NATURAL POLYMERS MU SCI 8 2018
1
NATURAL POLYMERS
PROTEINS I
Dr. Ladislav Pospíšil
January 8/2018

Time schedule
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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.Chemistry of Peptides and Proteins
2.Supermolecular Structure of Peptides and Proteins
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Chemistry of Peptides and Proteins
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AminoAcidball_svg.png
In the structure shown BELLOW the SLIDE, R represents a side chain specific to each amino acid. The
carbon atom next to the carboxyl group (which is therefore numbered 2 in the carbon chain starting
from that functional group) is called the α–carbon. Amino acids containing an amino group bonded
directly to the alpha carbon are referred to as alpha amino acids. These include amino acids such
as PROLINE which contain secondary amines, which used to be often referred to as "imino acids".

Chemistry of Peptides and Proteins
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Amino_acid_zwitterions_svg.png D+L-Alanine.gif Beta_alanine_comparison_svg.png
β-alanine and its α-alanine isomer
An amino acid in its (1) un-ionized and (2) zwitterionic forms
amfion
Převzato z NĚMČINY

Chemistry of Peptides and Proteins
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Lysine_fisher_structure_and_3d_ball_svg.png
LYSINE– it has „LENT“ one H+ Cation here !

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Amino acids are the structural units (monomers) that make up proteins. They join together to form
short polymer chains called peptides or longer chains called either polypeptides or proteins. These
polymers are linear and unbranched, with each amino acid within the chain attached to two
neighboring amino acids.
Twenty-two amino acids are naturally incorporated into polypeptides and are called proteinogenic or
natural amino acids.
Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins
during translation. The word "proteinogenic" means "protein creating". Throughout known life, there
are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an
additional 2 that can be incorporated by special translation mechanisms
A peptide bond, also known as an amide bond, is a covalent chemical bond linking two consecutive
amino acid monomers along a peptide or protein chain.
The peptide bond is synthesized when the carboxyl group of one amino acid molecule reacts with the
amino group of the other amino acid molecule, causing the release of a molecule of water (H2O),
hence the process is a dehydration synthesis reaction (also known as a condensation reaction).

Chemistry of Peptides and Proteins
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731px-Peptidformationball_svg.png

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576px-AminoacidCondensation_svg WIKI ENG 22012018.png
A peptide bond, also known as an amide bond, is a covalent chemical bond linking two consecutive
amino acid monomers along a PEPTIDE or PROTEIN CHAIN
PEPTIDES are short chains of amino acid monomers linked by peptide (amide) bonds.
PROTEINS are large biomolecules, or macromolecules, consisting of one or more long chains of amino
acid residues. A linear chain of amino acid residues is called a polypeptide. A protein contains at
least one long polypeptide. Short polypeptides, containing less than 20–30 residues, and are
commonly called peptides, or sometimes oligopeptides.

Chemistry of Peptides and Proteins
HIERARCHI
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AMINOACID = monomer
PEPTID = oligomer
PROTEIN = polymer

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AminoACIDS with  aliphatic Side chain
Glycine Gly (G)
Alanine Ala (A)
Valine Val (V)
Leucine Leu (L)
Isoleucine Ile (I)
AminoACIDS with Carboxyl or Amide Group in the Side chain
(Acid Groups)
Asparagic Acid Asp (D)
Asparagine Asn (N)
Glutamic Acid Glu (E)
Glutamine Gln (Q)
AminoACIDS with Amine Group in the Side chain
(Basic Groups)
Arginine Arg (R)
Lysine Lys (K)
AminoACIDS with Aromatic nucleus (ring) or Hydroxyl Group in the Side chain
Histidine His (H)
Phenylalanine Phe (F)
Serine Ser (S)
Threonin Thr (T)
Tyrozine Tyr (Y)
Tryptophane Trp (W)

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AminoACIDS with Sulphur Atom in the Side chain
Methionine Met (M)
Cysteine Cys (C)
AminoACIDS with the SECONDARY AMINE
ProlinE Pro (P)
21. AminoACID (CONTAINING Se)
SelenocysteinE SeCys
22. AminoACID
Pyrolysine Pyl

Chemistry of Peptides and Proteins
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Class
Name of the amino acids
Aliphatic
Glycine, Alanine, Valine, Leucine, Isoleucine
Hydroxyl or Sulfur-containing
Serine, Cysteine, Threonine, Methionine
Cyclic
Proline
Aromatic
Phenylalanine, Tyrosine, Tryptophan
Basic
Histidine, Lysine, Arginine
Acidic and their Amide
Aspartate, Glutamate, Asparagine, Glutamine

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Biogenic aminoacids
Glycine (Gly, G)
Alanine (Ala, A)
Valine (Val, V)
Leucine (Leu, L)
Isoleucine (Ile, I)
Amminoacido_glicina_formula.png Amminoacido_alanina_formula.png Amminoacido_valina_formula.png
Amminoacido_leucina_formula.png Amminoacido_isoleucina_formula.png

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Biogenní aminokyseliny
Threonine (Thr, T)
Tyrosine (Tyr, Y)
Methionine (Met, M)
Cysteine (Cys
Amminoacido_treonina_formula.png Amminoacido_tirosina_formula.png
115px-Amminoacido_metionina_formula.png 95px-Amminoacido_cisteina_formula.png

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Biogenní aminokyseliny
Lysine (Lys, K)
Asparagová ACID (Asp, D)
Asparagine (Asn, N)
Glutamic ACID (Glu, E)
Glutamine (Gln, Q)
Amminoacido_lisina_formula.png Amminoacido_asparagina_formula.png
Amminoacido_acido_aspartico_formula.png Amminoacido_glutammina_formula.png
Amminoacido_glutammina_formula.png

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Biogenní aminokyseliny
Arginine (Arg, R)
Histidine (His, H)
Phenylalanine (Phe, F)
Tryptofane (Trp, W)
Proline (Pro, P)
Amminoacido_arginina_formula.png Amminoacido_istidina_formula.png
Amminoacido_fenilalanina_formula.png Amminoacido_triptofano_formula.png
800px-Amminoacido_prolina_formula_svg.png

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Biogenní aminokyseliny
Selenocysteine (SeCys,U)
Pyrolysine (Pyl,O)
Serine (Ser, S)
N-formylmethionine (fMet)
711px-L-selenocysteine-2D-skeletal.png 560px-Pyrrolysine_svg.png
430px-(S)-N-Formylmethionine_V_1_svg.png Amminoacido_serina_formula.png

Chemistry of Peptides and Proteins
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img773.jpg img774.jpg img777.jpg
The Rest of N- ending Amino acid
The Rest of C- ending Amino acid
Peptide Chains are written horizontally using the Abbreviations of the particular Amino acids. An
Example showing the Structure of the Oxitocine Hormone is as follows:
An Example showing the Structure of the Horse Insulin Hormone
(M = 5 802, containing 51 Amino acids) is as follows:

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SCLEROPROTEINS or fibrous proteins
The roles of such proteins include protection and support, forming connective tissue, tendons, bone
matrices, and muscle fiber. A SCLEROPROTEIN forms long protein filaments, which are shaped like
rods or wires. SCLEROPROTEINS are structural proteins or storage proteins that are typically inert
and water-insoluble. A SCLEROPROTEIN occurs as an aggregate due to hydrophobic side chains that
protrude from the molecule.
A SCLEROPROTEIN'S peptide sequence often has limited residues with repeats; these can form unusual
secondary structures, such as a collagen helix. The structures often feature cross-links between
chains (e.g., cys-cys disulfide bonds between keratin chains).

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Composition of the Fibrous Proteins
Aminoacid
R
Aminoacid Content
(% Molar)
H2N-CHR-COOH
(Abbreviation)
Merino Wool
Silk Fibroin
Beef Collagen
Glycine (Gly)
-H
59,4
44,8
38,0
Alanine (Ala)
-CH3
15,7
29,4
11,9
Valine (Val)
-CH(CH3)2
5,8
2,2
2,2
Leucine (Leu)
-CH-CH(CH3)2
7,9
0,5
2,8
Isoleucine (Ile)
-CH2-C6H5
3,3
0,7
1,3
Serine (Ser)
-CH2-OH
11,8
12,1
1,5
Threonine (Thr)
-CH(CH3)OH
7,6
0,9
4,3
Tyrosine (Tyr)
-CH2C6H4OH
4,8
5,2
1,9

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Composition of the Fibrous Proteins
Aminoacid
R
Aminoacid Content (% w/w)
H2N-CHR-COOH
(Abbreviation)
Merino Wool
Silk Fibroin
Beef Collagen
Tryptophan (Trp)
1,4
0,2
---
Lysine (Lys)
-(CH2)4NH2
2,6
0,3
2,8
Arginine (Arg)
-(CH2)2 –N=C(NH2)2
8,2
0,5
5,4
Histidine (His)
0,8
0,2
0,5
Hydroxylysine
-(CH2)2CH(OH)CH2NH2
Traces
---
0,8
Asparagic Acid (Asp)
-CH2COOH
6,9
1,3
0,1
Glutamic Acid (Glu)
-(CH2)2COOH
13,8
1,0
0,1
Methionine (Met)
-(CH2)2SCH3
0,5
0,1
0,8
Amminoacido_triptofano_formula.png
Amminoacido_istidina_formula.png

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Composition of the Fibrous Proteins
Aminoacid
R
Aminoacid Content (% w/w)
H2N-CHR-COOH
(Abbreviation)
Merino Wool
Silk Fibroin
Beef Collagen
Cystine (Cys-S-S-Cys)
-CH2-S-S-CH2CH(NH2)COOH
6,4
0,1
---
Cystein (Cys)
-CH2SH
0,4
---
---
Proline (Pro)
---
---
4,81,
Hydroxyproline
---
---
10,3
Lanthonine
-CH2-S-CH2CH(NH2)COOH
0,01
---
---
800px-Amminoacido_prolina_formula_svg.png 800px-Amminoacido_prolina_formula_svg.png

Chemistry of Peptides and Proteins
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img778.jpg
The Characteristic Bonds which determine Protein Conformation are in the following Formulas:
Hydrogen Bond
Ionic Bond
Cystein disulfide Bond

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Sekundární struktura bílkovin 002.jpg Sekundární struktura bílkovin 003.jpg

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The isoelectric point (pI, pH(I), IEP), is the pH at which a particular molecule carries no net
electrical charge in the statistical mean. The standard nomenclature to represent the isoelectric
point is pH(I), although pI is also commonly seen, and is used in this article for brevity. The net
charge on the molecule is affected by pH of its surrounding environment and can become more
positively or negatively charged due to the gain or loss, respectively, of protons (H+).
IZOELECTRIC POINT OF Glycine_pI WIKI ENG.png IZOELEKTRICKÝ BOD WIKI ENG 1 ADENOSIE MONO
PHOSPHATE.png
glycine pK = 2.72, 9.60
adenosine monophosphate pK = 2.15, 9.16, 10.67

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For an amino acid with only one amine and one carboxyl group, the pI can be calculated from the
mean of the pKas of this molecule.
pI = (pKa + pKb)/2
Each Amino acid contains at least two Groups, which are able to dissociate giving: -COOH a -NH3+
and they form conjugated Bases -COO- a -NH2.
The Acid and their conjugated Base are in the proton Equilibrium:
R-COOH ↔ R-COO− + H+R-NH3+ ↔ R-NH2 + H+
It is depends on the Environments (Conditions) pH Value, so on the H+ Concentration, how is the
Equivalence set.  The Carboxylic Group is the stronger Acid and so the H+  is easily cleaved from
this Group then taken by this Group.

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Name
pK
pI
at 25°C
pK
α-CO2H
pK
NH3
pK
R-group
Alanine
2.35
9.87

6.11
Arginine
2.18
9.09
13.2
10.76
Asparagine
2.18
9.09
13.2
10.76
Aspartic Acid
1.88
9.60
3.65
2.98
Cysteine
1.71
10.78
8.33
5.02
Glutamic Acid
2.19
9.67
4.25
3.08
Glutamine
2.17
9.13

5.65
Glycine
2.34
9.60

6.06
Histidine
1.78
8.97
5.97
7.64
Isoleucine
2.32
9.76

6.04
Leucine
2.36
9.60

6.04
Lysine
2.20
8.90
10.28
9.47
Methionine
2.28
9.21

5.74
Phenylalanine
2.58
9.24

5.91
Proline
1.99
10.60

6.30
Serine
2.21
9.15

5.68
Threonine
2.15
9.12

5.60
Tryptophan
2.38
9.39

5.88
Tyrosine
2.20
9.11
10.07
5.63
Valine
2.29
9.74

6.02
pK and pl Values of Amino Acids

Chemistry of Peptides and Proteins
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Essential
Nonessential
Histidine
Alanine
Isoleucine
Arginine*
Leucine
Asparagine
Lysine
Aspartic acid
Methionine
Cysteine*
Phenylalanine
Glutamic acid
Threonine
Glutamine*
Tryptophan
Glycine
Valine
Ornithine*
Proline*
Selenocysteine*
Serine*
Tyrosine
(*) Essential only in certain cases
Of the 22 standard amino acids, 9 are called essential amino acids because the human body cannot
synthesize them from other compounds at the level needed for normal growth, so they must be
obtained from food.[52] In addition, cysteine, taurine, tyrosine, and arginine are considered
semiessential amino-acids in children (though taurine is not technically an amino acid), because
the metabolic pathways that synthesize these amino acids are not fully developed.[53][54] The
amounts required also depend on the age and health of the individual, so it is hard to make general
statements about the dietary requirement for some amino acids.

Amino acid > Peptide > Protein
•Amino acid – monomer, L- configuration only
•Peptide – it has less then 50 Amino acids, it is  MW up to approx. 5*105,  it goes through
Cellophane membrane at DIALYSIS •Protein – MW is over approx. 5*105 to X*106, X Î(1;10)
•Determination of the Peptide and Protein Composition
•Acid hydrolysis to Amino acids
•Chromatography (Thin layer, GPC)
•
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PEPTIDES X PROTEINS
•PEPTIDES
•It contains b and g Amino acids also
•Configuration  both D and L
•It belongs here:
•GLUTATHIONE (biological redox system)
•HORMONE
•ANTIBIOTICS
•TOXINE (death angel and the other TOXIC mushrooms, bee poison etc.)
•
•PROTEINS
• a Amino acids only
•Configuration D only
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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!
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CAM00548.jpg

Proteins dividing – the Occurrence of other Components in Macromolecule accordingly
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•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)
–
•

SOLUBILITY versus SWELING
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rozpust verus botnání.jpg
Biopolymer Molecule
Biopolymer Backbone
Water or the other Solvent (Solvating Agent) Molecule

Proteins dividing – Macromolecules’ Solubility in Water of accordingly
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•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
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•FIBRILAR > natural/genuine Silk, Hair, animal Hair, Muscles, fibrous connective Tissue •GLOBULAR >
ENZYM, Egg white, Milk white, INSULIN, …
•

PRIMARY STRUKTURE of Proteine I
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Protein_primary_structure_svg.png

Proteines Molecular Weight
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C:\Users\ladapospa\Documents\Lada\PŘÍRODNÍ POLYMERY SCAN SKRIPT VŠCHT Praha 1990\str 345.jpg
Protein
MW (Relativ, Mean)
I do not know, if it is the Mn or the Mw
Tobacco mosaic virus

PRIMARY PROTEINS STRUCTURE II
DETERMINATION OF THE AMINO ACIDS’ SEQUENCE
•PROTEINS are broken (cleaved) to Amino acids by ENZYMS -  the given ENZYM break (cleave) only the
Bond between the Definite AMINO ACIDS •Using the Different ENZYMS - Different Grafts (Broken Parts)
> AMINO ACIDS SEQUENCE Determination
•
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PRIMARY PROTEINS STRUCTURE III
DETERMINATION OF THE AMINO ACIDS’ SEQUENCE
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•Breaking (Cleaving) on the well define points (only the Bond between  the Definite AMINO ACIDS )
to shorter Parts by ENZYMS  „RESTRICTIVE  ENDONUCLEASES“  (their Number is approx. 200 Types)
•Consecutive Breaking (Cleaving) of this shorter Parts taken by Primary Breaking (Cleaving) by
„RESTRICTIVE  ENDONUCLEASES“ again, but other Types then used primary
•Electrophoretic Sorting (Separation) of the Grafts (Broken Parts)
•Computer Processing of the Results
•
800px-Sanger_sequencing_read_display.gif

PROTEIN SECUNDARY STRUCTURE I
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Hierarchie struktur bílkovin 001.jpg

PROTEIN SECUNDARY STRUCTURE II A
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Left-handed Helix
Sekundární struktura bílkovin 001.jpg

PROTEIN SECUNDARY STRUCTURE II B
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img779.jpg
Left-handed a Helix
b Skládaný list

PROTEIN SECUNDARY STRUCTURE III
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ALFA versus BETA šroubovice aminokyselin scan 04082017.jpg
400px-Cartesian_coordinate_system_handedness_svg.png
Right-handed
RIGHT HAND > thumb UP > Fingers round oriented in the Row Direction
Left-handed Helix
Right-handed Helix
Left-handed
LEFT HAND > thumb UP > Fingers round oriented in the Row Direction

PROTEIN SECUNDARY STRUCTURE IV
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img779.jpg
ALFA HELIX 04082017.jpg
Left-handed a Helix
Right-handed a Helix

Casein – the main Amino acid Components
•Glutamic acid (Glu, E)
•
•
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Amminoacido_glutammina_formula.png
Proline (Pro, P)
800px-Amminoacido_prolina_formula_svg.png img780.jpg
Casein is the  PHOSPHOPROTEID
Amminoacido_serina_formula.png
Serine (Ser, S)

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Amino acids Content in various Proteins
Amino acid
PROTEIN
Gelatine
Casein
Egg white
Egg yellow
(Molar %)
Hydroxyproline
6
0
0
0
Asparagic acid
4
6
10
11
Theorine
2
3
4
6
Serine
4
5
7
11
Glutamic acid
7
18
12
13
Proline
12
15
5
5
Glycine
35
3
6
6
Alanine
12
4
9
8
Valine
2
8
9
7
½ Cystine
0
0
2
2
Methionine
1
2
1
2

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Amino acids Content in various Proteins
Amino acid
PROTEIN
Gelatine
Casein
Egg white
Egg yellow
(Molar %)
Isoleucine
1
6
6
5
Leucine
3
9
10
9
Thyrosine
0
4
1
2
Phenylalanine
1
4
4
3
Lysine
3
6
7
5
Histidine
1
3
2
2
Arginine
5
3
5
4
Gelatine = Denaturated Collagen

Casein – characteristics
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CASEIN  versus QUARK
CASEIN is manufactered from the skimmed (fat-free) MILK, THE HIGH FAT CONTENT IS a DEFECT!
QUARK is manufactered from the Whole (fat) MILK, but it can be also manufactered as the Fat-free or
Low Fat Product!
Cacein Type (Sort)
Water
Fat
Ash
Acidity
Acid, grain
9,5
0,3
1,7
9,9
Acid, Cheese, Lumps
7,8
0,4
4,1
7,6
Acid, Salt, Lumps
7,1
0,2
5,7
6,7
Rennet coagulated
8,3
0,6
8,0
7,9

Casein – Charasteristics
•Protein Part of Milk
•Four Types of Casein recognised: aS1, aS2, b, k (kappa) •Casein is gained by precipitating of Milk
using Acids or Enzymes
•MW = approx. 75 000 – 350 000
•Insoluble in Water
•Soluble in Acids or Bases
•Alkali Solutions have the dispergation (dispersion) Ability
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From Casein to Cheese
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•Casein
–ENZYMEs
•PROTEASE -  it cleavages peptide Bond in the Middle of the Casein Backbone > ALBUMOSE & PEPTONS
are the Results
•PEPTIDASE - it cleavages peptide Bond on the End the Casein Backbone
•AMINASE – it cleavages Amino acids (UNDSIBABLE)
•Cheese  = cleavaged CASEIN
•„Holes “ in Cheese = it is done by Bacterias & Enzymes, which release CO2

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CASEIN
Protease
Aminopolypeptidase
Albumose
Peptones
Polypeptidase
Polypeptides
(PROTEINS)
Dipeptidase
Dipeptides
Aminoacids
Amidase
Desamidase
NH3, volatile acids, H2S
ENZYMS
ALBUMOSE:
Any of a class of substances derived from albumins and formed by the enzymatic breakdown of
proteins during digestion
PEPTONES:
Any of various water-soluble protein derivatives formed by partial hydrolysis or digestion of
proteins by an acid or enzyme, used in culture media in bacteriology.

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PEPTONES - they are Proteins  in general or the Mixture of Proteins which results from Proteins by
partial Hydrolysis done by Enzyme Pepsin and HCl in Stomach
It is stated, that PEPTONES have 3 – 4 Amino acids.
PEPTONES are further cleaved in the Small intestine by Trypsin and Chymotripsin, which are further
cleaved in to the individual Amino acids.

ALBUMOSE – they are only the shorter Proteins from CASEIN

Casein – Use
•Glus
•Paints
•Galalit (Thermoset crosslinked by FORMALDEHYDE)
•…………..
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Galalit is coming back (returning)!
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GALALIT z KASEINU002.jpg

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VÝROBA KASEINU PRŮMYSLOVÁ 05122016.jpg
Acid Dosing (HCl or H2SO4)
First Washing Trough
Second Washing Trough + Chopper
Trough
Continual Manufacture of CASEIN
The BYPRODUCT is WHEY (Proteins, Saccharides, Inorganic Substances etc. …)
MILK
Packing
Tunnel Dryer
Precipitation & Washing

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C:\Users\ladapospa\Documents\Lada\GRANT LABORKY PŘÍRODNÍ POLYMERY
2016\Galalith_Synthesis_SCHEMATIC_V1.png
CASEIN Crosslinking by Formaldehyde
Procedure :
• Prepare formulation from the CASEIN Paste, pour it into 4 % w/w Formaldehyde and leave it mature
several Days
• Form the Product from the CASEIN Paste + Formaldehyde (approx. 5 – 10 parts of CASEIN + 1 part of
Formaldehyde , leave it several Hours or several Days mature at Temperature of 30 – 40 °C

Casein Glues
•CASEIN Glue with Ammonia :
•50 g of pure (industrial Grade) CASEIN is mixed with 250 ml Water and is slightly heated. •15 g of
Ammonia is mixed with a bit of Water and is poured into heated CASEIN. The Solution boils over  and
CO2 is released. CASEIN Glue is mixed up to point, when the releasing of CO2 is finished.
•CASEIN Glue with Lime:
•4 Parts of Fat free QUARK is mixed with 1 Part of well matured (two Years old) Ca(OH)2.  The Glue
is finished after 10 Minutes. CASEIN Glue with Lime must be freshly prepared every Day. It is
diluted by 2 – 3 Parts of Water if used for binding Agent for Paints.
•CASEIN Glue with NaHCO3:
•50 g of NaHCO3 is dissolved in hot Water is chilled at continuous mixing. Add 500 g of Fat free
QUARK and mix it in the Kitchen mixer. Leave it stay for 30 Minutes. Dilute it by cold Water to
desired Consistency. CASEIN Glue with NaHCO3 is suitable as the Glue and/or binding Agent for
Paints.
•
•
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Casein Paints
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•CASEIN Glue – a simple Recipe:
•One Soup Spun (approx. 10 g) of Borax (Na2[B4O5(OH)4]·8H2O)  is dissolved in approx. 250 ml of
Water. Fat free QUARK is mixed with the Borax Solution. Leave it stay for 20 Minutes and mix one
more.
•CASEIN based Paints working:
•The Pigments are mixed with a bit of Water to a Paste. Mix 1 Part of the Coloured Paste with 1
Part CASEIN Glue and  3 Parts of Water.
•CASEIN based Wall Paint:
1.2 kg fat free QUARK
2.90 g of Borax (Na2[B4O5(OH)4]·8H2O) is dissolved in 500 ml of Water and this Solution is mixed
together 3.Mix it in the Kitchen mixer for 20 Minutes and leave it for 20 Minutes stay
4.It is diluted by 8 Litres of Water for basic Painting
5.Mix 1 – 2 Parts of the Pigments Water Paste with 1 Part of the CASEIN Glue and 2 – 3 Parts of
Water .

Egg Proteins – the main Amino acids Components
•Glutamic acid (Glu, E)
•
•
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Amminoacido_glutammina_formula.png Amminoacido_serina_formula.png
Serine (Ser, S)
Amminoacido_leucina_formula.png
Leucine (Leu, L)
Amminoacido_glicina_formula.png
Glycine (Gly, G)

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Amino acids Content in various Proteins
Amino acid
PROTEIN
Gelatine
Casein
Egg white
Egg yellow
(Molar %)
Hydroxyproline
6
0
0
0
Asparagic acid
4
6
10
11
Theorine
2
3
4
6
Serine
4
5
7
11
Glutamic acid
7
18
12
13
Proline
12
15
5
5
Glycine
35
3
6
6
Alanine
12
4
9
8
Valine
2
8
9
7
½ Cystine
0
0
2
2
Methionine
1
2
1
2

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Amino acids Content in various Proteins
Amino acid
PROTEIN
Gelatine
Casein
Egg white
Egg yellow
(Molar %)
Isoleucine
1
6
6
5
Leucine
3
9
10
9
Thyrosine
0
4
1
2
Phenylalanine
1
4
4
3
Lysine
3
6
7
5
Histidine
1
3
2
2
Arginine
5
3
5
4
Gelatine = Denaturated Collagen

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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

Egg Proteins – Use1
•Paints
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LECITHIN 800px-1-Oleoyl-2-almitoyl-phosphatidylcholine_Structural_Formulae_V_1.png
PHOSPHOLIPID  LECITINE – emulsifying Agent
It is Part of the Egg yellow,  but is NOT its Protein Part

Egg Proteins – USE 2
•Paints
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CHOLESTEROL – STEROID & emulsifying AgentIt is Part of the Egg yellow,  but is NOT its Protein Part
440px-Cholesterol_svg.png

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600px-Luteine_-_Lutein_svg.png
Luteine  - Colorant in the Egg yellow
Chemical Name
β,ε-karoten-3,3'-diol
Summary Formula
C40H56O2
CAS registration Number
127-40-2
Appearance
Solid, red – orange
Crystalic Matter
Molar Mass
568,871 g/mol
Melting Temperature
190 °C
Solubility in Water
no
Solubility in  Fats
yes
It is Part of the Egg yellow,  but is NOT its Protein Part

Egg White &Drinks
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• Clarifying of Fruit Juices
• Probably the oldest Clarifying Agent for Fruit Juices  and Wine

Whey
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•Whey is a yellow-green Liquid, which is the Rest gained after precipitation of Milk using Acids or
Enzymes. Whey is in fact Milk Serum.  It looks like in Practise, that the Milk is precipitated and
the Solid Part is CASEIN and the Liquid Part is Whey.  •Dried Whey arises also as the By-product at
Manufacture of Cheese and/or QUARK.  •Whey contains Vitamins B1, B2, B6, B12 and further Vitamins C
and E. As to Inorganic Elements it contains Mg, P, Ca, K, Na, Zn. It contains also the Saccharide
LACTOSE. •Whey has antiflammable Effect when used externally, so it is suitable for the sensitive
Skin also. The other Uses as Dermatologic Agents are also widely used.

Whey –contained PROTEINS
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•Whey protein is a mixture of globular proteins isolated from whey
•Whey protein is the collection of globular proteins isolated from whey, a by-product of cheese
manufactured from cow's milk. The protein in cow's milk is 20% whey protein and 80% casein protein,
whereas the protein in human milk is 60% whey and 40% casein. The protein fraction in whey
constitutes approximately 10% of the total dry solids in whey. This protein is typically a mixture
of beta-lactoglobulin (~65%), alpha-lactalbumin (~25%), bovine serum albumin (~8%)(see also serum
albumin), and immunoglobulins. These are soluble in their native forms, independent of pH.
•β-Lactoglobulin is the major whey protein of cow and sheep's milk (~3 g/l),
•α-Lactalbumin is an important whey protein in cow's milk (~1 g/l) that enhances efficiency of
brain function, •Serum albumin, often referred to simply as albumin is a globular protein. Serum
albumin is the most abundant plasma protein in mammals. •An antibody (Ab), also known as an
immunoglobulin (Ig), is a large Y-shaped protein produced by B cells that is used by the immune
system to identify and neutralize foreign objects such as bacteria and viruses.
•

Plant Proteins
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•Proteins are usually related with Animal Products, but Proteins can be also of the Plant Origin:
•Glutens (glutelins)
•Prolamins (gliadins)
•They are MOSTLY  Water insoluble (approx . 80 % of them)
•
Plant
Group
Protein
Remark, more Specific
Wheat, Barley, Rye
Gluten
glutenin
8 – 13, sometimes also 15 % w/w Proteins
Rice
oryzenin
Wheat, Rye
Prolamin
gliadin
coeliac disease, allergy to Gluten
Corn
zein
Barley
hordein
 GLYCOPROTEIN, coeliac disease, allergy to Gluten
Legumes
Pea, Bean, Lentil, Soya, Ground-nut etc., up to 45 % w/w  Proteins

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Prolamins are a group of plant storage proteins having a high proline content and found in the
seeds of cereal grains: wheat (gliadin), barley (hordein), rye (secalin), corn (zein), sorghum
(kafirin) and as a minor protein, avenin in oats. They are characterised by a high glutamine and
proline content and are generally soluble only in strong alcohol solutions. Some prolamins, notably
gliadin, and similar proteins found in the tribe Triticeae (see Triticeae glutens) may induce
coeliac disease in genetically predisposed individuals.
Gluten is a composite of storage proteins termed prolamins and glutelins and stored together with
starch in the endosperm (which nourishes the embryonic plant during germination) of various cereal
(grass) grains. It is found in wheat, barley, rye, oat, related species and hybrids (such as spelt,
khorasan, emmer, einkorn, triticale, kamut, etc.) and products of these (such as malt). Glutens,
and most especially the Triticeae glutens, are appreciated for their viscoelastic properties. It
gives elasticity to dough, helping it rise and keep its shape and often gives the final product a
chewy texture.
Gliadin (a type of prolamin) is a class of proteins present in wheat and several other cereals
within the grass genus Triticum. Gliadins, which are a component of gluten, are essential for
giving bread the ability to rise properly during baking. Gliadins and glutenins are the two main
components of the gluten fraction of the wheat seed. This gluten is found in products such as wheat
flour. Gluten is split about evenly between the gliadins and glutenins, although there are
variations found in different sources.
Gliadin is the water-soluble component of gluten, while glutenin is insoluble. There are three main
types of gliadin (α, γ, and ω), to which the body is intolerant in coeliac (or celiac) disease.
Diagnosis of this disease has recently been improving