ABSTRACT
Although recovery of fibers from used textiles with retained material quality is desired, separation of individual components from polymer blends used in today's complex textile materials is currently not available at viable scale. Biotechnology could provide a solution to this pressing problem by enabling selective depolymerization of recyclable fibers of natural and synthetic origin, to isolate constituents or even recover monomers. We compiled experimental data for biocatalytic polymer degradation with a focus on synthetic polymers with hydrolysable links and calculated conversion rates to explore this path The analysis emphasizes that we urgently need major research efforts: beyond cellulose-based fibers, biotechnological-assisted depolymerization of plastics so far only works for polyethylene terephthalate, with degradation of a few other relevant synthetic polymer chains being reported. In contrast, by analyzing market data and emerging trends for synthetic fibers in the textile industry, in combination with numbers from used garment collection and sorting plants, it was shown that the use of difficult-to-recycle blended materials is rapidly growing. If the lack of recycling technology and production trend for fiber blends remains, a volume of more than 3400â Mt of waste will have been accumulated by 2030. This work highlights the urgent need to transform the textile industry from a biocatalytic perspective.
ABSTRACT
D-glucosaminic acid (2-amino-2-deoxy-D-gluconic acid), a component of bacterial lipopolysaccharides and a chiral synthon, is easily prepared on a multigram scale by air oxidation of D-glucosamine (2-amino-2-deoxy-D-glucose) catalysed by glucose oxidase.
Subject(s)
Glucosamine/analogs & derivatives , Glucosamine/biosynthesis , Glucosamine/metabolism , Aspergillus niger/enzymology , Catalase/metabolism , Glucosamine/chemistry , Glucose Oxidase/metabolism , Hydrogen-Ion Concentration , Molecular Structure , Oxidation-ReductionABSTRACT
Degradation of 2,6-dichlorophenol (2,6-DCP) was accomplished by oxidation catalyzed by Coprinus cinereus peroxidase. Immobilization of the enzyme in a polyacrylamide matrix enhanced DCP oxidation. Hydrogen peroxide, peroxidase's natural substrate, was produced enzymatically in situ to avoid peroxidase inactivation by its too high concentration. In the case of larger scale utilization, the method would also avoid direct handling of this hazardous reagent.
Subject(s)
Chlorophenols/chemistry , Coprinus/enzymology , Hydrogen Peroxide/chemical synthesis , Peroxidase/chemistry , Catalysis , Enzymes, Immobilized/chemistry , Humans , Oxidation-ReductionABSTRACT
In order to estimate the size of the cavity remaining around the heme of the 3A3-microperoxidase 8 (MP8) hemoabzyme, the formation of 3A3-MP8-Fe(II)-nitrosoalkane complexes upon oxidation of N-monosubstituted hydroxylamines was examined. This constituted a new reaction for hemoabzymes and is the first example of fully characterized Fe(II)-metabolite complexes of antibody-porphyrin. Also, via a comparison of the reactions with N-substituted hydroxylamines of various size and hydrophobicity, antibody 3A3 was confirmed to bring about a partial steric hindrance on the distal face of MP8. Subsequently, the influence of the antibody on the stereoselectivity of the S-oxidation of sulfides was examined. Our results showed that MP8 alone and the antibody-MP8 complex catalyze the oxidation of thioanisole by H(2)O(2) and tert-butyl hydroperoxide, following a peroxidase-like two-step oxygen-transfer mechanism involving a radical-cation intermediate. The best system, associating H(2)O(2) as oxidant and 3A3-MP8 as a catalyst, in the presence of 5% tert-butyl alcohol, led to the stereoselective S-oxidation of thioanisole with a 45% enantiomeric excess in favour of the R isomer. This constitutes the highest enantiomeric excess reported to date for the oxidation of sulfides catalyzed by hemoabzymes.
