Trends on the cellulose-based textiles: raw materials and technologies

There is an emerging environmental awareness and social concern regarding the environmental impact of the textile industry, highlighting the growing need for developing green and sustainable approaches throughout this industrys supply chain. Upstream, due to population growth and the rise in consumption of textile fibers, new sustainable raw materials and processes must be found. Cellulose presents unique structural features, being the most important and available renewable resource for textiles. The physical and chemical modification reactions yielding fibers are of high commercial importance today. Recently developed technologies allow the production of filaments with the strongest tensile performance without dissolution or any other harmful and complex chemical processes. Fibers without solvents are thus on the verge of commercialization. In this review, the technologies for the production of cellulose-based textiles, their surface modification and the recent trends on sustainable cellulose sources, such as bacterial nanocellulose, are discussed. The life cycle assessment of several cellulose fiber production methods is also discussed.This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE 2020 (POCI-01-0145-FEDER-006684) and BioTecNorte Operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020– Programa Operacional Regional do Norte. Support from The Navigator Company through the I&D n◦ 21874, “Inpactus– Produtos e Tecnologias Inovadores a partir do Eucalipto,” funded through the Fundo Europeu de Desenvolvimento Regional (FEDER) and the Programa Operacional Competitividade e Internacionalização (POCI) is acknowledged.info:eu-repo/semantics/publishedVersio

Proteins derived from the dairy losses and by-products as raw materials for non-food applications

The disposal of a high volume of waste-containing proteins is becoming increasingly challenging in a society that is aware of what is happening in the environment. The dairy industry generates several by-products that contain vast amounts of compounds, including proteins that are of industrial importance and for which new uses are being sought. This article provides a comprehensive review of the potential of the valorisation of proteins that can be recovered by chemical and/or physical processes from protein-containing milk by-products or milk surplus, particularly whey proteins or caseins. Whey proteins and casein characteristics, and applications in non-food industries, with special emphasis on the textile industry, packaging and biomedical, are reported in this review, in order to provide knowledge and raise awareness of the sustainability of these proteins to potentiate new opportunities in a circular economy context.info:eu-repo/semantics/publishedVersio

Odorant binding proteins : a biotechnological tool for odour control

The application of an odorant binding protein for odour control and fragrance delayed release from a textile surface was first explored in this work. Pig OBP-1 gene was cloned and expressed in Escherichia coli , and the purified protein was biochemically characterized. The IC50 values(concentrations of competitor that caused a decay of fluorescence to half-maximal intensity) were determined for four distinct fragrances, namely, citronellol, benzyl benzoate,citronellyl valerate and ethyl valerate. The results showed a strong binding of citronellyl valerate,citronellol and benzyl benzoate to the recombinant protein, while ethyl valerate displayed weaker binding. Cationized cotton substrates were coated with porcine odorant binding protein and tested for their capacity to retain citronellol and to mask the smell of cigarette smoke. The immobilized protein delayed the release of citronellol when compared to the untreated cotton. According to a blind evaluation of 30 assessors, the smell of cigarette smoke, trapped onto the fabrics’ surface, was successfully attenuated by porcine odorant binding protein (more than 60 % identified the weakest smell intensity after protein exposure compared to β-cyclodextrin-treated and untreated cotton fabrics). This work demonstrated that porcine odorant binding protein can be an efficient solution to prevent and/orremove unpleasant odours trapped on the large surface of textiles. Its intrinsic properties make odorant binding proteins excellent candidates for controlled release systems which constitute a new application for this class of proteins.This work was co-funded by the European Social Fund through the management authority POPH and FCT. The authors Carla Silva and Teresa Matama would like to acknowledge their post-doctoral fellowships: SFRH/BPD/46515/2008 and SFRH/BPD/47555/2008, respectively

Protein formulations for emulsions and solid-in-oil dispersions

Needs from medical and cosmetic areas have led to the design of novel nanosized emulsions and solid-in-oil dispersions of proteins. Here, we describe the production of those emulsions and dispersions using high-energy methodologies such as high-pressure homogenization or ultrasound. Recent work has resulted in new mechanistic insights related to the formation of protein emulsions and dispersions. The production method and composition of these formulations can determine major parameters such as size, stability, and functionality, and therefore their final application. Aqueous nanoemulsions of proteins can be used for drug delivery, while solid-in-oil dispersions are often used in transdermal applications.This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE 2020 (POCI-01-0145-FEDER-006684

Insights on the mechanism of formation of protein microspheres in a biphasic system

Microspheres of bovine serum albumin (BSA) and silk fibroin are produced by applying ultrasound in a biphasic system consisting of an aqueous protein solution and an organic solvent. The protein microspheres are dispersed in an aqueous media where the protein remains at the interface covering the organic solvent. This only occurs when high shear forces are applied that induce changes to force the protein to the interface. Fourier transform infrared results indicate a large increase in the content of the β-sheet during the formation of silk fibroin microspheres. Molecular dynamics simulations show a clear adaption on the 3D structure of BSA when stabilized at the interface, without major changes in secondary structure. Further studies demonstrate that high water content, oil solvents, and larger peptides with separated and clear hydrophobic and hydrophilic areas lead to more stable and smaller spheres. This is the first time that these results are presented. We also present herein the rationale to produce tailored protein microspheres with a controlled size, controlled charge, and increased stability.This work was supported by Lidwine Project-Multifunctional medical textiles for wound (e.g., Decubitus) prevention and improved wound healing NMP2-CT-2006-026741. H.F. thanks POPH/FSE for cofinancing and FCT for Fellowship SFRH/BPD/38939/2007. We acknowledge Silvia Cappellozza from "Sezione Specializzata per la Bachicoltura" for the supply of silk cocoons

Peptideprotein interactions within human hair keratins

We selected 1235 decapeptides from human hair proteins encoded by human genes of keratins and keratin associated proteins. The peptides were linked to glass arrays and screened for their affinity towards a solution of human hair extracted keratin fraction. Based on the physicochemical properties of the peptides, ten variables were studied: content of different types of amino acid side chains (cysteine, hydrophobic, polar, basic, acidic, aromatic rings, amide, alcohol side chains), isoelectric point, and net charge. We found differences statistically significant on the binding affinity of peptides based on their content of cysteine, hydrophobic and polar amino acids, mainly containing alcohols. These results point to the formation of hydrophobic interactions and disulfide bonds between small peptides and human hair keratins as the main driving forces for the interaction of possible cosmetic peptides, namely designed to strength human hair. As so, our results enlighten the nature of the interaction of keratin based materials with human hair, which are claimed to enhance hair fiber strength, and enable a more directed and sustained hair care peptide design.We thank the Portuguese Foundation for Science and Technology (FCT) for providing Célia F. Cruz the grant for PhDstudies (scholarship SFRH/BD/100927/2014). This work was alsosupported by FCT under the scope of the strategic funding of UID/BIO/04469/2013 unit, COMPETE 2020 (POCI-01-0145-FEDER-006684) and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fundunder the scope of Norte2020 - Programa Operacional Regional doNorte. This study was also supported by the Portuguese Foundationfor Science and Technology (FCT) under the scope of the Project RECI/BBB-EBI/0179/2012 (FCOMP-01-0124-FEDER-027462).info:eu-repo/semantics/publishedVersio

Safety Assessment of Polypyrrole Nanoparticles and Spray-Coated Textiles

Polypyrrole (PPy) nanoparticles (NPs) are used for the coating of materials, such as textiles, with biomedical applications, including wound care and tissue engineering, but they are also promising antibacterial agents. In this work, PPy NPs were used for the spray-coating of textiles with antimicrobial properties. The functional properties of the materials were verified, and their safety was evaluated. Two main exposure scenarios for humans were identified: inhalation of PPy NPs during spray (manufacturing) and direct skin contact with NPs-coated fabrics (use). Thus, the toxicity properties of PPy NPs and PPy-coated textiles were assessed by using in vitro models representative of the lung and the skin. The results from the materials’ characterization showed the stability of both the PPy NP suspension and the textile coating, even after washing cycles and extraction in artificial sweat. Data from an in vitro model of the air–blood barrier showed the low toxicity of these NPs, with no alteration of cell viability and functionality observed. The skin toxicity of PPy NPs and the coated textiles was assessed on a reconstructed human epidermis model following OECD 431 and 439 guidelines. PPy NPs proved to be non-corrosive at the tested conditions, as well as non-irritant after extraction in artificial sweat at two different pH conditions. The obtained data suggest that PPy NPs are safe NMs in applications for textile coating

Insights on the Mechanism of Formation of Protein Microspheres in a Biphasic System

Microspheres of bovine serum albumin (BSA) and silk fibroin are produced by applying ultrasound in a biphasic system consisting of an aqueous protein solution and an organic solvent. The protein microspheres are dispersed in an aqueous media where the protein remains at the interface covering the organic solvent. This only occurs when high shear forces are applied that induce changes to force the protein to the interface. Fourier transform infrared results indicate a large increase in the content of the β-sheet during the formation of silk fibroin microspheres. Molecular dynamics simulations show a clear adaption on the 3D structure of BSA when stabilized at the interface, without major changes in secondary structure. Further studies demonstrate that high water content, oil solvents, and larger peptides with separated and clear hydrophobic and hydrophilic areas lead to more stable and smaller spheres. This is the first time that these results are presented. We also present herein the rationale to produce tailored protein microspheres with a controlled size, controlled charge, and increased stability