The impacts of two hybrid cloned commercial cellulases designed for detergency on cotton fibres were compared. HiCel45 has a family 45 catalytic domain and a fungal cellulose binding module (CBM) from the fungus Humicola insolens. BaCel5 has a family 5 catalytic domain and a fungal CBM from Bacillus spp. BaCel5 bound irreversibly to cellulose under the buffer conditions tested while HiCel45 was found to bind reversibly to cellulose because it showed low adsorption. BaCel5 seems to yield more activity towards cotton than HiCel45 under mild stirring conditions, but under strong mechanical agitation both enzymes produce similar amount of sugars. HiCel45 had a more progressive production of residual reducing ends on the fabric than BaCel5. These studies seem to indicate that HiCel45 is a more cooperative enzyme with detergent processes where high mechanical agitation is needed.
Díaz, M.; Rocasalbas, G.; Francesko, A.; Touriño, S.; Torres, J.; Tzanov, T. Biocatalysis and biotransformation Vol. 30, num. 1, p. 102-110 DOI: 10.3109/10242422.2012.646676 Data de publicació: 2012-01-18 Article en revista
The chronic wound environment is characterized by high concentrations of reactive oxygen species (ROS) and elevated
levels of myeloperoxidase (MPO) and collagenases, together impairing the healing process. Therefore, the management of chronic wounds at a molecular level requires the synergistic use of antioxidants, MPO and collagenase inhibitors to simultaneously target multiple factors from wound pathogenesis. In this study, a polyphenolic extract from Hamamelis virginiana plant, rich in condensed and hydrolysable oligomeric tannins, was evaluated as an inhibitor of MPO and collagenase.In addition to efficient scavengers of radical and non-radical reactive species, H. virginiana polyphenols were found to act as substrates in the MPO peroxidase cycle, preventing the accumulation of ROS in the chronic wound
site. Furthermore, it was also found that the plant exerts an irreversible inhibitory effect on collagenase activity (IC50 = 75 ± 10 μg/mL)
A bioprocess for machine washable wool, combining the advantages of both protease and transglutaminase in a simultaneous enzymatic treatment has been developed. This process reduced the felting tendency of woven wool fabrics by 9% at the expense of only 2% weight and tensile strength loss. In contrast to previously described protease-based processes for shrink resistant wool, the anti-felting properties achieved in the simultaneous enzymatic treatment produced insignificant fibre damage, confirmed also by scanning electron images of the fabrics.
Calafell, M.; Diaz, C.; Hadzhiyska, H.; Gibert, J.; Daga, J.; Tzanov, T. Biocatalysis and biotransformation Vol. 25, num. 2-4, p. 336-340 DOI: 10.1080/10242420701379874 Data de publicació: 2007-03 Article en revista
Cotton fabrics were dyed with dyes generated in situ by laccase-catalyzed oxidative coupling of the colorless 2,5-diaminobenzenesulfonic acid (2,5-DABSA) and 1-hydroxyphenol (catechol). The enzymatic oxidation of the dye intermediates led to cross-coupling reaction products when the reaction was conducted with an excess of catechol. At least fourfold excess of catechol was necessary to achieve satisfactory dye fixation on cotton. Formation of the same colored product using either an equimolar ratio of the reagents or tenfold excess of catechol was observed. Most probably, homo-molecular reactions predominate over the cross-coupling at equimolar ratio of the precursors, while with an excess of catechol, the cross-coupling occurs in higher yield. The reaction was followed using UV-Vis spectroscopy, HPLC, FTIR and MALDI-TOF MS. A reaction pathway for laccase-induced cross-coupling of catechol and 2,5-DABSA yielding a major colored product was proposed.