B
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
97
Detail
Technická želatina

•Basis is the  Interaction of  –OH or SO3-2 Groups of Tannin with side Chain Groups on the COLLAGEN
Chain forming the COVALENTN or HYDROGEN BOND
•
TŘÍSLOČINĚNÍ 002.jpg
H2O
------- SO3-2

Vegetable Tanning of the HIDE to LEATHER 2
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
98
img879.jpg img880.jpg img881.jpg
COVALENT BOND of CHINONE to AMINOGROUPS
HYDROGEN BOND WITH IMIDOGROUPS
COLLAGEN
COLLAGEN
TANNIN
COVALENT BOND of CHINONE to AMINOGROUPS +
HYDROGEN BOND WITH IMIDOGROUPS

CHROMIUM TANNING HIDE to LEATHER  1
January 9/2018
NATURAL POLYMERS MU SCI 9 2018
99
•Basis is Interaction of COLLAGEN Group  –COOH via Forming CHROMIUM COMPLEX COMPOUND
•
img878.jpg
Chromium(III) sulfate ([Cr(H2O)6]2(SO4)3) has long been regarded as the most efficient and
effective tanning agent.

January 9/2018
NATURAL POLYMERS MU SCI 9 2018
100
Detail
Technická želatina

lossy-page1-458px-Possible_Chromium(III)_Tanning_Mechanisms_tif.jpg