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Helmut Zahn, Deutsches Wollforschungsinstitut an der RWTH Aachen, Aachen, Federal Republic of Germany (Chaps. 1, 2.1, 2.2, 6 – 11, 13) Franz-Josef Wortmann, Deutsches Wollforschungsinstitut an der RWTH Aachen, Aachen, Federal Republic of Germany (Chaps. 2.3, 3.1) Gabriele Wortmann, Deutsches Wollforschungsinstitut an der RWTH Aachen, Aachen, Federal Republic of Germany (Chap. 8, 10) ¨ Karola Schafer, Deutsches Wollforschungsinstitut an der RWTH Aachen, Aachen, Federal Republic of Germany (Chaps. 3.2, 5.4, 5.5, 10, 13) Rainer Hoffmann, Hochschule Bremen, Bremen, Federal Republic of Germany (Chaps. 4, 5.1 – 5.4, 12) Robert Finch, Woolmark Europe, Inc., Ilkley, United Kingdom (Chaps. 11, 12)
1. 1.1. 1.2. 1.3. 1.4. 2. 2.1. 2.2. 2.3. 3. 3.1. 3.2. 4. 4.1. 4.2.
Introduction . . . . . . . . . . . . . . . . Deﬁnition . . . . . . . . . . . . . . . . . . Historical Aspects . . . . . . . . . . . . Biology . . . . . . . . . . . . . . . . . . . Chemical Composition . . . . . . . . . Structure . . . . . . . . . . . . . . . . . . Morphology . . . . . . . . . . . . . . . . α- and β-Keratin . . . . . . . . . . . . . Two-Phase Model . . . . . . . . . . . . Properties . . . . . . . . . . . . . . . . . Physical and Mechanical Properties Chemical Reactivity . . . . . . . . . . . Resources and Raw Materials . . . . Sheep Rearing and Breeding . . . . . Places of Origin and Types of Raw Wool . . . . . . . . . . . . . . . . . . . . .
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2 2 2 3 3 6 6 7 9 10 10 13 15 15 16
5. 5.1. 5.2. 5.3. 5.4. 5.5. 6. 7. 8. 9. 10. 11. 12. 13. 14.
Production Processes . . . . . . . . . . Methods of Obtaining Wool . . . . . Raw Wool Scouring . . . . . . . . . . . Mechanical Processing . . . . . . . . . Chemical Processing: Pretreatment Dyeing and Finishing . . . . . . . . . . Environmental Protection . . . . . . . Quality Speciﬁcations . . . . . . . . . . Testing and Analysis . . . . . . . . . . Storage and Transportation . . . . . Uses . . . . . . . . . . . . . . . . . . . . . Trademarks . . . . . . . . . . . . . . . . Economic Aspects . . . . . . . . . . . . Toxicology and Occupational Health References . . . . . . . . . . . . . . . . .
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Today, wool accounts for only ca. 3 wt % of world textile-ﬁber production. However, if the value added by dyeing and printing is included, the share in monetary terms is considerably higher. The importance of wool is due to its unique physiological properties as a clothing material and the wide range of techniques for converting it into textiles, including felts and ﬁnishing processes. Some important methods and discoveries in modern biological sciences had their origins in wool research (partition and paper chromatography, the structure of α- and β-keratin, intermediate ﬁlaments).
The production of wool and woolen textiles and the trade in these commodities have played an important role in political and economic history.
The natural ﬁber wool, like other types of ﬁne and coarse animal hair and also silks (→ Silk), is an animal ﬁber , and although the term “wool” can be used in conjunction with the names of various animals, e.g., “angora wool”, it is here understood to include only the hair of the various breeds of domesticated sheep (Ovis aries).
c 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim 10.1002/14356007.a28 395
Wool sheep, bred in Spain, produced wool of very ﬁne quality, and in the late 1700s Saxon merinos were exported via England and South Africa to Australia, where the climate proved to be very favorable for rearing this breed.
Wool ﬁbers and other animal hairs, including human hair, are formed in follicles – sheath-like formations of the epidermis, at the base of which are papillae of mesodermal cells (Fig. 1). Follicles are dynamic organs in which various processes occur simultaneously: cell division, cell differentiation, upward movement of the keratinocytes, biosynthesis of wool proteins as gene products, self-assembly of the proteins to form supramolecular structures, and ﬁnally keratinization (corniﬁcation) by formation of crosslinked disulﬁde and isodipeptide bridges. At the same time, cells of the inner and outer root sheath are catabolized . The various stages of development of the growing wool ﬁber in the follicle can be divided into six zones (Fig. 1). In the upper part of Zone 1, ﬁne keratin intermediate ﬁlaments (KIF) and trichohyalin granules are already forming. Between Zones 1 and 2, ﬁlaments aggregate to form macroﬁbrils, in which keratin-associated proteins (KAP) are deposited. In Zone 2, amorphous protein aggregates, ca. 30 nm in diameter, form in the ﬁber cuticle cells. By the end of Zone 2 the cuticle cells are hardened, while the ﬁnal keratinization of the entire wool ﬁber occurs in Zone 3.
Figure 1. Diagram of fully developed wool follicle (not to scale)  The six zones are: 1) Bulb; 2) Keratogenous zone; 3) Zone of ﬁnal hardening of the ﬁber; 4) Zone of inner root sheath degradation; 5) Zone of sloughing of inner and outer root sheath cells; 6) Pilary canal. AG = aprocine gland; AP = arrector pili; B = bulb; CTS = connective tissue sheath; DP = dermal papilla; E = epidermis; GM = glassy membrane; IRS = inner root sheath; ORS = outer root sheath; SG = sebaceous gland
1.2. Historical Aspects [55–57]
The wool of the sheep was the ﬁrst textile raw material used by humans for clothing purposes. The development of clothing began when people ﬁrst dressed themselves in the skins of mammals. Felts, which are more easily shaped, were produced later from hairs plucked or cut from the animal (→ Felts). The development of spinning and weaving to produce fabrics was a still later development. The ﬁrst country to process and trade in wool was Babylon (Babylonia = land of wool). The oldest known wool fabrics, dating from the second half of the second millennium b.c., were found in Danish tree cofﬁns. Sheep rearing reached a high point in the Middle Ages and the Renaissance. The merino
1.4. Chemical Composition [27, 31]
The protein ﬁber wool consists of carbon, hydrogen, oxygen, nitrogen, and sulfur. The elemental analysis of wool (free of water) is as follows:
Carbon Hydrogen Oxygen Nitrogen Sulfur Ash 50.5 wt % 6.8 wt % 22.0 wt % 16.5 wt % 3.7 wt % 0.5 wt %
Except for the sulfur content, this composition is typical for all proteins. The high sulfur
Wool content is due to the high content of cystine, a double amino acid containing two sulfur atoms in a disulﬁde bond:
HOOCCH(NH2 )CH2 S−SCH2 CH(NH2 )COOH
The side chains, which in wool account for a considerable proportion (50 %) of the protein material, interact with each other, thereby stabilizing the peptide by forming links between the chains and rings within a chain:
The ash contains potassium, sodium, calcium, aluminum, iron, silicon, sulfate, carbonate, phosphorus pentoxide, and chloride. Water-free wool consists mainly (ca. 97 %) of wool proteins, the remainder being made up of ca. 2 % structural lipids (Fig. 2) [59–62], ca. 1 % mineral salts, nucleic acids [63, 64], and carbohydrates. Industrially scoured wool has only small residual amounts of wool grease (ca. 0.5 %). The structural lipids, in contrast, are components of the cell membrane complex which binds together the cuticle and cortex cells. A characteristic of the structural lipids of the cuticle is the presence of a covalently bound branched-chain C21 fatty acid 18methyleicosanoic acid [65–67]. Total hydrolysis of the peptide bonds in wool proteins yields 24 amino acids. The data given in Table 1 were obtained by combining data from acidic and from enzymatic hydrolyses of wool. The amino acids are classiﬁed in ﬁve groups: “acidic” amino acids, “basic” amino acids, amino acids with hydroxyl groups, sulfur-containing amino acids, and amino acids with no reactive groups in the side chain. The total amount of amino acids with reactive side chain groups is 5395 µmol/g, and of amino acids without reactive side chain groups 3450 µmol/g. The sum of these two ﬁgures, after subtraction of the concentration of C-terminal amino acids (10 µmol/g), gives a ﬁgure of 8835 µmol/g for the concentration of peptide groups in the peptide chains of wool. Like all proteins, wool contains both cationic and anionic groups, and is therefore amphoteric. The cationic character is due to the protonated side chains of arginine, lysine, and histidine, and to the small number of free amino groups at the ends of the peptide chains. The amino groups of lysine, histidine, the amino end groups, and the thiol groups of cysteine are important sites for the covalent attachment of reactive dyes . Anionic groups are present as dissociated side chains of aspartic and glutamic acids and as carboxyl end groups.
This structural formula is a schematic representation of ﬁve such links between segments of two hypothetical peptide chains. From the top downwards it shows interactions between phenyl rings (for the role of aromatic rings as hydrogen bond acceptors see ), hydrogen bonds between an asparagine residue and a serine residue, a salt bridge between an arginine residue and a glutamic acid residue , a disulﬁde bridge between two cysteine residues, and an isodipeptide bridge between glutamic acid and lysine [71, 72]. The disulﬁde bridge plays an important part in stabilizing the wool ﬁber, leading in particular to its relatively high wet strength, moderate swelling, and insolubility. A second covalent bridge is provided by the isodipeptide N ε -(γglutamyl)lysine, which provides an additional stabilizing effect in the corniﬁed cell envelopes of the cortex and cuticle. The so-called salt bridge is due to the electrostatic interaction between cationic and anionic side-chain groups. Hydrogen bonds are formed in proteins between
alanine. Structural lipids as donors and as acceptors. and these fractions can be separated into deﬁnite proteins. The dissolved S-carboxymethylated wool proteins can be separated into the main groups listed in Table 2. valine. glycine. S-Carboxymethylated soluble wool proteins can be obtained by exhaustive mercaptolysis and carboxymethylation of the resulting SH groups [75–77]. and glutamic and aspartic acids. In two-dimensional polyacrylamide gel electrophoresis . and. the acid hydrolysis of wool liberates 50 µmol/g acetic acid . 3). serine.4-dinitroﬂuorobenzene: cystine. in the presence of sodium dodecylsulfate (SDS). some of which have been sequenced . especially in the helical rod domains of the keratin ﬁlaments. Hydrophobic effects stabilize the aggregation of nonpolar side chains. Thus. The keratins are well separated from the sulfur-rich proteins be- . the proteins are ﬁrst separated according to charge. The three-dimensional structure of the wool proteins is stabilized both by the hydrophobic effect and by a wide variety of electrostatic interactions between amino acid constituents . Other Nterminal amino acids are present in N-acetylated form. so reducing the area of the interface with water. The heterogeneity of this class of proteins can thus be demonstrated by a relatively simple analytical process. according to molecular mass (Fig. Eight N-terminal amino acids have been analyzed by means of 2. threonine. in the second dimension.4 Wool Figure 2.
2. which together with some other protein ﬁlaments are classiﬁed as intermediate ﬁlaments [81–84]. Amino acid composition of ﬁne merino wool ∗  5 cause of their high molecular mass. and the high glycine – tyrosine proteins are nearly at the front of the SDS dimension because their molecular mass is very low. The keratins in wool come from the microﬁbrils. Structure 2. In coarse ﬁbers. there is also a central medulla (Fig. and are thus larger than actin ﬁla- ments and smaller than the microtubuli  of the cell. Intermediate ﬁlaments form an important ﬁlamentary system in the cytoplasm of higher eukaryotic cells. Some of the heterogeneity of the keratins is caused by phosphorylation .Wool Table 1.1. They have a diameter of 8 – 10 nm. Morphology [85–89] Wool ﬁbers consist of two cell types: cuticle and cortex cells. The cuticle  consists of plate-shaped cells (“scales”) that overlap longitudinally and . 4).
peripherally. enveloping individual microﬁbrils and their aggregates. Two-dimensional polyacrylamide gel electrophoretic separation of wool proteins . Between overlapping cuticle cells is the cell membrane complex. The stability of the α-helix is due to intramolecular hydrogen bonds between the >C=O groups of the peptide bonds and adja- . (Fig.98 nm).and β -Keratin The microﬁbrils are partly crystalline. The cortex consists of spindle-shaped interdigitated cells . The natural color of brown wool is caused by pigment granula of black to brown eumelanin and yellow to red pheomelanin. with the 1 µm thick edges of the scales pointing in the direction of the tip of the ﬁber. This intermacroﬁbrillar material swells in water more than the macroﬁbrils. Wool that has been stretched by ca. para. The epicuticle consists of proteins and lipids. Proteins of the wool ﬁber  Type of protein Number of proteins Range of molecular mass.9 in one direction and in the presence of SDS in the other. and more rarely meso cells. the peptide chains are twisted like a right-handed screw (α-helix. UHS = ultrahigh sulfur. These consist of ortho. and endocuticle. 6 A) as α-keratin.2. A new interpretation for the α → β transition is given by CAO  and Kreplak et al.34 nm and equatorial reﬂections at 0. including covalently bound 18-methyleicosanoic acid. and on X-ray structural analysis give reﬂections on the meridian (0. 6 B). Each cuticle cell consists of four layers with different cystine and isodipeptide contents: epicuticle.98 nm. HS = high sulfur.6 Wool associated proteins (KAP) are intercalated. 50 % in water and then steamed gives a new ﬁber diagram with a meridian reﬂection at 0.465 nm and 0. exocuticle.51 nm) and equator (0. as well as many long-period reﬂections on the meridian and some on the equator. LS = low sulfur. This Xray diffraction pattern is due to the modiﬁcation known as β-keratin (Fig. Keratin- 2. 2). all differing in their cystine content and staining behavior with silver salts. kDa 40 – 50 56 Keratins Acidic keratins (Type I) Basic keratins (Type II) Keratin associated proteins (KAP) High-sulfur proteins 4 4 80 – 100 Ultrahigh-sulfur proteins High glycine – tyrosine proteins (Type I) High glycine – tyrosine proteins (Type II) 10 5 11 16 19 23 16 6–9 6–9 Figure 3. A macroﬁbril is a bundle of 500 – 800 keratin intermediate ﬁlaments (microﬁbrils). In α-keratin . Between the macroﬁbrils are cytoplasmic and nuclear remnants of the keratinocytes. . α. Astbury  designates the modiﬁcation that results in this ﬁber diagram (Fig. A cortex cell of wool contains around 5 – 8 macroﬁbrils with a diameter of 300 nm at their widest point. Fig. Table 2. The proteins were extracted from merino wool and subjected to electrophoresis at pH 8. a-layer. 7). which in turn consist of protoﬁlaments (Fig. HGT = high glycine – tyrosine The medulla in coarser wool ﬁbers consists of hollow cells with a skeleton of amorphous proteins and ﬁne ﬁlaments. An individual microﬁbril consists of protoﬁbrils. 5) .
. II) The 4. may be an eight-stranded subunit formed by the lateral aggregation of two four-stranded 3 nm protoﬁlament intermediates (shown on right). presumably one acidic (white) and one basic (black) species. depending upon protoﬁbril substructure. Longitudinal and cross section of a ﬁne merino wool ﬁber  Figure 6. alternatively. I) The 2 nm protoﬁlament consists of two coiled-coil keratin polypeptides. III) The 10 nm ﬁlament may comprise four (left) or three (right) protoﬁbrils. B) β-Keratin pattern Figure 5. or.5 nm protoﬁbril may be a six-stranded subunit composed of three 2 nm protoﬁlaments (shown on left). Schematic representation of the three distinct levels of ﬁbrillar organization in keratin ﬁlament assembly and architecture . The number of protoﬁbrils (four or three) per 10 nm ﬁlament is not unique but just represents one possible polymorphic form. Diagnostic X-ray reﬂections  A) α-Keratin pattern.Wool 7 Figure 4.
4).e. These dimers are the actual physical structural elements of the intermediate ﬁlaments (microﬁbrils).” In the β-keratin structure .1.8 Wool is formed by cross-linking of the chains by hydrogen bonds between peptide groups of opposing chains. The chains form socalled pleated sheet structures (Fig.e. and can be termed “molecular twins.. cent >N−H groups of amino acid units located on the next turn of the α-helix and intrahelical salt linkages. the intermicroﬁbrillar matrix. 3.34 nm corresponds with the geometry of the model. which includes the cuticle. i. Two-Phase Model The complex morphological and molecular structure of wool (Fig. Pleated sheet structure of β-keratin  2. The sheet . the helical chain must itself be slightly coiled (superhelix. Table 3 shows the stepwise differentiation of the morphological structure of the wool ﬁber into the most important two-phase structures. coiled coil).. the peptide chains are considerably stretched. Figure 8. α-Helix structure of α-keratin  The α-helix contains 18 amino acid units in ﬁve turns.51 nm). If only the α-helical central rodlike domains in the microﬁbrils (intermediate ﬁlaments) are regarded as microcrystalline.3. the essential difference between the components is in their degree of order. The phenomenon of the α → β transformation has been applied in the new developed OPTIM technology (see Section 5. the intermacroﬁbrillar matrix. the nonhelical ends of the keratin molecules or of the dimers. combining components with different properties in one material so as to maximize suitability for its purpose. 4) echoes the construction principle of all biological composite structures and many man-made materials. The sheet is folded at the −CHR groups of the chains to such an extent that the meridian reﬂection of the β-keratin X-ray diffraction pattern at 0. Chap.6 amino acid units per turn. rope-like assembly in which the superhelices are arranged such that the hydrophobic side chains on the outside of the helix interlink to form a stable “buttonhole” structure. On stretching the ﬁber in the linearviscoelastic region (ε < 0. With regard to elastic properties.). 2. i. The other components make up the noncrystalline phase. the behavior of the crystalline phase (hx) is linearly elastic and Figure 7. as in silk ﬁbroin (→ Silk. the crystalline phase accounts for 30 % of the ﬁber . Two superhelices combine to form a left-handed.8 %). the cell membrane complex. and 40 % of the microﬁbrils. 8). To give the distance between successive turns of the helix that leads to the observed meridian reﬂection (0. twostranded.
Survey. This fact can be explained by the low contents of individual components and their chemical and structural similarity.6 GPa.1 − 6. and the history of the wool (Fig. f/m = ﬁlament in matrix that of the noncrystalline matrix (nc) is linearly viscoelastic. 17. the . The adsorption and desorption curves exhibit hysteresis.31 g/cm3 at 25 ◦ C and 65 % relative humidity. → Fibers. depending on type and origin. ) Composite system Wool ﬁber Cortex Cortex cell Macroﬁbril Type ∗ r/c f/m f/m f/m Component 1 cuticle cortex cell macroﬁbrils microﬁbrils Component 2 cortex cell membrane complex intermacroﬁbrillar matrix intermicroﬁbrillar matrix 9 ∗ r/c = ring/core structure. 6. 114.8 − 9. Wool is hygroscopic. while they continue to exist in the crystalline region. This fact emphasizes the ideal arrangement and cooperation of the short α-helical segments in the microﬁbrillar crystal. 6. Testing and Analysis) 3. 48] (See also → Fibers. 9) [98. This value is remarkably close to the modulus of elasticity of crystalline ice. For small amounts of longitudinal strain in the linear-viscoelastic region. 0 ◦ C: E = 10 GPa). temperature.5 and 25 cm. The modulus of elasticity of the helices is  Ehx = 7. The elastomechanical behavior is satisfactorily represented by the simple Feughelman two-phase model . Physical and Mechanical Properties  Wool ﬁbers with no medulla have a density of 1. Moisture absorption of wool as a function of relative atmospheric humidity at 25 ◦ C  Water Absorption.5 GPa The ratio of the moduli of elasticity of the noncrystalline phase is in good agreement with the ratio of the corresponding torsion moduli (G d /G w = 10) . which is also stabilized by hydrogen bonds (ice I. At average relative humidities.6 GPa tional to its volume fraction. the relaxation behavior of a wool ﬁber shows no ﬁne structure ascribable to individual morphological components. Morphology of wool as a combination of two-component structures (see also Fig. The timedependent modulus of elasticity of the dry (d) and wet (w) noncrystalline phase (nc) are calculated to be d Enc = 3. 1. In a ﬁlament – matrix composite. all noncrystalline components behave as constituents of a homogeneous mixture. The elastic and viscoelastic properties of the ﬁber largely determine the crease resistance.Wool Table 3. For small deformations. The mean ﬁber diameter varies between 16 and 40 µm and the mean ﬁber length between 2. whereby the effect of each component is propor- Figure 9. The small difference between the values for the viscoelastic modulus of the noncrystalline phase in the dry state and the modulus of elasticity of the helical ﬁlaments is due to the fact that both components are stabilized mainly by strong hydrogen bonds which are broken under the inﬂuence of water in the noncrystalline phase. d w Enc /Enc ≈ 13 w Enc = 0.1. Properties [2. dimensional stability. drape. 6. 115]. and handle of a fabric. the torsion behavior is mainly a property of the matrix. and the amount of water taken up depends on the relative humidity of the air.
Above and below this point. and in the wet state 40 – 60 %. the elongation increases rapidly for small increases in stress. which is an important factor in the physiological effects of wool as a clothing material. on repeating the test. i. Point C lies between 25 and 30 % elongation. and is terminated by rupture of the ﬁber (D). b) Radial swelling. It has been shown that distinct domains of the keratin ﬁlaments undergo the α → β transformation in the three regions . 11). difference between the two curves is ca. If the ﬁber is then relaxed and kept in water at room temperature overnight or at ca. the fracture strain increases. Water absorption results in swelling. the moisture uptake of wool is accompanied by liberation of heat. Many physical and mechanical properties of wool depend on its moisture content. Although wool is hygroscopic. its surface is hydrophobic towards liquid water and is therefore difﬁcult to wet. is due to the fact that the interior of the ﬁber absorbs water vapor. Noteworthy is that when the wool ﬁber is stretched in water to point C at room temperature. the increase in tension that accompanies a given increase in elongation is larger.. but. Figure 11 shows the stress – strain behavior of a wool ﬁber in standard atmosphere of 65 % relative humidity at 20 ◦ C compared with that in water at 20 ◦ C. not only does the ﬁber return to its original length. Thus. 50 ◦ C for 1 h. This section of the curve (B – C) is known as the yield region. 150 – 200 N/mm2 in its initial state and a wet ultimate tensile strength of only 70 – 80 % of this value. In the dry state. where there is no excess of ionic groups. by ca. Whereas the tensile strength of wool decreases with increasing moisture content. The third region of the stress – strain curve is known as the post-yield region (C – D). As with all textile ﬁbers. 2 %. i. Stress – Strain Behavior. whereas liquid water is repelled by the hydrophobic outer surface of the cuticle. In this section of the curve. and post-yield regions are in the approximate ratio 100 : 1 : 10. The three characteristic regions of the stress – strain curve are very distinct in water at 20 ◦ C. 1 h. yield.9). After decrimping (not shown in Fig. there is complete reversibility of mechanical properties if the time in the stretched state does not exceed ca. This so-called initial region (A – B) is often incorrectly referred to as the “Hookean region”. c) Torsional modulus.10 Wool of the peptide chains. Above this.e. longitudinal and radial swelling are different (Fig. for example. dry undamaged wool has an ultimate tensile strength of ca. it is 35 – 55 %.e. The stress – strain curve can be divided into three regions which are affected to different extents by increasing humidity. the number of stabilizing salt bridges decreases. and the transitions at points B and C are sharp. 2 % and a radial swelling of 16 %. The slopes in the initial. thereby increasing the swelling . 10) . the tension in the ﬁber increases very rapidly and almost linearly up to a strain of 1 – 2 %. Figure 10. This apparently contradictory behavior. d) Extensional modulus An increase in the amount of absorbed moisture from 0 % to 33 % leads to a longitudinal swelling of ca.. and the wool carries excess negative or positive charges which cause electrostatic repulsion . The degree of ﬁber swelling is least at the isoionic point (pH 4. gives the same stress – strain curve as in the ﬁrst cycle. The extent of swelling depends on the pH and composition of the swelling medium. whereby wool shows considerable swelling anisotropy. Effect of moisture absorption on swelling and moduli  a) Length swelling. 30 %.
For dry wool. a straight line is obtained. Tensile stress – strain diagrams In addition to this simple tensile test. especially under the varying conditions of moisture content and temperature that can exist during the manufacture and wearing of woolen fabrics. 1 w1 w2 = + Tg Tg1 Tg2 11 The mass fraction of each component is represented by w. the indices 1 and 2 denoting dry wool and pure water respectively. Figure 11. Here the ﬁbers are stressed several times between constant elongation limits or constant tension limits. the elastic behavior of ﬁbers over the whole range of elongation up to the point of rupture can be determined. this gave T g1 = 447 K (174 ◦ C). Figure 12 shows the glasstransition temperature of wool as a function of water content in the ﬁber. and for water T g2 = 125 K (−148 ◦ C) . Glass-transition temperature of wool as a function of mass fraction of water in the ﬁber  The temperature dependence of the physical properties of wool – water systems has been investigated by many authors using a variety of . The test enables the permanent elongation and the elastic elongation to be determined. and also for an understanding of the aging and tempering processes of these fabrics. The glass-transition temperatures of the pure components can be calculated from the slope and the intersection of this line with the axis. A simple equation due to Fox  represents the relationship between the glasstransition temperature of wool and its water content: Figure 12. By replacing w1 by (1-w2 ). conﬁrming the validity of the Fox equation . The time-dependent recovery of wool ﬁbers after a ﬁxed torsional deformation as a function of temperature and water content has been measured. Knowledge of the glass transition temperature T g of wool  as a function of water content is of central importance for understanding its viscoelastic ﬁber properties. tensile elasticity testing can provide further information about the behavior of the ﬁber. In this way. Glass-Transition Temperature. the Fox equation becomes 1 1 1 = w2 − Tg Tg2 Tg1 + 1 Tg1 If the reciprocal of the glass-transition temperature of the wool – water system is plotted against the mass fraction of water.Wool This high degree of reversibility is not exhibited by any other ﬁber.
Chemical Reactivity [5. The liquors from acid-degraded wool contain ammonium salts. Heating with water at 130 – 140 ◦ C leads to the disappearance of the α-keratin X-ray diffraction pattern with chemical decomposition. 27. threonine. Second step: self-degradation of cystine residues by reduction of disulﬁde bonds with hydrogen sulﬁde. Degradation by Alkali. in analogy with the behavior of other glassy polymers. and the peptide bonds formed by serine. heating with water can lead to degradation of wool. 31] Dry Heat. Carbonizing by heating wool impregnated with sulfuric acid produces an N → O peptidyl shift in the serine and threonine units of the peptide chain. e. water in wool eliminates aging and tempering effects because the thermal history of the wool is erased when T g is exceeded. produce tolerable changes in the ﬁbers. Third step: Self-cross-linking by reaction of cysteine and lysine residues with dehydroalanine residues.2. pH of the liquor. liberating hydrogen sulﬁde which then attacks the cystine in the wool and accelerates the decomposition autocatalytically . In alkaline solution. Depending on the temperature.104]. 118]..g. cysteine. Sensitive sites in the wool proteins include the side chains of asparagine and glutamine. First step: self-degradation of cysteine residues by heat-induced β-elimination. 3. Formation of lanthionine and lysinoalanine cross-links. The reaction is reversible if the acid is removed after the process. The hydrolysis of peptide bonds leads to weight losses and the liberation of end groups in the wool proteins. Mineral acids can degrade wool proteins to an extent that depends on pH. the alkali binds to .g. free amino acids. Wool is sensitive to alkali.9). also further cross-links are formed in wool during heat exposure. temperature. but if the wool is stored in moist air in the O-peptidyl form. from which ammonia is released. Dry wool free of chemicals is stable for hours at 150 ◦ C. Acid Degradation. Beside cross-links based on sulfur. Short heating periods. and peptides (“wool gelatins”) [103.12 Wool methods. and the presence of salts and surfactants. signiﬁcantly below room temperature. 13. The cysteine in the wool proteins is decomposed ﬁrst. Formation of S-thiocysteine and cysteine residues. but chemical degradation occurs even below 100 ◦ C. Formation of dehydroalanine residues and hydrogen sulﬁde. the peptide chain is slowly and irreversibly hydrolyzed: B = amino groups of histidine or lysine residues and main-chain end groups. aspartic and glutamic acids. duration of reaction. Thus.. and tryptophan. and duration of heating. This is the cysteine – cystine self-degradation and self-cross-linking mechanism (thiol – disulﬁde degradation reaction). 185 ◦ C for 30 s. Wool in water has a T g of −5 ◦ C. Wool is most stable near the isoionic point (pH 4. linking via formation of dityrosine [117. e. Moist Heat.
Degradation reactions are also revealed by yellowing of the wool. A 0. and its solubility in a standard solution of alkali increases.5 M solution of sodium mercaptoacetate dissolves wool above pH 10 in a few hours by reducing the cystine bonds responsible for insolubility: WoCH2 SSCH2 Wo + 2 HSCH2 COONa → 2 WoCH2 SH + (SCH2 COONa)2 where Wo = peptide chains of the wool proteins.. The decomposition reactions depend on the type of alkali. chlorine removal. Nonionic surfactants have no effect on alkali damage to wool . The alkali binds to the wool so ﬁrmly that it cannot be completely removed by washing with water alone. In the reaction with sulﬁte or hydrogensulﬁte. discharge printing. and cause racemization of the amino acid residues: Cysteine → dehydroalanine + hydrogen sulﬁde Cystine → dehydroalanine + thiocysteine Dehydroalanine + cysteine → lanthionine Dehydroalanine + lysine → lysinoalanine Dehydroalanine + ammonia → β-aminoalanine Glutamine → glutamic acid + ammonia Asparagine → aspartic acid + ammonia Isoleucine → alloisoleucine. the reversible binding is accompanied by ﬁber damage. or oxidizing agents becomes sensitized to alkali. production of permanent creases by ironing. Alkalis hydrolyze the primary carbonamide bonds of asparagine and glutamine. Cationic surfactants increase the decomposition of cysteine and cystine and formation of lanthionine catalyzed by alkali. 13 Reducing Agents. the most important degradation reactions being the decomposition of cysteine and cystine. The sulﬁtolysis of wool is an important chemical reaction. 1 mol Bunte salt (S-sulfonate anion) and 1 mol cysteine are produced per mole of cystine: WoCH2 SSCH2 Wo + SO2− 3 WoCH2 SSO− 3 WoCH2 S− + WoCH2 SSCH2 Wo + HSO− 3 WoCH2 SSO− 3 WoCH2 SH + Maximum cleavage occurs in the pH range 3 – 6. stripping of dyes. Reducing agents such as sodium mercaptoacetate and mercaptoethanol reduce disulﬁde groups to thiol groups. The disulﬁde bonds in wool can also be reduced by aqueous solutions of sodium sulﬁde. This reaction is of industrial importance in the production of lime wool. On rinsing. cleave peptide bonds in the main chains. The solubility of wool in alkali under standard conditions is used as an indicator of chemical changes in the ﬁber. in permanent setting. e. the Bunte salt and cysteine groups recombine to give wool cystine. Oxidative sulﬁtolysis converts disulﬁde into two S-sulfonate anions: 2 WoCH2 SSO− + 2 HO− 3 WoCH2 SSCH2 Wo + 2 SO2− + [O] + H2 O → 3 In the reaction of wool with reducing agents. Even at low hydroxide concentrations.g. the temperature and duration of the reaction. cleavage of the stabilizing disulﬁde bonds leads . and chemical setting. Wool containing alkali residues undergoes decomposition on heating in a stream of dry air. Reaction of the thiol groups with iodoacetic acid produces S-carboxymethylkeratins: WoCH2 SH + ICH2 COONa → WoCH2 SCH2 COONa + HI Some of the wool proteins become soluble on degradation. This is the basis of the cold permanent waving process. Reversible reduction of cystine bridges without dissolving the ﬁber can be achieved with thiols if the reaction conditions are sufﬁciently mild. the pH. The alkali salts of the wool proteins must ﬁrst be decomposed by reaction with stronger acids. Wool that has been damaged by acids.Wool the wool proteins with swelling and simultaneous degradation. obtained by dehairing the skins of slaughtered sheep. reducing agents. Reducing agents are used in bleaching. and added salts and auxiliaries.
In undamaged wool. and the removal of skin-scale proteins from washed wool. but the wet strength does. Sheep Rearing and Breeding  Sheep growing is best suited to drier regions of the world. precipitation. Steppe and savannah pastures are suitable. Oxidizing agents attack the disulﬁde bonds. Such damage can be detected microscopically by the speciﬁc color reaction with lactophenol cotton blue and by splitting of the ﬁbers into multicellular ﬁbrillation products. the crossbreds became very Photodegradation [106–113]. These crossbreds have become established in South America as well as New Zealand. and mercaptans. Cysteine. Depending on the climatic and economic conditions. Macroﬁbrils remain intact. Progressive formation of nonspeciﬁc protein cross-links (e. to an increase in solubility. while maximum photoyellowing occurs with UV-B radiation (290 – 320 nm). and this can lead to damage to wool . Wool shows only limited fastness to light. e. The reaction proceeds via various cystine oxides (sulfoxides and sulfones) and leads ﬁnally to cleavage of the disulﬁde bond with formation of cysteic acid. and air temperature are important for the growth of sheep and their wool. and reaction time. Resources and Raw Materials 4. especially at weathered ﬁber ends.g. Argentina. The use of enzymes for pretreatment and ﬁnishing is described in Sections 5. the enzymatic degradability increases.1. Of industrial importance are oxidation reactions with hydrogen peroxide (for bleaching). peroxysulfuric acid.3 and 5. Visible blue light (380 – 475 nm) is responsible for photobleaching. In the chloramide reaction. Enzymatic Degradation. The dry stength does not always decrease. Enzymes are of industrial importance in wool processing. tryptophan. Photodamage results in the formation of a variety of oxidation states of cystine residues. but tropical regions are not. and proline residues are other targets for photodamage reactions. Under unfavorable conditions. At the same time. methionine. Sheep acclimatize well. After prolonged irradiation or irradiation with UV light the wool ﬁber yellows. and tyrosine are also attacked. These (microbial) degradation reactions are caused by bacteria or fungal proteases. Phenylalanine. which is important for the process of permanent setting by deformation followed by oxidation.g. tryptophan. temperature. mainly the endocuticle and cortical cell nucleus residues are degraded hydrolytically by proteases. and Uruguay). where the waste products from arable farming are used as feed. in the dissolution of skin residues from wool felts by selective degradation. dityrosine) has also been observed. With the introduction of frozen meat technology in 1882. The crossing of English mutton rams and merino yews produces the Corriedale sheep of New Zealand.. and with potassium manganate(VII). Enzymatic dehairing of the small hides from sheep and goats is an established process. peptide bonds are chlorinated: −CONH− + Cl2 → −CONCl− + HCl 4. and their bodies can adapt to extreme conditions and moderate food supplies. histidine. merino rams have been crossed with Lincoln yews. cortex cells. and peroxyacetic acid to give antifelting effects. tyrosine..14 Wool products at all stages of manufacture. Damaged wool is attacked more strongly. Plasticity increases.4. and macroﬁbrils. pH. chlorine. Sheep have also been bred in countries with intensive agriculture. sheep-farming countries specialize in wool production (Australia and South Africa) or the production of wool and meat (New Zealand. The extent of oxidation depends on the oxidizing agent and its concentration. wet wool is attacked by bacteria or fungi. On exposure to daylight wool is bleached after a short time. and are good producers of meat and wool. Climatic factors such as altitude. A linear relation exists between alkali solubility and cystine content of oxidatively and reductively bleached wool. In Australia. Scission of the main protein chain occurs with formation of keto-acyl end groups.
South American wool. However.g. South African wool (also known as Cape wool) including Karakul and indigenous wool. The New Zealand Minibowl process and the Australian Siro Scour process have been installed in some industrial plants.g. This problem has been solved satisfactorily by the sievedrum scouring process. mean ﬁber diameter usually > 30 µm.g. Argentinian (e. the residual fat content. Iran. Several other processes have been developed to improve wool scouring. In wool scouring. the major wool scouring is performed today by emulsion processes.. mean ﬁber diameter usually ≤ 25 µm. Raw Wool Scouring (See also → Textile Auxiliaries. ash content of the wool.2-trichloroethylene as solvent [147.1... it is labeled as pure wool. Chilean (e. crossbred wool from crossbred sheep. In accordance with textile labeling regulations. Scottish. and Chubut wool).g. and other Asian countries (China. However. etc. vigorous motion gives better washing. It is obtained by treatment with a mixture of lime and sulﬁdes. Places of Origin and Types of Raw Wool Places of Origin. 6 – 20 L of wastewater is produced per kilogram wool. Production Processes 5. see Chap. differs in having considerably shorter ﬁbers and lower quality and purity. The pure wool content of raw wool is variable. e. scouring with water or aqueous alcohol is also necessary to remove the wool suint. English. 5. the following being typical average values for Australian raw wool: Pure wool Wool grease Wool suint Soil and vegetable matter Moisture 55 % 10 % 4% 6 – 20 % 12 % 4. The product is known as sweated. and perchloroethylene. from North Africa. but can lead to a higher level of felting and hence to ﬁber shortening during later stages of the manufacturing process. To evaluate the scouring result. India.. wool recovered from skins is traded under the name slipes. Uruguayan (e. Bahia Blanca. after the French town of that name.) Wool obtained by sheep shearing contains varying amounts of impurities which must be removed in the scouring process. by ﬂoccula- . Types of Sheep. Peru. 8). or Mazamet wool. pulled. obtained by disintegrating used woollen textiles. 4. the method of determining this has been standardized (IWTO-19-76). In addition.g. Methods of Obtaining Wool  By far the largest proportion of wool is obtained by shearing live sheep.2. comeback wool from sheep obtained by crossbreeding crossbreds with merino sheep. but are not yet established in Western Europe.). Mongolia. e.. 15 5. mean ﬁber diameter usually > 25 µm. In New Zealand. Chap. Irish. depending on the process and raw wool.g. Solvent scouring systems are the de Smet plant using hexane and isopropyl alcohol as solvents . Montevideo wool) and other South American wools from Brazil. of minor importance.3. and soil impurities. biological methods are used to recover wool from the skins of slaughtered animals. 148]. and pH of the aqueous extract are determined (IWTO Methods. Buenos Aires. Punta Arenas wool). etc. European wool. Australian and New Zealand wool. e. These processes meanwhile all use suction drum bowls in combination with rake systems. and French. Solvent-based processes are. skin-ﬂake protein. e. and the Wooltech system using 1. Wool grease is highly soluble in organic solvents such as benzene.1.. acetone.2. The meat is mainly exported to the United Kingdom. exotic wools.g. In scouring machines. German. hexane.. ca. whiteness. Merino wool from merino sheep or sheep of the merino type. Reclaimed wool.Wool important. Consequently.. and even if most of the wool grease is removed. As wool is bought and sold on the basis of its pure wool content. therefore. there have been many attempts to use these solvents in wool scouring. coarse wool from coarse wool sheep.
which have linear densities of 14 – 24 g/m. → Felts. cannot usually be carried out immediately. Rotor spinning frames are now mainly used for short ﬁbers and blends of short ﬁbers. synthetic ﬁbers. and is then spun on a ring spinning machine. and detergents. These can then be removed from the ﬁber bundle because of their brittleness. Chap. is 1. This is followed by combing. is utilized in the production of felt from loose wool (carded web) or woven materials (→ Felts. The property of the wool ﬁber of migrating in various directions within the ﬁber bundle on mechanical treatment and in the presence of water and auxiliaries. The combed slivers (“tops”) from the ﬁnal stretching process. expressed as pure scoured wool. which removes most of the nonﬁbrous impurities.g. However. and this is then spun to produce worsted yarn. which sometimes also contain unacceptable amounts of vegetable matter. The back washing process once carried out before ﬁnal stretching is not now usually used. the use of enzymes to remove vegetable matter is being investigated [150. the dyeing method used must be as mild as possible. the slubbing is directly produced by splitting up the carded web. which is due to the frictional difference. The pollutants still present in the wastewater can be 80 – 90 % degraded in multistage chemical and biological plants. The mechanical processes of carding scoured raw wool and of combing prior to spinning worsted yarn remove most of the vegetable matter. the scoured wool is ﬁrst disentangled by carding. and ﬁnal stretching.3. The top undergoes further combing passes to give uniformity and can be blended with other types of ﬁber. but woolcombing plants (which are normally integrated with wool-scouring plants for cost and quality reasons) are found both in the wool-producing countries (advantage of proximity to the raw material) and in the processing countries (advantage of proximity to the market). 5.4 × 106 t in 1998. Several developments to increase the production of the ring spinning process. The web from the carding machine is gathered to form the socalled sliver.16 Wool centrifuge spinning. are therefore carbonized. Chemical Processing: Pretreatment Carbonization (→ Textile Auxiliaries). etc.3. Noils and woolen fabrics. This has provided a satisfactory solution to the problem of wastewater puriﬁcation. Pressed Felts. the remaining wastewater is still highly contaminated. So far. e. water.g. Evaporation and incineration plants are able to destroy > 99 % of the pollutants and recover energy. of which ca. the conversion of noil to wool yarn.4. If carbonized material is not dyed while it is still wet and contains acid. Chap. pot spinning. which consist mainly of cellulose. 3. form dark to black carbonization products after impregnation with sulfuric acid and heating. the fabric must be protected from the effects of moisture and light. are an important commerical form of wool. are being tested in pilot plants. In recent research. Ring spinning frames are generally used for this. Wool-scouring plants are today mainly located in the wool-producing countries.. some of these impurities remain in the wool. Chap... Several slivers are combined on the ﬁrst drawing frame and stretched. Mechanical Processing Total annual wool production. This name is derived from the fact that the impurities.). 3.3. To produce worsted yarn. Although it is no longer worth recovering potassium carbonate from the scouring water. Also. 600 000 t is converted into worsted yarn and 400 000 t into woolen yarn and carpet yarn . restretching. etc. thereby improving uniformity. e. The “roving” is then produced by stretching on rubber rollers or on a “ﬂyer”. . recovery of the byproduct wool wax is economically viable (→ Waxes.). 2. Both worsted and woolen yarns are converted to fabrics by the standard methods also used for other types of ﬁber (weaving. tion with acid and polyelectrolytes. Fiber migration is also used to cause fulling of wool fabrics and carpet yarns. none of these processes is used commercially In the production of woolen yarn. woven and tufted carpet manufacture. and the storage time must be as short as possible. 2.). so that the next stages of processing. like 5. 2. Felting Process.. knitting. 151].
softening. A process widely operated in Germany that can also be used on the top is a combination of relatively mild chlorination followed by treatment with a polyamide – epichlorhydrin resin (e. The most promising developments so far are treatment with peroxysulfuric acid and manganate(VII). The development in plasma technology is far advanced and tests with a pilot plant are running. strongly acidic salt solution 3) Treatment with sulﬁte 4) Stabilization with formaldehyde The process removes the cuticle almost completely. a treated ﬁber will often look no different from an untreated ﬁber under the microscope . whereas the other processes can also be used on tops. involving replacement of the conventional chlorination by a treatment with a low-temperature plasma. and gives the wool a luster resembling that of much more expensive ﬁne animal hairs. and then bleached with hydrogen peroxide . Although they are present in very small numbers in high-quality wools (a few naturally colored ﬁbers in 10 g wool). Hercosett 125). an environmentally friendly procedure for antifelting treatment of wool was developed. or coating the scale layer. comprises the following steps: 1) Pretreatment with heavy metal ions (can be omitted) 2) Treatment with hypochlorite in a saturated. 17 For ecological reasons. e. is a process of some importance. For carpet wools. 25 000 t. but a commercial process of this type for tops treatment is not yet available. which contain sodium . Precise process control gives very good stability to washing accompanied by low losses in weight and strength.g. Antifelting ﬁnishes work by partially removing. followed by application of a new developed polyurethane based polymer [153–156]. Recently. For white articles and sometimes for pastel shades. Treatment with adhesives can only be used on the ﬁnished fabric. Naturally pigmented dark wool ﬁbers require special treatment. It is now known that this is not so. A commercial process will be available in the next years. At one time it was believed that antifelting treatments had to remove the surface scales entirely. This is today the most important process for the production of machinewashable articles of pure wool. for garments ﬁnished in this color or for those dyed in dark shades. This practice can lead to increased wool yellowing during dyeing but is commercially attractive because the whiter wool attracts a higher price. work is directed towards the development of a new antifelting process that does not use chlorine or chlorine compounds . the total quantity of wool sliver treated worldwide in accordance with the IWS Super Wash speciﬁcations was ca..Wool Antifelting Treatments. They include chlorination and treatment with manganate(VII) or peroxysulfuric acid. preferably with hydrogen peroxide (see → Textile Auxiliaries). simply by adding hydrogen peroxide or reducing agents to the last bowl. and gives products complying with the speciﬁcations of the IWS Super Wash mark.. The highest level of whiteness can be obtained by a combination of bleaching with hydrogen peroxide and reductive bleaching with. whereas the Kroy process uses gaseous chlorine. Research is being carried out into antifelting effects produced by plasma technology  or topochemical enzyme processes . The so-called Vantean process. the natural cream color of wool is acceptable. carefully washed.g. The chlorination stage of the process is carried out with hypochlorite. In 1994.. The colored ﬁbers can be selectively bleached by a process in which the wool is pretreated with an iron salt. This must be carried such that only the scale layer is attacked and not the interior of the ﬁber. This affects the scales such that the difference between the “roughness” of the ﬁber surface in the tip-to-root and root-to-tip directions is reduced or even eliminated. e. the wool must be bleached. an oxidative process developed in Japan.g. they have a detrimental effect on the appearance of garments dyed in pale shades. bleaching during raw wool scouring. or by preventing movement of the ﬁbers relative to each other by spot welding. For many purposes. Bleaching of wool is not as important as the bleaching of natural cellulose ﬁbers. Most of the antifelting treatments developed for wool modify the surface of the ﬁber by chemical attack. Blankit products.
scouring liquors. 30 %). Reactive dyes represent an alternative method of achieving the high wetfastness of chrome dyes whilst eliminating the problem of heavy metal contamination of dyehouse. The process combines a stretching and either permanently or temporarily set in stretched conﬁguration (α → β transformation) so that a new wool ﬁber with different chemical and physical characteristics is produced . As a result of this. Dyeing is the most important wet ﬁnishing process for wool. a decrease in breaking strength of only 2 – 5 % occurs. Most of the reduction in ﬁber strength is due to setting of bends or curvatures of the packed ﬁbers by the hot water treatment. A new technology for reduction of the ﬁber diameter of wool ﬁbers has been developed by Woolmark Company and CSIRO. Wool . 1 : 1 metal-complex dyes (ca. Chrome dyes continue to fulﬁll a high proportion of wool dyeing capacity. yarn. particularly as a cost effective. not only for sports and leisurewear but for formal wear also. This has been minimized by the use of modiﬁed chrome dyeing techniques [122–124]. a 20 % stretch requires the application of reducing agents. The tenacity of wool is often reduced in stock-dyeing processes. Dyeing and Finishing [37. residual chrome creates a problem in dyehouse wastewater.e.. 45. Color discrepancies can usually be leveled by mixing slivers without additional dyeing. and histidine side chains. acid dyes (ca. i. particularly for wool and wool rich trousers (Wool plus Lycra). 50] Dyeing and Printing.18 Wool can be dyed in most stages of its manufacture. The most important dye classes for wool dyeing are afterchrome dyes (ca. 159]. 40. Another variant. H2 S. New Developments. i. high-wetfastness system for slubbings and loose wool. Due to the allergic and toxicological potential of chromium the usage of afterchrome dyes for wool dyeing is strongly decreasing. due to the α → β transformation OPTIM ﬁne has a more silk-like character than untreated wool . process and wool ﬁbers have the trade name OPTIM [158. slubbings. 25 – 30 %). Furthermore. care has to be taken in this bleaching process as ﬁber damage can occur. 25 – 30 %). reactive dyes further enhance wool quality by chemical reaction with thiol groups. from super- dithionite and sometimes also an optical brightener. Dyeing of wool blends is described in [45. → Textile Printing. Such set ﬁber bends are nonuniformly strained by tensions and thus resist smaller loads than ﬁbers set in the straight state . 5. and reactive dyes (ca. or piece. Solubility in alkali is a sensitive indicator of bleaching damage to wool (see page 13). 7 %). Some natural stretch can be produced in wool ﬁbers by subtle yarn technology. and dyed textiles . however. as ﬂock. However. Bleached and. both. Chap. Chap. The disadvantage of elastomeric ﬁbers in the fabric is that these ﬁbers are not dyeable to the fastness standards of the main ﬁbers in the cloth. Research studies have been performed to dye wool from nonaqueous media.1.5. and by acting as antisetting agents [125–128]. In the last few years there has been a growing demand for elastic fabrics and easy care properties. 7.. Chromium residues (especially Cr(VI)) in the dyed textiles can cause allergies and toxic skin reactions in sensitive individuals. The dyeing and printing of wool are treated in detail in → Textile Dyeing. 5. it is possible that although the alkali solubility (30 %) may be twice its normal value (12 – 17 %).e. of woolen yarn consisting of blends with other types of ﬁber or of large batches of uniform shades. This permanent elasticity of yarns and fabrics is achieved through supercontraction of the wool ﬁber. The dyeing of sliver is useful for the production of large batches of completely uniform color. In addition to the minimum wool damage exerted due to their optimum application pH in the isoionic region. 9]. Chap. 10 %) . to an even greater extent.. optically brightened wool undergoes more yellowing than unbleached wool on exposure to light. The dyeing of ﬂock is of importance in the production of melange shades. many ﬁbers are broken in the card. However. OPTIM ﬁne (permanently stretched ﬁber) reduces the diameter of wool by 3 – 4 µm.). OPTIM max (temporarily stretched ﬁber) is a ﬁber which is able to shrink by 20 to 25 % so that a higher bulkiness and softness is achieved. Sulﬁte-based textile auxiliaries were developed that provide worsted wool fabrics with a natural stretch . 1 : 2 metalcomplex dyes (ca.
The decisive role of cysteine thiol groups as initiators of the reactions that lead to permanent set is common to both theories.6.). the result being a signiﬁcant improvement in the natural ﬂame resistance of wool that is fast to washing and dry-cleaning. to provide the required thickness. The complexes with carboxylic acids are exhausted on the wool ﬁber . Wool can be dyed from supercritical carbon dioxide with hydrophobic dyes. 7. so that treatment with these products is recommended mainly for carpets and for storage protection. Wool is less ﬂammable than cellulose and synthetic ﬁbers (see → Textile Auxiliaries. 163]. preventing the catalysis of cysteine degradation reactions. Permanent set in wool requires the rupture of disulﬁde bonds in addition to the hydrogen bonds in the ﬁber. According to de Boos . are added to the dyebath and are taken up by the wool with the dye.e. Conventional wool-speciﬁc protection agents based on Sulcofuron are Mitin FF h. Its high ignition temperature. Wool treated with Mitin FF has very good fastness towards moisture and light. i. and is imparted whenever wool is distorted at temperatures above the glass-transition temperature (Fig. setting is an essential feature of the ﬁnishing of wool fabrics. and low ﬂame temperature are particularly advantageous and are connected with the chemical and morphological structure of the wool ﬁber.5. handle and visual properties to fabrics. Mothprooﬁng agents are usually applied during the exhaustion dyeing process. Permethrin-based insect-resist (IR) products account for ca. See → Insect Control. Chap.. Cohesive set in wool ﬁbers is thought to involve rearrangement of the hydrogen bonds in the ﬁber. This set conﬁguration of the fabric is stable as long as the ﬁbers remain below their T g . Others [131–135] consider the “transition temperature” for the onset of thiol – disulﬁde exchange reaction as the temperature required for chemical cysteine degradation and H2 S formation (see page 13). Chap. which has high nitrogen (16 %) and moisture (10 – 14 %) contents. 163]. It is used to stabilize fabrics prior to scouring and dyeing. 132] believe that thiol – disulﬁde exchange reactions at temperatures in excess of 60 ◦ C are required to impart permanent set. (80 % AS. Permethrin-treated wool has poor fastness to moisture and light. but also amino groups of the wool proteins. 7. high limiting oxygen index. Thus. 14. based on the volume of treated wool. low heat of combustion. Setting. Other possible methods include application during scouring. and Mitin FF liquid (Ciba Specialty Chemicals). all industrially proven methods of minimizing dyeing damage due to permanent set are based on the same principle.. to provide some durability to the ﬁnal ﬁnish. 90 % of the European market. For these reasons. blockage or oxidation of the cysteine thiol groups during dyeing [136. improved fastness properties are achieved by application of reactive disperse dyes [162. Shrink-Resistant Finishes. 19 Protection from Moths and Beetles [138– 141].c. 12) of the ﬁber and cooled while distorted..Wool critical carbon dioxide [162. The effectiveness of reactive dyes or other reactive chemicals is due to the fact that they block not only the cysteine thiol groups. Chap. Negatively charged titanium and zirconium complexes with α-hydroxycarboxylic acids and ﬂuorides can be exhausted on the positively charged wool ﬁber in acid conditions. and is therefore suitable for articles from which high standards of colorfastness are demanded.4. Ciba Specialty Chemicals). i.). which decreases the rate of H2 S formation. setting is an integral part of good ﬁnishing and fabric quality. Flameprooﬁng.5. Most authors [131. and occasionally to minimize dimensional changes in subsequent tailoring and wear.e. Fabrics or garments can be treated with nonchlorination processes which utilize polymers alone (→ Textile Auxiliaries. 137].
1. Dyeing and ﬁnishing with minimum environmental impact is crucial to the manufacture of eco-textiles [171. probably because of better penetration of the ﬁber by the smaller titanium complexes. French Hydrophobization and Oleophobization Treatments.. An important quality criterion is mean ﬁber diameter (ﬁneness). fungi. 6. 6. 4. 173] Testing methods are described in → Fibers. Woolen materials are .. are faced with wastewater limitations due the pesticide residues in the clip . i. 6. whereas the ﬂuoride complexes can be effectively exhausted at lower temperatures. which increases with light exposure.. If necessary. Testing and Analysis. Environmental Protection Like the other organic natural ﬁbers. wool.4. however. 14. By strict compliance with dyeing instructions the chromium(VI) content in the efﬂuent can be kept within tolerable limits. titanium complexes cause yellowing of wool. 2. renewable textile raw material. including bleached and dyed wool. Chap. 52]. 2. can be improved by the application of sulfonated UV absorbers. Modern efﬂuent treatment removes pollutants by ecologically tolerable processes. Tests of Form and Mass. wool is an environmentally friendly. 7. and spinnability of the raw wool. Chap. For interior woolen textiles photobleaching is the main problem because window glass ﬁlters short-wave UV light which induces photoyellowing... Chap. Testing and Analysis. and sheep farmers. 172]. Photobleaching is especially marked when woolen textiles are also thermally stressed (e. merchants. However.2) . visible light (especially blue light. in automobiles). Titanium complexes are more effective than the zirconium ones. Wool wastes are biodegraded by bacteria. However. which causes a marked photobleaching. as used by spinners. 3. carpet beetles) and can be used as long-acting nitrogen fertilizers .4 Ecological Aspects of Fabric Pretreatment . 36’s). light with a wavelength of 400 – 450 nm). Price is determined mainly by ﬁneness. held in 1990 and 1995 [42. which inﬂuences the softness of hand and is of paramount importance in spinning. Quality of wool or tops implies a statement of the type. like other ﬁbers. Lightfastness Treatment. 1. → Fibers. → Textile Auxiliaries. The lightfastness of wool. and the application of insect resist (IR) agents . AOX in the shrink-resist processes. Wool production and wool industry. cotton and silk. Legal and environmental aspects of the textile ﬁnishing industry are described in → Textile Dyeing. A new approach was developed by WRONZ-Institut to prevent photobleaching by application of a sulfonated aromatic compound (Lanalbin APB) .and oil-repellent by treating it with silicones or ﬂuorinated hydrocarbons. Wool ﬁneness is speciﬁed by the mean ﬁber diameter in micrometers. chromium in the dyeing process [168. → Textile Auxiliaries.e. Tensile Properties. can be made water. 4. at the boil. hydroxybenzophenones (Uvinuls) or hydroxybenzotriazoles (Cibafast W) from the dyebath [143–145].g. The effect of light on wool is ﬁrst to bleach it (photobleaching) and then to cause yellowing (photoyellowing). the highly polluted wool scouring efﬂuent (see Section 5. origin. A detailed and authoritative account of the environmental aspects of wool production and wool processing is afforded by the published proceedings of the two quinquennial wool textile research conferences.g. passes window glass. The ﬂuoride complexes can also be applied by a pad – batch – rinse – dry technique. 53.. e.20 Wool reusable. Chap. Zirconium complexes do not affect the shade of wool and are fast to light .4. In the past. and insects (moths. Chap. 3. The most important systems are the British (numbers ranging from 100’s to ca.4 Environmental Aspects. 169]. Quality Speciﬁcations [48. there were various systems of quality speciﬁcation.
3 3. Mean ﬁber µm ﬁneness. etc. peroxide bleaching..e. 176]. or chlorination. Table 4 compares the British system with mean ﬁber diameter and ﬁneness. It is only possible to collect typical values for undamaged wools . ash.5 µm mean ﬁber diameter). up to EE]. cysteic acid in hydrolysates of wool and S-carboxymethyl proteins in mercaptolytic digests. are mechanical properties such as ultimate tensile strength. In the FAST System (Fabric Assurance by Simple Testing). those with on average ca. Decreases by up to 15 % of the maximum ultimate tensile strength are acceptable for ﬁnishing processes. Recently British mills have agreed that the existing micron deﬁnitions should be extended for superﬁne wools to 100’s – 200’s (i.1 11 12 14 21 8. These enable statements to be made about the stiffness. The most important criteria for the assessment of changes to wool caused by industrial processing. 17. 6. and mean ﬁber ﬁneness  British quality number Mean ﬁber diameter.e. Chap.7 4. and surface condition of the fabric.. British quality numbers.) are applied in wool research for estimation of lanthionine. is a better predictor of (ﬁne) physical yarn properties than mean ﬁber diameter alone . and C). Onedimensional electrophoresis allows up to 50 distinct wool proteins to be separated (Fig. especially wet ﬁnishing. but these can decrease on dyeing. 14 fabric properties are determined using three compact instruments.4 6. I – VI. B. dtex 90’s 80’s 74’s 64’s 60/64’s 60’s 58’s 56’s 50’s 48’s 46’s ≤17 17 – 18 18 – 19 21 22 23 25 28 33 34 37 ≤3 3 – 3. because of increased demand for ﬁne fabrics for traditional tailoring. 17 fabric properties relevant to the hand are determined with four measuring devices. In the Kawabata System. There are two systems for obtaining an objective measurement of hand. and alkali or urea – bisulﬁte solubility.). lysinoalanine. as well as yarn evenness and tensile properties. such as carbonization. i. spinning oils. can deﬁnite tolerances be given which must not be exceeded after a correctly performed process in order to ensure a defect-free product. The methods include the determination of foreign substances (wool grease. The dry and wet strength and elongation of yarn bundles are determined (IWTO method 32-1982). The use of a combination of methods enables the causes of impairment of mechanical properties to be elucidated with a high degree of certainty. For ﬁne yarns. and German [letters in the range AAAA (4 A) to A. wool-ﬁberdiameter distribution affects spinning performance. Efﬁcient separation methods for amino acids and proteins by chromatography and electrophoresis (see → Amino Acids. histidinoalanine. It is not possible to quote mandatory values of mechanical and chemical data for a given wool. The dry values for undamaged wool are in the range 10 – 12 cN/tex. etc.Wool (numbers in the ranges 150 – 100. When these are plotted on a multiaxial graph (the socalled ﬁngerprint). conclusions can be drawn about the processing properties of the fabric during manufacture . Only in the case of certain standard treatments. elasticity. amino acids .6 g) of wool (spinning limit). These analytical data vary on wet ﬁnishing of the wool in various directions and to various extents. Comparison of electrophoretic patterns of digests of dyed and ﬁnished wool textiles allow speciﬁc statements on the involvement The British grade number gives the number of hanks of 560 yards (512 m) that can be spun from 1 lb (453. mean ﬁber diameter.3 – 3. Most chemical testing methods for wool have been standardized by the Technology and Standards Committee of the International Wool Textile Organization (IWTO) . 48] Chemical methods of testing wool to assess damage at the various stages of manufacture are well established.5 5.0 5. Testing and Analysis [46.4 8. Table 4. . a parameter derived from yarn-evenness theory. and objective dimensionless hand indices can be calculated from these if required [175. Effective ﬁneness. 13).. Reliable ﬁgures are obtained if samples are taken by standardized methods at the various stages of a treatment process and analyzed. 35 ﬁbers in the cross section.0 to 13.
such as keratins versus keratinassociated proteins [181–184]. SO2 and NOx . Wool has been used for thermal insulation in houses in Europe for many decades and is being increasingly used for both homes and commercial buildings [190– 194]. Storage and Transportation  Wool must be stored and transported under normal atmospheric conditions. Keratin hydrolysates can be isolated from wool by acid.2. Trademarks The Woolmark Company was founded in 1937 as the International Wool Secretariat. The packaging material must allow some exchange of air to avoid damp and high-humidity condi- 11. e. especially felts. Together with its three well known trademarks. to the use of wool for high-performance sportswear clothing. The moisture absorbing and desorbing properties of wool can also contribute to passive heating and cooling effects and.4. of morphological components and chemical constituents. and the increased use is being driven by consumer demand for natural products in their homes. namely aldehydes. or for production of new textile materials . to some extent in automobile upholstery (most often blended with polyester) and in aircraft seatings [186–188]. has led to new applications in the private and commercial sector [195–197]. l-Cystine can be isolated from hydrolysates of hair or wool (see → Amino Acids. furthermore.. domestic furnishings. led. 10. and bedding). 3. Chap. The wool pack material should not pose problems in dyeing and ﬁnishing. Uses  Merino and crossbred wools are mainly used in clothing. Schematic electrophoretic protein-separation pattern of merino wool  9. scoured wool. or any other form should be kept dry to avoid bacterial and fungal attack. and as a means to soak up oil spills. These hydrolysates are used as ﬁber protective agents during wool dyeing .22 Wool tions in the bale. for cosmetics. The natural property of wool to effectively absorb speciﬁc classes of widespread indoor air pollutants. Figure 13. Today it is known as The Woolmark Company and is the world’s leading wool textile marketing organization. it is synonymous with research and .). Wool is naturally ﬁre resistant. the wool ﬁber can now be found in applications as diverse as thermal insulation. Bales of raw wool. Of minor importance are special wool products. for ﬁlter materials. weed mats. basic. tops.g. or enzymatic hydrolysis in combination with a reductive (or sometimes oxidative) treatment. home textiles (carpets. geotextile products. According to .
and pay the relevant usage fee . It is used by companies licensed by the Woolmark Company in more than 65 countries extending across a wide range of products – clothes. New Zealand produces mainly scoured coarse wools that are exported for use in the production of home textiles. Argentina. Admixtures of wool recovered by mild methods from the skins of slaughtered sheep are permitted. promotion. and thus being the most important supplier for the wool combers of the industrialized countries. The Woolmark was launched in 1964. Each pro- 23 gram is also identiﬁed by a specially designed sub-brand logo. as grazing land for sheep cannot be increased indeﬁnitely. and is now a registered trademark in over 140 countries. vicuna. and therefore is not available on the international market. and export wool either in scoured loose form or as tops (scoured and combed wool). angora. provided that here also it is obtained by a mild process. and political economy (economic decline in Eastern Europe). Uruguay. The suppliers of the raw material to the international wool textile industry are those countries that produce and export amounts of wool in excess of their own requirements. In addition to its three main brands. http://www. and yak. Textiles with this mark must consist of 100 % virgin wool. The Wool Blend symbol was introduced in mid1999 to extend the opportunities offered by The Woolmark Company’s blends program. which highlight selected product attributes.com). and became valid in the European Community in 1972. Wool production has grown only slowly over recent decades.com. including Cool Wool. 14). Sportwool . home furnishings. A decline has even occurred since 1990/91 for reasons of climate. 60 % of its wool production as raw wool. The Woolmark symbol was designed by an Italian. exporting ca. cashmere and cashgora goats.wool. Table 5 gives world wool production ﬁgures for the major producing countries during the period of the shearing seasons from 1995/96 to 1999/2000.woolmarkbrand. the Woolmark Company has introduced a series of programs. although at widely varying levels of intensity. This also applies to important wool-producing countries such as China and the countries of the former Soviet Union. These programs are backed by speciﬁcations and clear product descriptions to ensure a clear and globally consistent message. 14). Machine Washable Wool. innovation. Wool plus Lycra . Figure 15 shows percentage shares of world production. Maintaining consistent high quality is a key feature of the Woolmark program. llama. price (lucrative alternatives for farmers). Before a manufacturer can use the Woolmark or any trademarks of the Woolmark Company he needs to apply for a license. angora-mohair. the Wool Blend symbol is used to identify products that contain at least 30 % (but less than 50 %) new wool (Fig. rabbit. and it is important that all licensees have good in-plant quality assurance procedures in place. the logos are featured on a range of promotion tickets. In 1970. guanaco. and South Africa. These principally comprise Australia. 12. carpets. Wool Cotton. Franceso Sarroglia to identify quality products made from pure new wool (Fig. the designation “pure new wool” (Reine Schurwolle) was included in the textile labeling law (TKG) of the Federal Republic of Germany. Pure Merino Wool. The same high performance standards apply to all three trademarks. Argentina. camel. Merino Extraﬁne. Sheep rearing and hence wool production exist in almost all parts of the world. New Zealand. The Woolmark Blend symbol (originally called Woolblendmark) was introduced in 1971 to identify quality products made from wool rich blends (products comprising at least 50 % new wool). and quality assurance in pure new wool and wool blend products (cf. home-produced wool is processed and consumed internally. washing machines and detergents. especially carpets. Australia is the world’s largest producer and exporter of garment wools (merinos). Equal status is given to ﬁne animal hair from the alpaca. Further details are available from The Woolmark Company at http://www. Table 5 shows actual weights of raw wool or lime wool. Economic Aspects Wool Production. Uruguay. and South Africa have also built their own wool scouring and combing plants. He also needs to be able to meet the quality standards that are required under the Woolmark program.Wool development. Total Easy Care Wool. Table 6 lists . In most countries.
Other quality and price parameters are the content of vegetable matter and pigmented ﬁbers.85 A$/kg (September 1994). The reasons for the relatively low prices for ﬁne wools may be an increased supply of “hunger-ﬁne” wools after a drought. crimpiness.5 µm.6 – 32.1 A$/kg (March 1999) and 8. The market indicator during this period ﬂuctuated between 5. wool export ﬁgures.24 Wool Figure 14. color. albeit ﬁne wools. and the lack of interest in such low-quality. Figure 16 shows the development of the average auction price of Australian raw wool.. the weighted average of the qualities) in the sales seasons 1994/95 to 1999/2000.80 A$/kg (March 1996) and 7. A high price is evidence of a strong. the price differences between two given qualities can vary greatly over time with supply and demand.5 µm and ﬁner. The difference in price between this and the market indicator varied between 0.e. the so-called market indicator (i. prices have been determined by the market forces of supply and demand. which also shows the price curve for 19 µm wools. Carpet wool covers 32. elasticity. Woolmarks for pure new wool and new wool with other ﬁber Table 5. The price differences between the various wool qualities are considerable. for the ﬁve most important exporting countries for the seasons 1994/95 to 1998/99. Figure 15. World wool production (1997/98) Wool Prices. and many others.6 µm and coarser. This is illustrated in Figure 16. tensile strength. 1995/96 1996/97 1997/1998 1998/99 1999/2000 Raw wool weight Australia 697 725 700 684 671 New Zealand 269 275 266 252 256 Former Soviet Union 238 196 164 140 135 China 277 298 255 277 290 Argentina 81 78 68 70 63 Uruguay 79 85 78 63 58 South Africa 65 59 54 58 53 Others 826 804 811 812 814 World 2532 2520 2396 2356 2340 Merinoa 1077 1061 992 976 957 Crossbredb 626 620 582 557 551 Carpet woolsc 836 839 822 823 832 b c a Merino wool covers 24. and South Africa. . Crossbred wool covers 24. Since the collapse in early 1991 of the minimum price system which imposed a lower limit on wool prices for 17 years in Australia. World wool production by the major producing countries (in 106 kg) (source IWTO). However.6 A$/kg (March 1995). but also the uniformity of distribution are of great importance. New Zealand. Not only the mean ﬁneness and length. The most important factors determining quality and therefore price are the ﬁneness and staple length of the ﬁber.
and Spain account for 29 %.7 280. Consumption of shorn wool by the wool textile industry spinning mills in 1998 (in 106 kg scoured wool) 106 kg % Italy Germany UK Spain Other Western Europe Central and Eastern Europe Total Europe Africa (incl.1 70. Germany. with 28 % of the total world industrial demand for wool.5 42. New Zealand World 263. Wool products that have reached the end of their useful life may be recycled via the woolen . In second place is the Far East. woolen clothing protects against heat.2 46.1 61. Wool exports (raw wool.4 110. is remarkable. scoured wool. United Kingdom.8 86.. The comparatively minor importance of the wool textile industry in the United States.8 66. cold. 3 % of the world’s consumption of virgin wool.0 38.2 138. and sliver) by the ﬁve major exporting countries (in 106 kg scoured wool) 1994/95 Australia New Zealand South Africa Argentina Uruguay Total 591 228 26 46 15 906 1995/96 534 196 29 32 14 805 1996/97 608 200 20 34 17 879 1997/98 556 192 24 25 8 805 1998/99 475 171 25 24 8 703 25 Figure 16. The four EU countries Italy. For German wool imports.e.1 23.6 1372 42 18 11 6 22 8 36 3 10 16 3 3 6 53 47 10 73 16 9 2 28 3 100 Wool Consumption. Table 7. water. see Table 8. On the contrary. b) 19 µm indicator fashion-induced demand accompanied by a restricted supply.3 34. This underscores the world importance of the European woolen industry. South Africa) Middle East Total +Africa and Middle East North America Central and South America Total Americas India Other Indian Subcontinent Total Indian Subcontinent China and Hong Kong Japan South Korea Taiwan Total Far East Australia.2 39.Wool Table 6. 13. and sun as well as mechanical impact . Table 7 lists world wool consumption.0 221.6 85.9 142. Europe has the highest consumption of wool (36 % of the world total). Toxicology and Occupational Health The wool ﬁber itself poses no health problems. Price development of Australian raw wool a) Average auction price (market indicator).6 495. the rest of Western Europe 14 %.0 75.9 8.2 46.7 385. and Central and Eastern Europe 8 % of total world consumption for spinning mills. i.
Properly dyed wool articles do not contain such azo dyes that could set free carcinogenic aromatic amines such as benzidine. etc. is today discouraged and nonharmful alternatives are recommended. Glafey. Wool incompatibility is caused neither by toxic components of wool. No health risks are involved in wearing properly ﬁnished and dyed wool clothing. Wool prickle is due to the coarser wool ﬁbers digging into human skin with enough force to excite pain receptors. it is a purely mechanical irritation of the skin.7. Members of the Ecological and Toxicological Association of Dyes and Organic Pigment Manufacturers (ETAD) ceased the manufacture of benzidine-based dyes in the early 1970s due to the inability to ensure their safe handling in dyeing plants. All the existing ectoparasiticide products are evaluated for potential hazard to shearers and farm workers for incorporation into the protocol of the Australian Occupational Health and Safety Commission. Ulrich: “Technologie u der Wolle – Chemische Technologie und mechanische Hilfsmittel f¨ r die Veredlung von u Wolle. Users of lanolin products are at lower risk. Peter Dufﬁeld. 213. Chap. ﬂame retardants or dyes have impact on the ecotoxicology of wool materials.26 Wool Table 8. incl. 215]. vol. References 1. Berlin 1938.. As measure of the “safe exposure level” the acceptable daily intake is compared with the potential exposure calculated from the amount of active ingredient present and the amount of wool grease covering the shearer . VIII. G. nor is it a wool allergy. tops and noils (clean basis) Raw wool (clean basis) greasy (actual) scoured (actual) Animal hair Tops. but can be caused by other natural and synthetic ﬁbers if sufﬁcient coarse ﬁber ends per unit area of skin are present. even if it comes in direct contact with the skin. For the ecotoxicological potential of textile dyes. However. However. part 3 B. Wool is biodegradable. Hans-Georg Hebecker. German imports of wool and tops (in t) (Source: Comtext. Acknowledgement. etc. Also operational procedures are now strictly laid down to control and minimize any risks to farm workers. because of the particular economic and technical merits of these dyes. see → Textile Dyeing. This mechanical skin irritation is not speciﬁc to wool.. Provided the dyed goods have good fastness characteristics. D. Kr¨ ger. Azo Dyes [209–211]. they have continued to be manufactured in many countries. there is not a concern about consumer risk. pretreatments or presence of contaminants such as pesticides or textile ﬁnishing agents like mothproofing agents. There is a potential human health hazard to shearers and farm workers handling the treated sheep and wools. Prickle [204–208]. Eurostat) Import Category Wool. etc. especially if the commercially available “reduced pesticide” grades of lanolin are used where there is human skin contact. . problems are caused by exposure of workers to noise and to respirable and alveolar dust [212. and Kevin Russel for helpful suggestions. Noils and waste 1999 (full year) 63 302 33 800 33 969 12 434 1 732 23 944 5 588 Jan – April 1999 19 874 10 705 8 873 4 671 819 9 136 1 938 Jan – April 2000 18 826 10 924 9 417 4 520 1 059 8 378 1 748 process and can be used for production of wool materials of minor quality or technical products. Occupational Health.” in Technologie der Textilfasern. the use of toxic agents for sheep dips. Fabrics made from wool with no more than 5 % of ﬁbers larger than 30 µm will not be perceived as prickly by most people. In the processing of wool. 14. Springer Verlag. However. H. 14.The authors thank ¨ Hartwig Hocker (Director of the Deutsches Wollforschungsinstitut an der RWTH Aachen) for checking the manuscript and Klaus Wolf.
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