NATURAL POLYMERS MU SCI 10 2018 1 NATURAL POLYMERS FIBROUS PROTEINS II KERATIN & FIBROIN Dr. Ladislav Pospíšil January 10/2018 Time schedule January 10/2018 NATURAL POLYMERS MU SCI 10 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.Keratin 2.Fibroin • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 3 2.Keratin January 10/2018 NATURAL POLYMERS MU SCI 10 2018 4 Where is found KERATIN? •The Skin Structures – Hair, Feathers, Animal Hair, Bristle •ENDS of the Fingers and Limb – Nails, Claw, Hooves •OBJECT from the Horny Tissue – Horns •Outer Skin (Humans) - Horny Tissue like Layer (old Skin) January 10/2018 NATURAL POLYMERS MU SCI 10 2018 5 What is KERATIN characterized by 1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 6 •The PROTEIN’S Chains are CROSSLINKED via SULFIDIC BRIDGES (-S–S-) formed via – SH Groups of CYSTEINE and the CYSTINE is the Result • 95px-Amminoacido_cisteina_formula.png 800px-Cystine-skeletal.png What is KERATIN characterized by 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 7 •RATIO (approx.) of the three Main AMINO ACIDS in the KERATIN AMINOKYSELINA PODÍL VZOREC HISTIDINE 1 LYZINE 4 ARGININE 12 Amminoacido_lisina_formula.png Amminoacido_arginina_formula.png Amminoacido_istidina_formula.png What is KERATIN characterized by 3 •WATER INSOLUBLE •RESISTANT TO DILUTED ACIDS •NONRESISTANT TO BASIS (e.g. NaOH, KOH etc.) > to clean the Keratin made Brush in the NaOH must be done very carefully, because the natural Bristles can be dissolved entirely! •The most important KERATIN Fiber is the Sheep's Wool January 10/2018 NATURAL POLYMERS MU SCI 10 2018 8 What is KERATIN characterized by 4/1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 9 SOFT KERATIN - Hen's & Chicken Feathers is easily cleaved by Inorganic acids and Bases to Amino acids > ANIMALS’FEEDING Composition of the AMINO ACIDS in the KERATINS of various Origin AMINO ACID Human’s Skin Human’s Hair Horny Tissue Hen's Feathers Pig’s Bristle Glycine 10,4 4,1 – 4,2 9,6 7,2 NA Alanine 4,3 2,8 2,5 5,4 NA Valine 3,3 5,9 5,5 5,8 5,9 Leucine 8,3 6,4 – 8,3 8,3 7,4 – 8,0 8,3 Isoleucine 3,3 4,7 – 4,8 4,8 5,3 – 6,0 4,7 Phenyalanine 4,0 2,4 – 3,6 4,0 4,7 – 5,3 2,7 Tyrosine 4,7 2,2 – 3,0 5,6 2,0 – 2,2 3,5 Serine 11,5 7,6 – 10,6 6,1 4,4 – 4,8 NA Methionine 1,6 0,7 – 1,0 2,2 0,4 – 0,5 0,5 Proline 2,7 4,3 – 9,6 8,2 8,8 – 10,0 9,6 Arginine 5,7 8,9 – 10,8 10,7 6,5 – 7,5 10,9 Histidine 1,6 0,6 – 1,2 1,1 0,7 1,1 CYSTINE 1,5 16,6 – 18,0 15,7 6,8 – 8,2 14,4 What is KERATIN characterized by 4/2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 10 Composition of the AMINO ACIDS in the KERATINS of various Origin AMINO ACID Human’s Skin Human’s Hair Horny Tissue Hen's Feathers Pig’s Bristle Asparagic acid 9,35 3,9 – 7,7 7,9 5,8 – 7,5 8,9 Triptophane 1,0 0,4 – 1,3 0,7 0,7 NA Lysine 5,2 1,9 – 3,1 3,6 1,7 3,8 Threonine 4,3 7,0 – 8,5 6,1 4,4 – 4,8 NA Glutamic acid 15,3 13,6 – 14,2 13,8 9,7 17,9 AMIDIC NITROGEN 0,9 1,2 1,1 1,1 NA TOTAL NITROGEN 19,6 15,5 – 16,9 16,9 16,2 NA TOTAL SULPHUR 0,8 3,0 – 4,0 5,2 3,9 NA NA – Not Available 197px-L-Threonin_-_L-Threonine_svg.png Threonine SOFT KERATIN - Hen's & Chicken’s Feathers is easily cleaved by Inorganic acids and Bases to Amino acids > ANIMALS’ FEEDING CYSTINE > contains –S-S- Bond What is KERATIN characterised by 4/3 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 11 KERATIN Composition it so different for the different Parts of the Human or Animal Bodies and also for different Animals (It is not given in the previous Table) KERATIN is sometimes sorted to SOFT (approx. 2 % w/w of Cystine) and HARD (up to 20 % w/w of Cystine) SOFT KERATIN - Hen's & Chicken’s Feathers is easily cleaved by Inorganic acids and Bases to Amino acids > ANIMALS’FEEDING What is KERATIN characterized by 5 •Ability to form Connection between Fibres by Chemical Bond > it is Analogue to Rubber Crosslinking or to the Hide Tanning • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 12 440px-Disulfide-bond two cystein molecules form CISTIN SULFUR BRIDGE.png Two Cysteines > one CYSTINE What is KERATIN characterized by 6 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 13 468px-Disulfide_Bridges_(SCHEMATIC)_V_1_svg.png 350px-Proinsuline_schematic_topological_diagram_svg two cystein molecules form CISTIN SULFUR BRIDGE.png These Bonds are the Principle of the Permanent wave of Hair Enzymatic Cleavage of the Backbone What is KERATIN characterized by 7 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 14 img902.jpg KERATIN is so very chemicaly reactive Fibre Amminoacido_asparagina_formula.png ASPARAGINE The reactive Sites of the KERATIN’S Amino acids What is KERATIN characterized by 8/1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 15 AMINO ACIDS in the KERATINS- Dividing into various Groups (the Sheep's Wool ) AMINO ACID Group AMINO ACID AMINO ACID Content (mg/g Wool) Kationic Arginine 570 Lysine 228 Histidine 66 Anionic Asparagic acid ----------------- Glutamic acid 772 Alcoholic -OH Serine 888 Treonine 528 Phenolic –OH Tyrosine 300 Sulphur Cystein 24 Cystin 500 Methionine 29 Cysteinsulfonic acid 15 What is KERATIN characterized by 8/2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 16 AMINO ACIDS in the KERATINS- Dividing into various Groups (the Sheep's Wool ) AMINO ACID Group AMINO ACID AMINO ACID Content (mg/g Wool) Polar covalent Bond Asparagine ------------------ Glutamine 822 Nonpolar covalent Bond Alanine 438 Valine 487 Leucine 643 Isoleucine 275 Proline 570 Phenylalanine 239 Tryptophane 32 Glycine 749 What is KERATIN characterized by 9 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 17 AMINO Acid Formula Cisteine Cistine It is formed only by the Reaction of two Cisteine Molecules by intermolecular or intramolecular Way Methionine Cysteinsulfonic acid It is formed only by the Reaction (OXIDATION) –S-S- Bringe (Bond) in Cistine Lanthionine (two ALANINES bonded via –S- ) 115px-Amminoacido_metionina_formula.png 95px-Amminoacido_cisteina_formula.png 800px-Lanthionine.png January 10/2018 NATURAL POLYMERS MU SCI 10 2018 18 Value of Heat of Hydration for Wool with Water and Alcohols at 20 °C Hydration Agent Moly Volume at 20 °C (cm3/mol) Heat of Hydration (J/g) Water 30 100 Methanol 67 91 Ethanol 97 54 Acetic acid 95 119 The molar volume, symbol Vm, is the volume occupied by one mole of a substance (chemical element or chemical compound) at a given temperature and pressure. It is equal to the molar mass (M) divided by the mass density (ρ). It has the SI unit cubic metres per mole (m3/mol), although it is more practical to use the units cubic decimetres per mole (dm3/mol) for gases and cubic centimetres per mole (cm3/mol) for liquids and solids. Why the wet Wool provides Heat? The Sorption Properties of the KERATIN January 10/2018 NATURAL POLYMERS MU SCI 10 2018 19 KERATIN a sorpce kyselin a zásad.jpg PAY ATTENTION TO THIS! Y Axis is the POSITIV ONE in both Directions! The Interaction of the WOLL with HCl and KOH Solutions (mmol/g) in Dependance on pH Value: 1 – at 0°C, 2 - at 25°C, 3 - at 40°C, 4 - at 50°C KERATIN Reactivity 1 •It is based on the Reactions of the CYSTEIN CYSTEINU • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 20 img903.jpg Two Cysteines > one CYSTINE 800px-Cystine-skeletal.png CYSTINE can create both INTERMOLECULAR and ITRAMOLECULAR Bonds KERATIN Reactivity 2 •It goes on preferably the •DISULFIDIC BRIDGE (Bond) •Hydrolysis of the DISULFIDIC BRIDGE (Bond) •Oxidation •Reduction January 10/2018 NATURAL POLYMERS MU SCI 10 2018 21 KERATIN Reactivity 3 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 22 Oxidace CISTINU na KYS. CYSTEINSULFONOVOU.jpg CYSTEINSULFONIC ACID arises only by Reakction (OXIDATION) –S-S- BRIDGE (Bond) of the CYSTINE The four Fractions of the KERATIN 1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 23 The Observation of the Reaction of the Wool with Bases (Alkali), Hyhrogensulfite, Formaldehyde and Thioglycolic acid was revealed, that Cystine in the Wool is possible to divide into two primary Parts (A+B) and (C+D) and four secondary Parts( A, B, C, D). The various Behaviour of the particular Parts of the Cystine is explained so, that Cystine is in the Wool bonded with various Amino acids, which have various Sidegroups. The most reactive Part (A+B) je either near to or surrounded by polar Sidegroups, whereas less reactive Part is connected with nonpolar Sidegroups. The four Fractions of the KERATIN 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 24 Creation of the new BRIDGES (Bonds) Except for minor Exceptions is the Wool different from another textile Fibres by that, containing Covalent Cross Bonds which connect the main Peptide Bonds of the Backbone. As a Consequence (Result) of this, the Wool is insoluble in the Polar Solvents and is swollen by in such Solvents, having relatively high wet Strength. These Properties can be changed by cleavage of the disulphide Bonds. The wet Strength is decreased in direct proportion to the Number of the ruptured Cross Bonds. The Endeavour is focused for long time already to establish (constitute) a new Cross Bonds, more resistant than disulphide Bonds. The Constitution of the new Cross Bonds in the Wool has not only scientific Importance, but also a practical one also. So e.g. by the Constitution of the new Cross Bonds is lowered a Tendency to Wool felting power as the Results of the lower elasticity of the Wool Fibres. The Resistance to Alkali and the common clothes Moth is also increased. The Cross Bonds can be constituted in the Wool by scission of the disulphide Bonds and their replacing by other, more resistant Bonds. The Way is the Reaction with polyfunctional Compounds, which can react other reactive amino Groups, amide Groups, carboxylic Groups, Phenolic Groups. KERATIN Crosslinking 1 •Crosslinking Reagents January 10/2018 NATURAL POLYMERS MU SCI 10 2018 25 síťovací činidla na keratin.jpg KERATIN Crosslinking 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 26 síťování keratinu 1.jpg HF must removed (neutralised) by some Way! KERATIN Crosslinking 3 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 27 síťování keratinu 2.jpg HF must removed (neutralised) by some Way! ovat KERATIN Crosslinking 4 - FORMALDEHYDE January 10/2018 NATURAL POLYMERS MU SCI 10 2018 28 AMINO ACIDS presented In the Equations are written as the Functional Groups only! The Formulae are not corresponding to the AMINO ACIDS presented bellow. The Optimal reaction Course at Proteins is with 4 % w/w Formaldehyde at 70 °C and pH 3 – 7. The Cross Bonds in the Wool in the Acid Environment are created by Reaction of the Glutamic acid with the Guanidyl Residue from Arginine. The Cross Bonds created by this way are Resistant to Alkali, but are broken by Acids. The Wool Solubility in Alkalis so treated Wool deceases from approx. 13 % w/w. R-NH2 + HCHO R.NHCH2OH R-NH.CH2.OH + H2N-CO-R’ R-NH.CH2-NH-COR’ January 10/2018 NATURAL POLYMERS MU SCI 10 2018 29 Glutamic acid (Glu, E) Amminoacido_glutammina_formula.png Arginine (Arg, R) Amminoacido_arginina_formula.png KERATIN Reakctions – Grafting of other Monomers January 10/2018 NATURAL POLYMERS MU SCI 10 2018 30 Creation of the POLYMERS in the Fibre The POLYMERISATION from the Solution or form the Gas Phase creates the Increase of the Wool Weight, Strength and Decrease of the felting Power. The most well known is the Ethylenesulphide, especially in the Presence of various Catalysts (Peroxides, Per sulphate). The Ethylenesulphide reduces the Disulphidic Bonds at first and then the POLYMERISATION in the Fibre start and goes on. The Methylmethacrylate and the Metacrylic acid are also suitable for this POLYMERISATION in the Fibre. R-CH2-SH + n (CH2)S RCH2S(CH2.CH2.S)n-1.CH2CH2SH KERATIN Crosslinking - Quinone January 10/2018 NATURAL POLYMERS MU SCI 10 2018 31 Benzoquinone reacts with the Amino group or with the –SH Group as follows: síťování Keratinu chinony 001.jpg The Optimal reaction Course is at pH 3 – 7. Reaction with Quinone is employed for the Wool increase of Strength since a long time ago. The Quinone treated Wool is more resistant to chemicals and has lower tendency to the felting Power. The Tensile Strength Increase is higher than using other Reagents able to create the Cross Bonds. It is explained by the easy ability of the Benzoquinone polymerise in the Wool. KERATIN Crosslinking – Polyfunctional Alkylation Reagents 1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 32 Chlormethylethers react with the Wool in the organic Solvents Medium and creates the Cross Bonds. The Reaction goes PROBABLY as follows: RNH2 + ClCH2OCH2Cl > RNHCH2OCH2Cl + R1COOH > RNHCH2OCH2OOCR1 The other bifunctional Reagents, e.g. Ethyleneimis, 1,3-difluoro-4,6-dinitrobenzen, bisepoxides, were tested also: It was revealed by this that in the acetylated Wool cannot be created the Cross Bonds, whereas in the esterified Wool it was possible. síťování Keratinu chinony 002.jpg KERATIN Crosslinking – Polyfunctional Alkylation Reagents 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 33 síťování keratinu přes dibrometan.jpg So modified Wool is much more resistant to Bases, Acids, Oxidising Agents a Reduction agents Phase Transitions of KERATIN 1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 34 DTA, DTG, TG KERATINU na vzduchu.jpg Evaporation of the Water a Keratin (Coil) > b Keratin (Folded (Pleated) Sheet) The greatest Decrease of the Phase Transition Temperature of KERATIN goes with Increase of the Water Content in the interval 12 – 17 % w/w. The Phase Transition Temperature of the a KERATIN goes in Temperature Region 210 – 213 °C. The Phase Transition Temperature of the enlarged (strained) b KERATIN Wool Fibre (b Keratin (Folded (Pleated) Sheet) into Amorphous KERATIN is in the Temperature Region 220 – 225 °C. It is clear from this, that the b Keratin (Folded (Pleated) Sheet is more resistant to the Influence of the Temperature. DTA and TG Curves 100 % w/w of Wool heating up to 300 °C in Air Phase Transitions of KERATIN & FIBROIN 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 35 DTA, DTG, TG KERATINU na vzduchu.jpg On Air > OXIDATION > Burning already at approx. 230 °C DTA keratinu X fibroinu obrázek.jpg Decomposition in NITROGEN is only at higher Temperature and is more slowly FIBROINE is more Temperature stable than KERATIN (Phase Transition Temperature ) DTA and TG Curves 100 % w/w of Wool heating up to 300 °C in Air a Keratin (Coil) > b Keratin (Folded (Pleated) Sheet) Evaporation of the Water DTA Curves in the NITROGEN: 1) Human Hair, 2) Mohair Wool, 3) Natural/Genuine silk 1 2 3 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 36 Keratin Colouring REACTIV COLOURS for KERATIN January 10/2018 NATURAL POLYMERS MU SCI 10 2018 37 Reaktivní barvivo dichlortriazin a keratin.jpg January 10/2018 NATURAL POLYMERS MU SCI 10 2018 38 Preservation of Keratinu against to clothes Moth Pest Hindrance of Wool and Furs against to clothes Moth are employed either Substances without bond to the Keratin Molecules or the Substances directly bonded to the Keratin Molecules. These bonded Substances are usually Chlorine containing Compounds, e.g. dichlorodiphenyltrichlormethan. This Compound is bonded to Keratin irreversibly and is impossible to extract it. This Bond is also hydrolytic stable. There are also other Possibilities to get permanent Resistance to clothes Moth. The Situation is changed from time to time, because new Data regarded to the Danger to Humans. An well known Example is so called DDT (Substance without bond to the Keratin Molecules), which was banned years ago already. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 39 Preservation of Keratinu against to clothes Moth – an EXAMPLE of the Reactiv (PERMANENT) Substance directly bonded to the Keratin Molecules MITIN FF PROTI MOLŮM ChemIndex_action_1_.gif MITIN FF Sheep's Wool - Structure of the KERATIN Part •It can be in two Chains’ Secondary Structures: §a Left-handed Helix §b Folded (Pleated) Sheet va Helix is changing during elongation at higher Temperature (approx. 85 °C) to b Folded (Pleated) Sheet vb Folded (Pleated) Sheet forms the INTERFIBRES’ PART between a Left-handed Helixes and their Aggregate (Complex) creates the MACROSCOPIC Sheep's Wool Fibre •Sheep's Wool Fibre is so Composite Structure, where are some Components and cross Design (Bonds between particular Macromolecules) • • • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 40 Sheep's Wool - Structure Hierarchy 1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 41 The Model of the a KERATIN in the Sheep's Wool Fibre: a)Protofibril composed from three a Helixes b)Microfibril composed from eleven Protofibrillas c)Cross Cut of the Sheep's Wool Fibre with Dividing of the Core Part into ORTHO and PARA Share (Part): 1.Papilla 2.Wool Fibre 3.Para Part of the Core Share (Part) 4.Wool Cuticle 5.Outer Sheath of the Wool’s Root 6.Henley’s Layer 7.Huxley’s Layer 8.Inner Sheath of the Wool’s Root Struktura vlákna ovčí vlny 001.jpg Left-handed a triple Helix Sheep's Wool - Structure Hierarchy 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 42 Left-handed a triple Helix Struktura vlákna ovčí vlny 002.jpg The Model of the Sheep's Wool Fibre: a)Wool Fibre b)Fibrilla (Fibril) c)Microfibril d)Microfibril Cross Cut 1.Cortex Cell 2.ORTHO Cortex 3.PARA Cortex 4.Left-handed a triple Helix 5.Protofibril Sheep's Wool - Structure Hierarchy 3 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 43 Sekundární struktura bílkovin 022.jpg Sekundární struktura bílkovin 021.jpg Sekundární struktura bílkovin 020.jpg Sekundární struktura bílkovin 019.jpg Left-handed a Helix Sheep's Wool – Fibre's Morphology •Outer Sheath = CUTICLE = cell Wall which creates Scale Surface of the Fibre oriented Points (Darts) •Inner Sheath = CORTEX = cortical Part formed by Fibres oriented in the Fibres Direction •Pith = Medulla = it cerates inner Part of the Fibre and is divided into closed Air Bubbles > it is the Reason of the Thermal isolation properties Part of the Wool • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 44 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 45 TECHNICAL IMPORTANCE OF THE WOOL CONSTITUTION It is well known, that the Content of some Amino acids (e.g. Cystine, Cysteine, Tyrosine, Lanthionine) is influenced (DESREASED) by the Weather. The Wool can be seriously damaged during Processing. So the Alkalic washing Bath or the Colouring in the neutral Bath at high Temperature or at high Pressure. The Damage is the hydrolytic Cleavage of the Peptide Bonds. The Carbonisation of the Wool by H2SO4 or by the Acid Salts at 100 – 130 °C has the same undesirable Effect. The Bleaching of the Wool by oxidation Substances can create the irreversible Oxidation of the Cysteine. It is well known, that the Wool is very Elastic, it can be strained up to 60 – 70 %. If the strained Wool is left in the cold Water, the Wool is shrunk back to the initial Length. If the Wool is stretched out in the hot Water or in the Steam and then cold in that stretched State, it keeps the elongated (stretched) length. This Phenomena is the Principle of the so called „ Crabbing“ and the Manufacture of the elastic Wool Fabric. It is usually explained so, that the a Configuration is transformed to the b Configuration at simultaneous Orientation in the Longitudinal Axis. The Hydrogen Bonds between Backbones are released by Action of the hot Vapour or the hot Water and the Backbones can slip one on the other to the new Equilibrium State. In that new Equilibrium State can arise new Hydrogen Bonds between Backbones and new stable Configuration. The Wool give in so called „ Felting“. It is sometime desirable, sometime undesirable. To prevent Wool against „ Felting“, there are many Modifications. The most of them is based on the Surface chemical modification, mostly on chloration. The Care must be paid to side Reactions, which can lead to undesirable Wool Damages. Sheep's Wool - b Keratin (Folded (Pleated) Sheet) January 10/2018 NATURAL POLYMERS MU SCI 10 2018 46 img082.jpg Schema showing the Protein’s b Keratin (Folded (Pleated) Sheet) Structure a)PARALEL arrangement b)ANTIPARALEL arrangement The Backbone is bonded by the Covalent Bonds in the a Axis Direction. The Backbone is bonded by the Hydrogen Bonds in the b Axis Direction. The Backbone is bonded by the Wan der Waals Forces in the c Axis Direction. Sheep's Wool - b Keratin (Folded (Pleated) Sheet) January 10/2018 NATURAL POLYMERS MU SCI 10 2018 47 220px-Beta_sheet_bonding_antiparallel-color_svg.png 220px-Beta_sheet_bonding_parallel-color_svg.png ANTIPARALEL arrangement PARALEL arrangement Sheep's Wool - Composition Component % w/w Remark MAIN FIBRE (KERATIN) Rest up to 100 % w/w SHEEP’S FAT (LANOLIN) 5 – 15 Acid Esters Mixture (it is stated up to 36) with Alcohols (it is stated up to 23 aliphatic), Sterols (mainly Cholesterol) Impurities 5 – 20 Plant Rest 1 – 5 Moisture 8 - 12 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 48 Scale like Structure of the Sheep's Wool January 10/2018 NATURAL POLYMERS MU SCI 10 2018 49 naturalwoolfiber-closeup.jpg January 10/2018 NATURAL POLYMERS MU SCI 10 2018 50 img907.jpg Optical Microscop, it is not given, which Animal is the Source Wool Magnificatin 180 x Wool Cross Cut Magnificatin 500 x January 10/2018 NATURAL POLYMERS MU SCI 10 2018 51 img542.jpg img544.jpg img543.jpg Inner Structure Sheep's Wool and other Animals’ Hairs Sheep Rabbit Wild Cat KUTIKULA CORTEX MEDULA January 10/2018 NATURAL POLYMERS MU SCI 10 2018 52 UNDERHAIR is the fine, thick, usually unmarked coloured and functions as the ISOLATION LAYER. It is constituted from the fine, dense grown short Fibres. It forms the typical structure, called WOLL of some domestic or wild Animals (Sheep, Camel, Rabbit, Lama etc.). The UNDERHAIR function is the thermal Insulation during both Summer (Heat) and Winter (Cold). GUARD HAIR is the long, rough, straight Hair, which overhangs UNDERHAIR and functions as the Guard. GUARD HAIR is of various Length and thick and is carries out the typical Colour of the particular Animal’s Colour. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 53 P1040290.JPG Cat Male Hugo is the HOME CAT, but well hairy for the outdoor Life Hugo’s Hair January 10/2018 NATURAL POLYMERS MU SCI 10 2018 54 kocour chlup 500x.jpg kocour chlup 1kx.jpg GUARD HAIR UNDERHAIR January 10/2018 NATURAL POLYMERS MU SCI 10 2018 55 kocour chlup 2kx.jpg kocour chlup 4kx.jpg GUARD HAIR Hugo’s Hair January 10/2018 NATURAL POLYMERS MU SCI 10 2018 56 kralik 5kx b.jpg Rabbit – unknown Origin kocour chlup 5kx.jpg Hugo’s Hair UNDERHAIR Main Sources of the KERATIN Fibres •Sheep •VICUNA, that is Lama vicugna (Vicugna vicugna) it is the wild Species of Llama •Lama pacos, that is Alpaka – domesticated Llama with silky Fleece •Mohair from angora Goat •Angora Rabbit •……………… January 10/2018 NATURAL POLYMERS MU SCI 10 2018 57 From the Sheep’s Wool to the Felt January 10/2018 NATURAL POLYMERS MU SCI 10 2018 58 1.NONWOVEN TEXTILE 2.Wet Felting 3.Needle Felting •Sheep’s Wool is very suitable for the Felting, because having small scale KUTIKULA Fibre’s „Thickness“ dtex •dtex – it is not any REAL THICKNESS! •dtex - it is the Mass of the 10 km of Fibre expressed in Grams •The English Unit is denier, what is the Mass of the 10 000 yards (approx. 9000 m) of Fibre expressed in Grams •The Units dtex and denier are used for Expression of the Textile Fibres Strength. Its Strength is measured as the Force (N), not as the Mechanical Stress (N/m2) •So called „Textile Strength“ is then expressed as (in) cN/dtex (cN/denier) • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 59 Sheep’s Wool Strength Fibre Tensile Strenght (cN/dtex) Elongation at Break (%) E-Modulus (N/tex) Moisture uptake (%) Woll 0,90 – 2,18 25 – 35 0,34 16 –18 Polyester 4,00 – 6,50 15 – 40 9 –11,5 0,5 – 0,8 Viscose 1,80 – 3,50 15 – 30 5,4 26 – 28 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 60 The Source don’t get Information, if these Values are for Measurement „At dry“ or „At wet“. PROBABLY IT COULD BE „At dry“, because Values „At wet“ are usually lower then state here. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 61 SEM – by Courtesy of Miss Mgr. Gabriela Vyskočilová modra nit 10kx (2).jpg Sheep’s Wool, coloured, treated, TEXTIL FIBER modra nit 15 kx (2).jpg Typical SMALL SCALE on the Surface Treatment of the Sheep’s Wool •WOOL CARBONIZATION – removal of Dirt from the Wool using concentrated H2SO4 •Modification against Felting up (Removing of the SMALL SCALE on the Surface by Oxidation and Mechanical Separation) •……………. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 62 modra nit 10kx (2).jpg January 10/2018 NATURAL POLYMERS MU SCI 10 2018 63 WOOL CARBONIZATION is the chemical Process, which Reason is removal from the Sheep’s Wool all the Plant (vegetable) Impurities E.g. Straws and Culms, Leafs, Grass etc. WOOL CARBONIZATION can be done at Dry or at Wet Conditions. Wet Process The strong inorganic Acid is used most frequently, e.g. (H2SO4 or HCl) or the Salt with acid Reaction, e.g. (NH4)2SO4). The Wool is resistant for short Time even at high temperature, e.g. Approx. 15 minutes at 90 -110 °C. The Plant (vegetable ) Impurities (Cellulose based material) are carbonised and change to Brittle State. The Products arisen are easy to crush and the remove. It is possible and mostly done to carbonise both Fabric and Flocks. Dry Process The Vapour of HCl is mostly used for this technology. This Procedure is employed less frequently then the Wet Process, despite it is Efficient and fast. The Machinery is expensive , because of Corrosiveness of the HCl , which is also Hazardous Chemical. •2. LANOLIN January 10/2018 NATURAL POLYMERS MU SCI 10 2018 64 •LANOLIN January 10/2018 NATURAL POLYMERS MU SCI 10 2018 65 Lanolin.png It is nothing special on the first Sight LANOLIN is further purified for the Cosmetic use to be Colourless Raw Sheep’s Wool from one Sheep (one cutting) contains approx. 100 – 300 ml of Lanolin It is NOT a Glyceride! January 10/2018 NATURAL POLYMERS MU SCI 10 2018 66 Lanolin also called wool wax or wool grease, is a wax secreted by the sebaceous glands of wool-bearing animals. Lanolin used by humans comes from domestic sheep breeds that are raised specifically for their wool. Historically, many pharmacopoeias have referred to lanolin as wool fat (adeps lanae); however, as lanolin lacks Glycerides (glycerol esters), it is NOT a true fat. Lanolin primarily consists of sterol esters instead. Lanolin's waterproofing property aids sheep in shedding water from their coats. Certain breeds of sheep produce large amounts of lanolin. There is an inverse correlation between wool fiber diameter and lanolin content. Lanolin's role in nature is to protect wool and skin from climate and the environment; it also plays a role in skin (integumental) hygiene. Lanolin and its derivatives are used in the protection, treatment and beautification of human skin. A typical high-purity grade of lanolin is composed predominantly of long chain waxy esters (approximately 97% by weight) the remainder being lanolin alcohols, lanolin acids and lanolin hydrocarbons An estimated 8,000 to 20,000 different types of lanolin esters are present in lanolin, resulting from combinations between the 200 or so different lanolin acids and the 100 or so different lanolin alcohols identified so far. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 67 Lanolin and its many derivatives are used extensively in both the personal care (e.g., high value cosmetics, facial cosmetics, lip products) and health care sectors such as topical liniments. Lanolin is also found in lubricants, rust-preventive coatings, shoe polish, and other commercial products. Lanolin, when mixed with ingredients such as neatsfoot oil, beeswax and glycerine (glycerol), is used in various leather treatments, for example in some saddle soaps and in leather care products •3. FIBROIN January 10/2018 NATURAL POLYMERS MU SCI 10 2018 68 Where can be found FIBROIN? •Natural/Genuine Silk produced by Silkworm •Spider's is Protein Fibre from the Secret of Spiders Species Argiope and Nephila •Secret of the night Butterflies January 10/2018 NATURAL POLYMERS MU SCI 10 2018 69 Natural/Genuine Silk January 10/2018 NATURAL POLYMERS MU SCI 10 2018 70 •MOST OF THE Natural/Genuine Silk is gained from the Secret produced by Silkworm Moths. It is called „Endless“ natural textile Fibre •This FIBROIN has the typical PRIMARY STRUCTURE, as shown bellow: 800px-Silk_fibroin_primary_structure_svg.png January 10/2018 NATURAL POLYMERS MU SCI 10 2018 71 Fibre’s Properties Natural/ Genuine Silk Polyamide (PA 6) Polyester (PETP) Viscose (CV) Density (g/cm³) 1,25 1,14 1,33 1,52 dtex 1,17 1,0 1,1 1,4 Strength DRY (cN/dtex) 3-5 3,6-7,5 3,8-7,2 1,8-3,0 Strength WET (% of the DRY) 85 85 95-100 60 Elengation (%) 24 23-55 50-70 15-30 Water uptake (%) 30 3-4,5 0,3-0,4 28 World Consumption approx. (1000 t) 107 3.500 14.500 500 TYPICAL FIGURES ARE GIVEN IN THIS TABLE! January 10/2018 NATURAL POLYMERS MU SCI 10 2018 72 AMINO ACIDS COMPOSITION of some grades ot the Natural/Genuine Silk (the very minor Amino acids are not given) AMINO ACID Bombyx mori Tussah Caligula Tussah II Anaphe Chrasopha flava Glycine 43.6 23.6 23.9 41.7 23.5 Alanine 29.6 39.4 47.2 52.1 50.2 Serine 11.7 10.5 14.8 ----- 40.7 Asparagic acid 1.4 4.2 7.5 ----- ----- Glutamic acid ----- ----- 1.5 ----- ----- Tyrosine 4.8 4.4 10.6 ----- ----- Histidine 0.4 2.2 1.6 ----- ----- Arginine 1.7 9.2 5.4 2.1 1.8 Proline 0.4 0.3 0.4 ----- ----- Tryptophan 0.4 2.0 2.7 ----- ----- January 10/2018 NATURAL POLYMERS MU SCI 10 2018 73 P1020856.JPG P1020863.JPG P1020862.JPG P1020858.JPG January 10/2018 NATURAL POLYMERS MU SCI 10 2018 74 Silk cocoons Mulberry silk worms - Bombyx Mori January 10/2018 NATURAL POLYMERS MU SCI 10 2018 75 Silk production process January 10/2018 NATURAL POLYMERS MU SCI 10 2018 76 Degumming and stretching Preparing silk bedding January 10/2018 NATURAL POLYMERS MU SCI 10 2018 77 EXTRACTING RAW SILK The production process of silk can seem deceptively simple but indeed has several steps. In fact, the process of creating silk fibres of the highest quality take a few weeks to complete. Silk fibres are a continuous protein fibre created from natural processes and extracted from cocoons, which means that these fibres can retain the properties that are associated with the chemicals produced by the silkworm. When secreted by the silkworm, the natural state of the fibre is a single silk thread made up of a double filament of protein material (fibroin) glued together with sericin, an allergenic and gummy substance that is normally extracted during the processing of the silk threads. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 78 1.First, the new born larvae of the silkworms are kept in a warm and stable environment and given plenty of mulberry leaves, their favourite diet. 2.The silkworms naturally produce cocoons around themselves to pupate. This process is done through “spinning”: the worm secretes a dense fluid from its gland structural glands, resulting in the fibre of the cocoon. 3.The cocoons are sorted carefully according to size and quality. 4.Boiling water with soap is used unravel the silk fibres from the cocoon. This is known as the degumming process. 5.The outer shell of the cocoon is fed into into the spinning reel, which is still often operated manually 6.The long fibre thread that are extracted from the cocoon are then cleaned and stripped from any deficiencies. The degumming process •The Fibre is connected by Sericine in the COCOONS, which is the SOLUBLE GLYCOPROTEINE „guarding“ (protecting) the FIBROIN •SERICIN is dissolved in the boiling Water and so are the Fibres released •The Fats and Waxes are dissolved also •The only approx. 1 % w/w is the Ash (inorganic Materials) in the Fibre, the Rest are Proteins. January 10/2018 NATURAL POLYMERS MU SCI 10 2018 79 Natural/Genuine Silk SECUNDARY STRUCTURE bKeratin folded –(Pleated) Sheet • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 80 img082.jpg Schema showing the Protein’s b Keratin Folded (Pleated) Sheet Structure a)PARALEL arrangement b)ANTIPARALEL arrangement The Backbone is bonded by the Covalent Bonds in the a Axis Direction. The Backbone is bonded by the Hydrogen Bonds in the b Axis Direction. The Backbone is bonded by the Wan der Waals Forces in the c Axis Direction. Natural/Genuine Silk Fibre is very COMPLICATED (COMPLEX) STRUCTURE January 10/2018 NATURAL POLYMERS MU SCI 10 2018 81 img905.jpg It is so called TWINFIBRE CONNECTED BY SERICINE (so called Silk Glue) of Length approx. 3000 – 4000 m Vodíkový můstek ve fibroinu.jpg Hydrogen Bond of the FIBROIN’s PRIMARY FIBRES SECUNDARNÍ FIBRES a) The Crosscut of the Natural/Genuine Silk Fibre 1.Sericine Skin 2.Sericine’s Core 3.Fibroin’s Fibre Cubicula 4.Fibroin’s Fibre Core 5.Fibroin’s Fibre central Part (Zone) b) Longitudinal cut of the Natural/Genuine Silk Fibre 3.Fibroin’s Fibre Skin 4.Fibroin’s Fibre Core 5.Fibroin’s Fibre central Part (Zone) c) Polypeptide Chains of Fibroine in the ANTIPARALEL CONFORMATION b) a) c) Phase Transitions of KERATIN & FIBROIN 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 82 DTA, DTG, TG KERATINU na vzduchu.jpg On Air > OXIDATION > Burning already at approx. 230 °C DTA keratinu X fibroinu obrázek.jpg Decomposition in NITROGEN is only at higher Temperature and is more slowly FIBROINE is more Temperature stable than KERATIN (Phase Transition Temperature ) DTA and TG Curves 100 % w/w of Wool heating up to 300 °C in Air a Keratin (Coil) > b Keratin (Folded (Pleated) Sheet) Evaporation of the Water DTA Curves in the NITROGEN: 1) Human Hair, 2) Mohair Wool, 3) Natural/Genuine silk 1 2 3 CHEMICAL REACTIONS AND SOLUBILITY OF THE FIBROIN 1 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 83 •Decomposition by Acids (more Efficient) and Alkali •OXIDATION (Chlorine) •ACETANHYDRIDE, ALKALIC METALLS AND ALKALIC EARTH SALTS •HEAVY METALLS SALTS, MAINLY STANNUM (TIN) > Natural/Genuine Silk takes up 100 % w/w > „WEIGHTING“ of the Natural/Genuine Silk •Formation of the Cross Bonds CHEMICAL REACTIONS AND SOLUBILITY OF THE FIBROIN 2 January 10/2018 NATURAL POLYMERS MU SCI 10 2018 84 •Decomposition by Acids (more Efficient) – hot concentrated HCl dissolves Natural/Genuine Silk in 30 minutes QUANTITAVELY •OXIDACTION – H2O2, KMnO4 at higher concentration damages Natural/Genuine Silk •CHLORINE •ACETANHYDRIDE, ALKALIC METALLS and ALKALIC EARTH SALTS and also e.g. ZnCl2 dissolves Natural/Genuine Silk (similar as the PA6) •Formation of the Cross Bonds – via more complex organic Substances Natural/Genuine Silk Fibre OPTICAL MICROSCOPY January 10/2018 NATURAL POLYMERS MU SCI 10 2018 85 img906.jpg Natural/Genuine Silk Magnificatin 180 x Natural/Genuine Silk (CROSS CUT) Magnificatin 500 x January 10/2018 NATURAL POLYMERS MU SCI 10 2018 86 img909.jpg img908.jpg Fibre’s Thickness of the Sheep’s Wool and Natural/Genuine Silk at the same Magnification Sheep’s Wool Magnificatin 180 x Natural/Genuine Silk Magnificatin 180 x SUROVINOVÝ VÝZNAM Natural/Genuine Silk Fibre •Natural/Genuine Silk is the very exclusive textile raw Material •Annual World Production is only approx. 300 000 t/annum •China is the principal Producer now •There were many Attempts to start the Natural/Genuine Silk Production in Europe, but they ended unsuccessfully • January 10/2018 NATURAL POLYMERS MU SCI 10 2018 87