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Surface modification of polyamide 6.6 fibers by enzymatic hydrolysis
National Technical University of Athens, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens.
MIRTEC, Materials Industrial Research & Technology Center S.A.
Surface Science Laboratory, Department of Chemical Engineering, University of Patras.
Surface Science Laboratory, Department of Chemical Engineering, University of Patras.
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Number of Authors: 62016 (English)In: Process Biochemistry, ISSN 1359-5113, E-ISSN 1873-3298, Vol. 59 A, p. 97-103Article in journal (Refereed) Published
Abstract [en]

Synthetic fibers are used extensively in textile industry, however, their high hydrophobicity is a drawback that needs to be considered. The decrease of hydrophobicity can be achieved via a ‘green” root using enzymes as biocatalysts. In this study, the enzymatic surface modification of polyamide (PA) 6.6 fabric was studied with the use of the commercial protease Alcalase 2.4 L at optimal conditions. The modified fabrics were studied via dyeing parameters K/S and ΔΕ values. For treatment at 40–60 °C and pH 8 ΔE was found to be approximately 14 and K/S was 1.24-fold increased. Additionally, the enzymatic surface modification of PA textile was justified using different spectroscopy techniques, such as FTIR-ATR and XPS. FTIR-ATR indicated alterations of Cdouble bond; length as m-dashO and N-H band intensities, while via XPS, there proved to be differences in relative intensities of carbon component peaks. Finally, thermogravimetric and mechanical tests were also conducted to prove the non-degradation of the properties of the bulk material. In conclusion, the investigated enzymatic process increased the hydrophilicity with 2.7-fold increased water absorbency and 1.24-fold enhanced color strength of PA textiles, while maintaining the thermal and mechanical properties of the bulk synthetic material.

Place, publisher, year, edition, pages
2016. Vol. 59 A, p. 97-103
National Category
Bioprocess Technology
Research subject
Biochemical Process Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-5161DOI: 10.1016/j.procbio.2016.06.022ISI: 000407983700013Scopus ID: 2-s2.0-84977671879Local ID: 331ae157-3dc7-477c-827a-90045e41e88eOAI: oai:DiVA.org:ltu-5161DiVA, id: diva2:978035
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Konferensartikel i tidskrift

Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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Christakopoulos, Paul

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