Treatment of effluents containing phenols such as textile dyes with fungal laccases is usually limited to the acid to neutral pH range and moderate temperatures. Here we demonstrate for the first time that spore-bound laccases which are stable at high temperatures and pH values can be used for phenolic dye decolorisation. Laccase containing spores from Bacillus SF were immobilized on alumina pellets. Both immobilized and free spores were able to completely decolorize the common textile dyes Mordant Black 9, Mordant Brown 96/Mordant Brown 15, and Acid Blue 74 within 90 min of incubation time and decolorized solutions were successfully used in re-dyeing.

Upgrading of the surface characteristics could enhance the bulk properties of naturally abundant fiber-forming materials for better performance or create new value-added products. Laccase can induce cross-linkage and covalent coupling of low molecular weight compounds onto lignocellulosic surfaces. For this purpose the 38-kDa laccase from Trametes hirsuta was purified and characterized. The best conditions for laccase-induced coating of flax fibers were determined. This evaluation was based on the obtained coloration and color depth. A screening was carried out with different phenols for their potential as monomers for enzyme-catalyzed polymerization resulting in a coating with antibacterial performance. While all the methoxyphenols showed different coloration with weak fastness properties, bacterial growth of Bacillus subtilis and Staphylococcus aureus was reduced significantly using ferulic acid and hydroquinone. Using laccase-induced coupling and polymerization, multi-functionality of the lignocellulosic surface, such as coloration and antimicrobial performance, was achieved, which depended on the nature of the applied phenolic monomer.

The chemical functionalization with fluorinated silane provides considerably improved water and oil washability of highly conductive stretchable nanocomposite fibers.

The protease Esperase † was modified by covalent bonding with two grades of a reversible soluble-insoluble co-polymer of methacrylic acid and methyl-methacrylate, namely Eudragit † L 100 and Eudragit † S 100. The optimum reaction conditions and washing protocol were investigated and it was found that Esperase † modified with Eudragit † L 100 showed greater activity than if modified with Eudragit † S 100. This should be expected as there is a greater quantity of active sites, namely carboxyl groups, per mass of Eudragit † L 100 in comparison with Eudragit † S 100 to interact with the enzyme. Gel filtration confirmed that Eudragit † L 100 covalently bonded to Esperase † . Treatment of the modified Esperase † on wool showed that the enzyme modified with Eudragit † L 100 had greater activity towards the wool and appeared more effective in shrink resistant finishing.