Thermostabile und alkaliresistente Proteasen in der Wollveredlung : Möglichkeiten der industriellen Nutzung und Auswirkungen auf Wolle

This work aimed at the industry related development of an enzymatic finishing treatment based on the finishing processes of a medium-seized textile plant (Tuchwerk Westmark, Mönchengladbach (TW)). Moreover the wool modifying potential of enzyme preparations from newly isolated hyperthermophilic micro organisms provided by the TU Hamburg-Harburg (TU-HH) were to be investigated. Of the three enzyme preparations from the TU-HH only the culture supernatants of Fervidobacterium gondwanense and Thermoanaerobacter keratinophilus are generally able to modify wool. However due to the low activity the industrial use of the culture supernatant of F. gondwanense in reasonable treatment time and dosage is not sensible. The enzyme fraction of the culture supernatant of T. keratinophilus showed a higher activity towards wool. Nonetheless the incubation didn’t result in positive effects on the degree of whiteness or the dye ability of wool top. The available portion of enzyme only allowed a limited amount of experiments. Therefore a concluding evaluation of a potential use of the enzyme preparation of T. keratinophilus in the textile technical process was not possible. Investigations in laboratory scale with the commercial available thermo stable and alkali-resistant serine protease Esperase 8.0 L (Novo Nordisk) showed that the treatment parameters of the pre washing step to the dyeing of wool fabrics at TW are suitable for the integration of Esperase 8.0 L. The hard well water used at TW and the added water softener showed no impact on the enzyme catalysed wool modification. The auxiliaries used have synergistic effects on the influence of the enzyme with regard to the degree of whiteness and the dye ability. After the completed pre washing the Esperase 8.0 L does not show an activity, it is consequently irreversible heat-denatured. The denaturation is necessary to rule out uncontrolled enzyme catalysed reactions in the following finishing steps or at the end consumer (e.g. while washing). The treatment that was carried out successfully in laboratory scale was up-scaled to the semi industrial scale. In the 40 l winch beck at TW several wool- and blended fabrics were treated with Esperase 8.0 L and afterwards dyed in competition with blind treated reference fabric. Additionally the impact of the enzyme treatment was compared with the effects of a traditional chlorination with Basolan DC exemplary on one fabric that was also available in chlorinated form. The semi-industrial treatment with Esperase 8.0 L did not influence or enhance the degree of whiteness respectively, whereas the chlorination caused a yellowing of the fabric. The dyeability of the enzyme treated samples at 100 °C and the printability with an Ink Jet are comparable with that of chlorinated fabric. Due to the different kind of modification of the wool the enzyme treatment but not the chlorination implies the possibility of a low temperature dyeing. This is especially interesting for the industry because of ecological and economic reasons. The felting tendency of the enzyme treated fabrics was significantly reduced but for strongly felting fabrics an anti-felting treatment can not be reached. The fabric that was used to compare the chlorination to the enzyme treatment showed only a slight felting tendency (each ~ 3% in broadness and length) that was reduced by the chlorination as well as the enzyme treatment to the same extent. Therefore the impact of the enzyme treatment with Esperase 8.0 L on the felting behaviour of this kind of wool fabric is regarded as comparable to that of the chlorination. In the last part of this work the mode of action of the proteases used was investigated and checked if they are able to catalyse not only the hydrolysis of the “non-keratinous” parts of wool but also the hydrolysis of the KIF and KAP. Esperase 8.0 L catalyses at the begin of the reaction the hydrolysis of the endocuticle and the soluble proteins of the ZMK entering via the ZMK the cortex and accumulate within the nucleus remnants. Moreover also the degradation of a low amount of the HGT proteins is catalysed. The mode of action of the serine protease from T. keratinophilus is comparable to this of the Esperase 8.0 L. The KIF as well as the HS proteins of the matrix are not accessible for these enzymes and for the serine protease from F. gondwanense.

Grantor dc:publisher

Publikationsserver der RWTH Aachen University

Year dc:date

2002

Author dc:creator

• Schumacher, Karin

Contributors dc:contributor

• Höcker, Hartwig

• info:eu-repo/classification/ddc/660
• Technische Chemie
• Wolle
• enzymatische Veredlung
• thermostabile und alkaliresistente Proteasen

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

ger

Identifier

https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-121319%22

OAI identifier oai:identifier

oai:publications.rwth-aachen.de:59540