The influence of selected factors on wool cortisol concentration in alpacas (Vicugna pacos).

Several internal and external factors can influence animals' hormonal activity. Cortisol level in hair and wool determines chronic stress, which is connected with the long-term HPA axis effect. Wool cortisol levels in alpacas have never been determined to this time. The study aimed to assess the influence of selected factors on wool cortisol concentration in alpacas. The study included 36 alpacas. Wool samples were collected during shearing in June 2021, cut with an electric clipper from the right shoulder and the rump. Wool samples were fragmented into proximal (winter-spring regrowth) and distal (summer-fall regrowth) segments. Alpacas' Heat Stress Index (HSI) for the summer of 2020 was 139.4, and 116 for the winter of 2021. The cortisol levels in the wool samples were determined with the General Cortisol ELISA Kit assay. The most significant differences in wool cortisol concentrations were caused by two factors: the wool segment (P < 0.001; η2 = 0.889) and the region on the body (P < 0.001; η2 = 0.876). Wool cortisol level was higher in the distal segment (referring to the summer-fall season) than in the proximal one (referring to the winter-spring season). It is suggested that alpacas can feel heat stress in summer (HSI = 139.4), which could influence higher cortisol levels in the distal segment. The wool cortisol level was higher in the rump samples than the shoulder ones. Therefore, it is essential in future studies that wool samples from all tested animals should be completed from the same body region. Differences among age and sex groups were also observed. Wool cortisol level was higher in older animals, as differences between age groups were observed in samples from the rump in the distal and proximal segments (distal, the rump younger*older: P < 0.001; η2 = 0.321; proximal, the rump older*younger: P = 0.007; η2 = 0.195). Males showed higher cortisol levels than females, as a difference between sexes was observed in samples from the rump in the proximal segment (P = 0.001, η2 = 0.271). This study emphasizes that various factors may significantly influence wool cortisol levels, which can be helpful in alpacas' welfare estimation using this hormonal indicator as a noninvasive long-term stress assessment method.

Textile effluent treatment by reductive process using commercial steel wool followed by oxidative process.

Textile industries stand out as one of the main polluters of water resources, generating large amounts of liquid effluents with variable composition and intense coloration. The objective of this work is the integration of the reductive process using commercial steel wool, combined with oxidative processes, in the treatment of textile effluent. The effect of the variables of the reductive process were studied using a 32 factorial design. After 30 minutes, the reductive process allowed a reduction of 68% COD, 46% TOC, 62% true color and 72% of total phenols, but showed an increase in color apparent and turbidity, due to the iron species formed by the oxidation of steel wool during the process. With the combined process using sunlight, the reduction was 73% COD, 50% TOC, 97% phenols, 93% true color and 48% apparent color. With artificial light, the reduction was 94% COD, 63% TOC, 95% phenols, 98% true color and 65% apparent color. The evaluation of the acute toxicity against Daphnia magna indicated that after the proposed treatments, the effluent did not present toxicity or the toxicity was reduced. It is concluded that the combined process can be considered an efficient alternative for the treatment of textile effluent.

Wool keratin as a novel alternative protein: A comprehensive review of extraction, purification, nutrition, safety, and food applications.

The growing global population and lifestyle changes have increased the demand for specialized diets that require protein and other essential nutrients for humans. Recent technological advances have enabled the use of food bioresources treated as waste as additional sources of alternative proteins. Sheep wool is an inexpensive and readily available bioresource containing 95%-98% protein, making it an outstanding potential source of protein for food and biotechnological applications. The strong structure of wool and its indigestibility are the main hurdles to achieving its potential as an edible protein. Although various methods have been investigated for the hydrolysis of wool into keratin, only a few of these, such as sulfitolysis, oxidation, and enzymatic processes, have the potential to generate edible keratin. In vitro and in vivo cytotoxicity studies reported no cytotoxicity effects of extracted keratin, suggesting its potential for use as a high-value protein ingredient that supports normal body functions. Keratin has a high cysteine content that can support healthy epithelia, glutathione synthesis, antioxidant functions, and skeletal muscle functions. With the recent spike in new keratin extraction methods, extensive long-term investigations that examine prolonged exposure of keratin generated from these techniques in animal and human subjects are required to ascertain its safety. Food applications of wool could improve the ecological footprint of sheep farming and unlock the potential of a sustainable protein source that meets demands for ethical production of animal protein.

Wool fiber curvature is correlated with abundance of K38 and specific keratin-associated proteins.

Curvature in mammalian fibers, such as wool and human hair, is an important feature of the functional trait of coat structure-it affects mechanical resilience and thermo-insulation. However, to examine the relationship between fiber curvature, ultrastructure and protein composition fiber diameter variability has to be minimal. To achieve this we utilised the progeny of straight-wool domestic sheep mutant rams (crimp mutants) and wild-type ewes. Proteomic and structural results of the resulting mutant/wild-type twin pairs confirmed that straight crimp mutant wool had a normal cuticle and the same cortical protein and ultrastructural building blocks as wild-type (crimpy) fibers but differed in the layout of its cortical cells and in the relative proportions of keratin (K) and keratin-associated proteins (KAPs). In the case of the crimp mutants (straight fibers), the orthocortex was distributed in a fragmented, annular ring, with some orthocortical cells near the central medulla, a pattern similar to that of straight hairs from humans and other mammals. Crimp mutant fibers were noted for the reduced abundance of some proteins in the high glycine-tyrosine class normally associated with the orthocortex, specifically the KAP6, KAP7, and KAP8 families, while proteins from the KAP16 and KAP19 were found in increased abundance. In addition to this, the type I keratin, K38, which is also associated with the orthocortex, was also found at lower abundance in the mutant fibers. Conversely, proteins from the ultra-high sulfur class normally associated with the paracortex, specifically the KAP4 and KAP9 families, were found in higher abundance.

Preparation and applications of keratin biomaterials from natural keratin wastes.

Keratin is a kind of natural polymer that is abundant in feathers, wool, and hair. Being one of the natural biomolecules, keratin has excellent biological activity, biocompatibility, biodegradability, favorable material mechanical properties, and natural abundance, which exhibit significant biological and biomedical application potentials. At present, the strategies commonly used for preparing keratin from hair, feathers, wool, etc. include physical, chemical, and enzymatic methods. The present article mainly reviews the structure, classification, preparation methods, and the main biological applications of keratin, and these applications cover wound healing, hemostasis, targeted release of tissue engineering drugs, and so on. It is expected to lay the foundations for its future in-depth investigations and wide applications of keratin biomaterials. KEY POINTS: • There are several pathways to prepare biologically active keratin from wool, feathers, and human hair, etc • Promoting blood coagulation by keratin is related to the adhesion and activation of platelets and the aggregation of fibrin • The biological applications of keratin, including wound healing and tissue engineering, are summarized.

Facile fabrication of durable antibacterial and anti-felting wool fabrics with enhanced comfort via novel N-phenylmaleimide finishing.

In this study, we successfully synthesized N-phenylmaleimide (NPMI) and applied it to wool fabrics to obtain robust antimicrobial properties. First, tris(2-carboxyethyl) phosphine (TCEP) was utilized as a reducing agent to produce thiol-active groups on wool fibers. These thiol groups were then reacted with the C=C group of NPMI via thiol-ene click chemistry. The morphology and structure of the finished NPMI composite wool fabric were characterized using FT-IR spectroscopy, Raman spectroscopy and scanning electron microscopy (SEM). The composite wool fabrics exhibited durable antibacterial properties against both S. aureus and E. coli and the antimicrobial rates of both E. coli and S. aureus were around 99% after one standard washing cycle, with only a slight decrease of 95% after ten standard washing cycles, respectively. In addition, the composite wool fabric exhibited good anti-felting performance and maintained its original excellent breathability and moisture permeability. The present work provides a facile and sustainable strategy for constructing durable antimicrobial wool fabrics without losing their original properties.

Development of Environmentally Friendly Wool Shrink-Proof Finishing Technology Based on L-Cysteine/Protease Treatment Solution System.

The particular scale structure and mechanical properties of wool fiber make its associated fabrics prone to felting, seriously affecting the service life of wool products. Although the existing Chlorine-Hercosett treatment has a remarkable effect, it can lead to environmental pollution. Therefore, it is of great significance to develop an environmentally friendly and effective shrink-proof finishing technology. For this study, L-cysteine was mixed with protease to form a treatment solution system for shrink-proof finishing of wool fibers. The reduction performance of L-cysteine and its effect on wool were compared with those of other reagents, demonstrating that L-cysteine has an obvious reduction and destruction effect on the wool scale layer. Based on this, L-cysteine and protease 16L were mixed in a certain proportion to prepare an L-cysteine/protease treatment solution system (L/PTSS). The shrink-proof finishing of a wool top was carried out by the continuous multiple-padding method, and the processing parameters were optimized using the response surface method. The results indicated that when the concentrations of L-cysteine and protease 16L were 9 g/L and 1 g/L, respectively, the wool was padded five times at 50 °C, and each immersion time was 30 s, the felt ball density of the treated wool reduced from 135.86 kg/m3 to 48.65 kg/m3. The structure and properties of the treated wool were also characterized using SEM, TG, and tensile strength tests, which indicated that the fiber scale structure was stripped evenly. Meanwhile, the treated fibers still retained adequate thermal and mechanical properties, indicating suitable application value. XPS, FT-IR, Raman, UV absorbance, and other test results revealed the reaction mechanism of L/PTSS with the wool fibers. After L-cysteine rapidly reduced the disulfide bonds in wool, protease can hydrolyze peptide chains more effectively, causing the scale layer to gradually peel off. Compared with the chlorination method and other protease shrink-proof technologies, L/PTSS can achieve the finishing effect on wool rapidly and effectively, without causing excessive pollution to the environment. The conclusions of this study provide a foundation for the development and industrial application of biological enzyme shrink-proof finishing technology.

A detailed mapping of the readily accessible disulphide bonds in the cortex of wool fibres.

Trichocyte keratin intermediate filament proteins (keratins) and keratin associated proteins (KAPs) differ from their epithelial equivalents by having significantly more cysteine residues. Interactions between these cysteine residues within a mammalian fiber, and the putative regular organization of interactions are likely important for defining fiber mechanical properties, and thus biological functionality of hairs. Here we extend a previous study of cysteine accessibility under different levels of exposure to reducing compounds to detect a greater resolution of statistically non-random interactions between individual residues from keratins and KAPs. We found that most of the cysteines with this non-random accessibility in the KAPs were close to either the N- or C- terminal domains of these proteins. The most accessible non-random cysteines in keratins were present in the head or tail domains, indicating the likely function of cysteine residues in these regions is in readily forming intermolecular bonds with KAPs. Some of the less accessible non-random cysteines in keratins were discovered either close to or within the rod region in positions previously identified in human epithelial keratins as involved in crosslinking between the heterodimers of the tetramer. Our present study therefore provides a deeper understanding of the accessibility of disulfides in both keratins and KAPs and thus proves that there is some specificity to the disulfide bond interactions leading to these inter- and intra-molecular bonds stabilizing the fiber structure. Furthermore, these suggest potential sites of interaction between keratins and KAPs as well as keratin-keratin interactions in the trichocyte intermediate filament.

TiO2 modified orthocortical and paracortical cells having enhanced photocatalytic degradation and photoreduction properties.

In this study, cortical cells resultant from wool fibers were loaded with TiO2 nanoparticles in a hydrothermal process and were then engineered as organic-nonorganic hybrid composite photocatalysts for both photodegradation of organic dyes and photoreduction of heavy metal ions. The microstructure and photocatalytic properties of TiO2 modified cortical cells (i.e. both orthocortical and paracortical cells) were systematically characterized using a series of analytical techniques including FESEM, TEM, element analysis, Mott-Schottky curve, BET specific surface area, Zeta potentials, as well as XRD, FTIR, XPS, DRS, PL, UPS, EDS and ESR spectra. Their photocatalytic performance and trapping experiments of the TiO2 modified cortical cells were measured in the photodegradation of methylene blue (MB) dye and Congo Red (CR) dye as well as the photoreduction of Cr(VI) ions under visible light irradiation. It was found that anatase TiO2 nanoparticles were chemically grafted on the surface of the two cortical cells via O-Ti4+/O-Ti3+ bonds, and that TiO2 nanoparticles were formed inside the orthocortical cells in the hydrothermal process. The TiO2 modified orthocortical and paracortical cells possessed much higher photocatalytic efficiency than the commercially available TiO2 nanoparticle powder, Degussa P25, in the photodegradation of cationic MB dye and photoreduction of Cr(VI) ions, while their photocatalytic efficiency in the photodegradation of anionic CR dye is smaller because of their greater negative Zeta potentials and photogenerated holes as the main reactive radical species. In comparison with the TiO2 modified paracortical cells, the higher photocatalytic efficiency of the TiO2 modified orthocortical cells was demonstrated in the photodegradation of MB dye solution and this might be due to both the S-doped TiO2 nanoparticles infiltrated into the naturally hydrophilic orthocortical cells and the primary reactive radical species of photogenerated holes being trapped in the cells.

The Complexity of the Ovine and Caprine Keratin-Associated Protein Genes.

Sheep (Ovis aries) and goats (Capra hircus) have, for more than a millennia, been a source of fibres for human use, be it for use in clothing and furnishings, for insulation, for decorative and ceremonial purposes, or for combinations thereof. While use of these natural fibres has in some respects been superseded by the use of synthetic and plant-based fibres, increased accounting for the carbon and water footprint of these fibres is creating a re-emergence of interest in fibres derived from sheep and goats. The keratin-associated proteins (KAPs) are structural components of wool and hair fibres, where they form a matrix that cross-links with the keratin intermediate filaments (KIFs), the other main structural component of the fibres. Since the first report of a complete KAP protein sequence in the late 1960s, considerable effort has been made to identify the KAP proteins and their genes in mammals, and to ascertain how these genes and proteins control fibre growth and characteristics. This effort is ongoing, with more and more being understood about the structure and function of the genes. This review consolidates that knowledge and suggests future directions for research to further our understanding.

Sheep Wool Humidity under Electron Irradiation Affects Wool Sorptivity towards Co(II) Ions.

The effect of humidity on sheep wool during irradiation by an accelerated electron beam was examined. Each of the samples with 10%, 53%, and 97% relative humidity (RH) absorbed a dose of 0, 109, and 257 kGy, respectively. After being freely kept in common laboratory conditions, the samples were subjected to batch Co(II) sorption experiments monitored with VIS spectrometry for different lapses from electron beam exposure. Along with the sorption, FTIR spectral analysis of the wool samples was conducted for cysteic acid and cystine monoxide, and later, the examination was completed, with pH measuring 0.05 molar KCl extract from the wool samples. Besides a relationship to the absorbed dose and lapse, the sorptivity results showed considerable dependence on wool humidity under exposure. When humidity was deficient (10% RH), the sorptivity was lower due to limited transformation of cystine monoxide to cysteic acid. The wool pre-conditioned at 53% RH, which is the humidity close to common environmental conditions, demonstrated the best Co(II) sorptivity in any case. This finding enables the elimination of pre-exposure wool conditioning in practice. Under excessive humidity of 97% RH and enough high dose of 257 kGy, radiolysis of water occurred, deteriorating the sorptivity. Each wool humidity, dose, and lapse showed a particular scenario. The time and humidity variations in the sorptivity for the non-irradiated sample were a little surprising; despite the absence of electron irradiation, relevant results indicated a strong sensitivity to pre-condition humidity and lapse from the start of the monitoring.

Microextraction of Reseda luteola-Dyed Wool and Qualitative Analysis of Its Flavones by UHPLC-UV, NMR and MS.

Detailed knowledge on natural dyes is important for agronomy and quality control as well as the fastness, stability, and analysis of dyed textiles. Weld (Reseda luteola L.), which is a source of flavone-based yellow dye, is the focus of this study. One aim was to reduce the required amount of dyed textile to ≤50 µg for a successful chromatographic analysis. The second aim was to unambiguously confirm the identity of all weld flavones. By carrying out the extraction of 50 µg dyed wool with 25 µL of solvent and analysis by reversed-phase UHPLC at 345 nm, reproducible chromatographic fingerprints could be obtained with good signal to noise ratios. Ten baseline separated peaks with relative areas ≥1% were separated in 6 min. Through repeated polyamide column chromatography and prepHPLC, the compounds corresponding with the fingerprint peaks were purified from dried weld. Each was unequivocally identified, including the position and configuration of attached sugars, by means of 1D and 2D NMR and high-resolution MS. Apigenin-4'-O-glucoside and luteolin-4'-O-glucoside were additionally identified as two trace flavones co-eluting with other flavone glucosides, the former for the first time in weld. The microextraction might be extended to other used dye plants, thus reducing the required amount of precious historical textiles.

Vibrational Study on Structure and Bioactivity of Protein Fibers Grafted with Phosphorylated Methacrylates.

In the last decades, silk fibroin and wool keratin have been considered functional materials for biomedical applications. In this study, fabrics containing silk fibers from Bombyx mori and Tussah silk fibers from Antheraea pernyi, as well as wool keratin fabrics, were grafted with phosmer CL and phosmer M (commercial names, i.e., methacrylate monomers containing phosphate groups in the molecular side chain) with different weight gains. Both phosmers were recently proposed as flame retarding agents, and their chemical composition suggested a possible application in bone tissue engineering. IR and Raman spectroscopy were used to disclose the possible structural changes induced by grafting and identify the most reactive amino acids towards the phosmers. The same techniques were used to investigate the nucleation of a calcium phosphate phase on the surface of the samples (i.e., bioactivity) after ageing in simulated body fluid (SBF). The phosmers were found to polymerize onto the biopolymers efficiently, and tyrosine and serine underwent phosphorylation (monitored through the strengthening of the Raman band at 1600 cm-1 and the weakening of the Raman band at 1400 cm-1, respectively). In grafted wool keratin, cysteic acid and other oxidation products of disulphide bridges were detected together with sulphated residues. Only slight conformational changes were observed upon grafting, generally towards an enrichment in ordered domains, suggesting that the amorphous regions were more prone to react (and, sometimes, degrade). All samples were shown to be bioactive, with a weight gain of up to 8%. The most bioactive samples contained the highest phosmers amounts, i.e., the highest amounts of phosphate nucleating sites. The sulphate/sulphonate groups present in grafted wool samples appeared to increase bioactivity, as shown by the five-fold increase of the IR phosphate band at 1040 cm-1.

Identification and characterization of circRNAs in the skin during wool follicle development in Aohan fine wool sheep.

BACKGROUND: Aohan fine wool sheep (AFWS) is a historically bred fine wool sheep, cultivated in China. The wool has excellent quality and good textile performance. Investigating the molecular mechanisms that regulate wool growth is important to improve wool quality and yield. Circular RNAs (circRNAs) are widely expressed non-coding RNAs that can act as competitive endogenous RNAs (ceRNAs) to bind to miRNAs. Although circRNAs have been studied in many fields, research on their activity in sheep wool follicles is limited. To understand the regulation of circRNAs in the growth of fine wool in sheep, we used RNA-Seq to identify circRNAs in sheep shoulder skin samples at three developmental stages: embryonic day 90 (E90d), embryonic day 120 (E120d), and at birth (Birth). RESULTS: We identified 8753 circRNAs and found that 918 were differentially-expressed. We then analyzed the classification and characteristic of the circRNAs in sheep shoulder skin. Using Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG), we identified the source genes of circRNAs, which were mainly enriched in cellular component organization, regulation of primary metabolic processes, tight junctions, and the cGMP-PKG and AMPK signaling pathways. In addition, we predicted interactions between 17 circRNAs and eight miRNAs, using miRanda software. Based on the significant pathways, we speculate that circ_0005720, circ_0001754, circ_0008036, circ_0004032, circ_0005174, circ_0005519, and circ_0007826 might play an important role in regulating wool follicle growth in AFWS. Seven circRNAs were randomly selected to validate the RNA-Seq results, using qRT-PCR. CONCLUSION: Our results provide more information about circRNAs regulation of wool follicle development in AFWS, and establish a solid foundation for future research.

Development of an eco-friendly antibacterial textile: lysozyme immobilization on wool fabric.

Lysozyme, a type of natural enzyme, has been widely used for bacteriostatic functionalization of various materials due to its efficient and selective antibacterial properties. Herein, we report the preparation and characterization of an eco-friendly antibacterial textile based on the immobilization of lysozyme from chicken egg white onto wool fibers. Tris(hydroxymethyl)phosphine (THP) was employed as the cross-linker for the immobilization of lysozyme on the surface of wool fiber. The mechanism of THP cross-linking was investigated via phosphorus test, energy-dispersive spectroscopy (EDX) and Fourier transform infrared spectroscopy (FT-IR). The surface staining, optimization of immobilization parameters, morphology, antibacterial properties, and durability of wool fibers with immobilized lysozyme were also assessed. The results show that hydroxymethyl groups of THP reacted with amino groups of wool fiber and lysozyme through Mannich reaction, which successfully immobilized lysozyme on the wool fiber. The wool fibers incorporated with lysozyme had better antibacterial properties and durability compared with the untreated wool fabric. This facile immobilization approach of lysozyme provides an effective strategy for environmentally benign modification and functionalization of keratin and keratin-containing materials.

Structure and Properties of Oxidized Chitosan Grafted Cashmere Fiber by Amide Covalent Modification.

In this study, oxidized chitosan grafted cashmere fibers (OCGCFs) were obtained by crosslinking the oxidized chitosan onto cashmere fibers by amide covalent modification. A novel method was developed for the selective oxidation of the C6 primary hydroxyls into carboxyl groups for chitosan. The effect of oxidization reaction parameters of HNO3/H3PO4-NaNO2 mediated oxidation system on the oxidation degree, structure, and properties of chitosan were investigated. The chemical structure of the oxidized chitosan was characterized by solid-state cross-polarization magic angle spinning carbon-13 Nuclear Magnetic Resonance (CP/MAS 13C-NMR), Fourier transform infrared spectroscopy (FT-IR), and its morphology was investigated by scanning electron microscopy (SEM). Subsequently, the effect of the oxidized chitosan grafting on OCGCF was examined, and the physical properties, moisture regain, and antibacterial activity of OCGCFs were also evaluated. The results showed that oxidation of chitosan mostly occurred at the C6 primary hydroxyl groups. Moreover, an oxidized chitosan with 43.5-56.8% carboxyl content was realized by ranging the oxidation time from 30 to 180 min. The resulting OCGCF had a C-N amido bond, formed as a result of the reaction between the primary amines in the cashmere fibers and the carboxyl groups in the oxidized chitosan through the amide reaction. The OCGCF exhibited good moisture regain and remarkable bacteriostasis against both Staphylococcus aureus and Escherichia coli bacteria with its durability.

Helical twist direction in the macrofibrils of keratin fibres is left handed.

Macrofibrils, the main structural features within the cortical cells of mammalian hair shafts, are long composite bundles of keratin intermediate filaments (KIFs) embedded in a matrix of keratin-associated proteins. The KIFs can be helically arranged around the macrofibril central axis, making a cylinder within which KIF helical angle relative to macrofibril axis increases approximately linearly from macrofibril centre to edge. Mesophase-based self-assembly has been implicated in the early formation of macrofibrils, which first appear as liquid-crystal tactoids in the bulb of hair follicles. Formation appears to be driven initially by interactions between pre-keratinized KIFs. Differences in the nature of these KIF-KIF interactions could result in all macrofibrils being internally twisted in a single handedness, or a 50:50 mixture of handedness within each cortical cell. We data-mined 41 electron tomograms containing three-dimensional macrofibril data from previously published studies of hair and wool. In all 644 macrofibrils examined we found that within each tomogram all macrofibrils had the same handedness. We concluded that earlier reports of left- and right-handed macrofibrils were due to artefacts of imaging or data processing. A handedness marker was used to confirm (using re-imaged sections from earlier studies) that, in both human and sheep, all macrofibrils are left-handed around the macrofibril axis. We conclude that this state is universal within mammalian hair. This also supports the conclusion that the origin of macrofibril twist is the expression of chiral twisting forces between adjacent KIFs, rather than mesophase splay and bending forces relaxing to twisting forces acting within a confined space.

Volatiles from Merino fleece evoke antennal and behavioural responses in the Australian sheep blow fly Lucilia cuprina.

To identify flystrike-related volatile compounds in wool from Merino sheep, the attractiveness of wool to Lucilia cuprina Wiedmann (Diptera: Calliphoridae) was examined. First, a selection of wool samples guided by previous knowledge of sheep lines, predicted to be more susceptible or more resistant to flystrike, was tested. The attractiveness of the 10 samples selected was not associated with field susceptibility: two samples from the more resistant line were identified as most attractive and two samples from the more susceptible line were identified as least attractive, based on the behavioural assays with gravid flies. Comparison of the headspace volatiles of these samples, using solid phase microextraction and gas chromatography-mass spectrometry-electroantennographic detection, revealed octanal and nonanal to be present in the attractive wool samples that elicited responses from the fly antenna. Furthermore, the two compounds were not present in wool that was least attractive to L. cuprina. In laboratory bioassays, octanal and nonanal evoked antennal and behavioural responses in gravid L. cuprina, thus confirming their potential role as semiochemicals responsible for attracting L. cuprina to Merino sheep.

Some Properties of Electron Beam-Irradiated Sheep Wool Linked to Cr(III) Sorption.

We examined the characteristics of an electron beam irradiated wool with an absorbed dose of (21-410) kGy in comparison with natural wool with respect to the determination of the isoelectric point (IEP), zero charge point (ZCP), mechanism of Cr(III) sorption from higher concentrated solutions, and the modelling of the wool-Cr(III) interaction. The data of ZPC and IEP differed between natural and irradiated samples. Increasing the dose shifted the pH of ZPC from 6.85 for natural wool to 6.20 for the highest dosed wool, while the natural wool IEP moved very little, from pH = 3.35 to 3.40 for all of the irradiated samples. The sorption experiments were performed in a pH bath set at 3.40, and the determination of the residual Cr(III) in the bath was performed by VIS spectrometry under optimized conditions. The resulting sorptivity showed a monotonically rising trend with increasing Cr(III) concentration in the bath. Lower doses, unlike higher doses, showed better sorptivity than the natural wool. FTIR data indicated the formation of complex chromite salts of carboxylates and cysteinates. Crosslinks via ligands coming from different keratin chains were predicted, preferably on the surface of the fibers, but to a degree that did not yet inhibit the diffusion of Cr(III)-cations into the fiber volume. We also present a concept of a complex octahedral structure.

Role of Post-Exposure Time in Co(II) Sorption of Higher Concentrations on Electron Irradiated Sheep Wool.

Sorption of Co(II) was investigated on natural as well as accelerated electron beam modified sheep wool involving low and high concentrations up to 200 mmol·dm-3. The sorption experiments confirmed the dependence of the sorption capacity not only on sorbate concentration and absorbed dose of energy, but also on post-exposure time. Post-exposure heating to accelerate transformation of the wool structure was of no effect on the sorption comparing with a simple storage for a period of 100 days. Under all tested conditions, the sorption maximum was measured for Co(II) concentration of 125 mmol·dm-3 and that was assigned to form a Co(II) complex with keratin. This assumption was tested on visible spectra of mixed solutions of Arginine and Co(II) to be a simplified model of Co(II) interaction with keratin. The sorption decrease is associated with generation of cross links between macro-chains through ligands of the Co-complex. The nodal points are a hindrance to diffusion of next ions into the fibers. Also, pH variations of aqueous extracts from the wool samples depending on absorbed dose and post-exposure time indicate complexity of the structural transformation being specific for each dose applied.