Innovative Technologies for Sustainable Textile Coloration, Patterning, and Surface Effects

The environmental impact of textile dyeing and finishing is of paramount concern in the textile industry. Enzyme and laser processing technologies present attractive alternatives to conventional textile coloration and surface patterning methods. Both technologies have the capability to reduce the impact of manufacturing on the environment by reducing the consumption of chemicals, water and energy, and the subsequent generation of waste. Two emerging textile processing technologies, laser processing and enzyme biotechnology, were investigated as a means of applying surface design and color to materials with a focus on improving the efficiency and sustainability of existing textile design and finishing methods. Through industrial stakeholder engagement and interdisciplinary research involving textile design, fiber and dye chemistry, biotechnology and optical engineering, this design-led project brought together design practice and science with a commercial focus. Each technology was used to modify targeted material properties, finding and exploiting opportunities for the design and finishing of textiles. The work resulted in a catalog of new coloration and design techniques for both technologies making it possible to achieve: selective surface pattern by differential dyeing, combined three-dimensional and color finishing and novel coloration of textile materials. The chapter provides a literature review mapping the use of enzyme biotechnology and laser processing technology within textile design and manufacturing to date, identifying current and future opportunities to reduce environmental impacts through their application. The methodological approach, which was interdisciplinary and design-led, will be introduced and the specific design and scientific methods applied will be detailed. Each of the techniques developed will be discussed and examples of the design effects achieved will be presented. And, an indication of the reductions in chemical effluent, efficiencies in resource use, and design-flexibility in comparison with traditional textile coloration and surface patterning techniques will be given

MOESM3 of Exploring xylose metabolism in Spathaspora species: XYL1.2 from Spathaspora passalidarum as the key for efficient anaerobic xylose fermentation in metabolic engineered Saccharomyces cerevisiae

Additional file 3. List and sequence of primers used in this study

MOESM1 of Exploring xylose metabolism in Spathaspora species: XYL1.2 from Spathaspora passalidarum as the key for efficient anaerobic xylose fermentation in metabolic engineered Saccharomyces cerevisiae

Additional file 1. Time course of substrate consumption (xylose at an initial concentration of 40–50 g L−1) and product formation by Spathaspora species under moderate and severe oxygen-limited batch fermentations

MOESM2 of Exploring xylose metabolism in Spathaspora species: XYL1.2 from Spathaspora passalidarum as the key for efficient anaerobic xylose fermentation in metabolic engineered Saccharomyces cerevisiae

Additional file 2. ClustalW multiple alignment of XYL1p, XYL1.1p, and XYL1.2p amino acid sequences from Spathaspora species and Scheffersomyces stipitis (XYL1p N272D)

2LT8 : Eurocin solution structure

Experimental Technique/Method:SOLUTION NMR Resolution: Classification:ANTIMICROBIAL PROTEIN Release Date:2012-10-31 Deposition Date:2012-05-15 Revision Date:2012-11-07 Molecular Weight:4348.84 Macromolecule Type:Protein Residue Count:42 Atom Site Count:302 DOI:10.2210/pdb2lt8/pdb Abstract: Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications because they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, which have been found in different species. Here we describe a new fungal defensin, eurocin. Eurocin acts against a range of Gram-positive human pathogens but not against Gram-negative bacteria. Eurocin consists of 42 amino acids, forming a cysteine-stabilized α/β-fold. The thermal denaturation data point shows the disulfide bridges being responsible for the stability of the fold. Eurocin does not form pores in cell membranes at physiologically relevant concentrations; it does, however, lead to limited leakage of a fluorophore from small unilamellar vesicles. Eurocin interacts with detergent micelles, and it inhibits the synthesis of cell walls by binding equimolarly to the cell wall precursor lipid II

Exploring xylose metabolism in Spathaspora species: XYL1.2 from Spathaspora passalidarum as the key for efficient anaerobic xylose fermentation in metabolic engineered Saccharomyces cerevisiae

Abstract Background The production of ethanol and other fuels and chemicals from lignocellulosic materials is dependent of efficient xylose conversion. Xylose fermentation capacity in yeasts is usually linked to xylose reductase (XR) accepting NADH as cofactor. The XR from Scheffersomyces stipitis, which is able to use NADH as cofactor but still prefers NADPH, has been used to generate recombinant xylose-fermenting Saccharomyces cerevisiae. Novel xylose-fermenting yeasts species, as those from the Spathaspora clade, have been described and are potential sources of novel genes to improve xylose fermentation in S. cerevisiae. Results Xylose fermentation by six strains from different Spathaspora species isolated in Brazil, plus the Sp. passalidarum type strain (CBS 10155T), was characterized under two oxygen-limited conditions. The best xylose-fermenting strains belong to the Sp. passalidarum species, and their highest ethanol titers, yields, and productivities were correlated to higher XR activity with NADH than with NADPH. Among the different Spathaspora species, Sp. passalidarum appears to be the sole harboring two XYL1 genes: XYL1.1, similar to the XYL1 found in other Spathaspora and yeast species and XYL1.2, with relatively higher expression level. XYL1.1p and XYL1.2p from Sp. passalidarum were expressed in S. cerevisiae TMB 3044 and XYL1.1p was confirmed to be strictly NADPH-dependent, while XYL1.2p to use both NADPH and NADH, with higher activity with the later. Recombinant S. cerevisiae strains expressing XYL1.1p did not show anaerobic growth in xylose medium. Under anaerobic xylose fermentation, S. cerevisiae TMB 3504, which expresses XYL1.2p from Sp. passalidarum, revealed significant higher ethanol yield and productivity than S. cerevisiae TMB 3422, which harbors XYL1p N272D from Sc. stipitis in the same isogenic background (0.40 vs 0.34 g g CDW −1 and 0.33 vs 0.18 g g CDW −1 h−1, respectively). Conclusion This work explored a new clade of xylose-fermenting yeasts (Spathaspora species) towards the engineering of S. cerevisiae for improved xylose fermentation. The new S. cerevisiae TMB 3504 displays higher XR activity with NADH than with NADPH, with consequent improved ethanol yield and productivity and low xylitol production. This meaningful advance in anaerobic xylose fermentation by recombinant S. cerevisiae (using the XR/XDH pathway) paves the way for the development of novel industrial pentose-fermenting strains