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Study of the interaction between collagen and naturalized and commercial dyes by Fourier transform infrared spectroscopy and thermogravimetric analysis

Authors :
Marco Bonanni
Emilia Bramanti
Alessandro D'Ulivo
D. Pellegrini
Roberto Bianchini
Massimo Corsi
Source :
Dyes and pigments 116 (2015): 65–73. doi:10.1016/j.dyepig.2015.01.012, info:cnr-pdr/source/autori:Pellegrini, Davide; Corsi, Massimo; Bonanni, Marco; Bianchini, Roberto; D'Ulivo, Alessandro; Bramanti, Emilia/titolo:Study of the interaction between collagen and naturalized and commercial dyes by Fourier transform infrared spectroscopy and thermogravimetric analysis/doi:10.1016%2Fj.dyepig.2015.01.012/rivista:Dyes and pigments/anno:2015/pagina_da:65/pagina_a:73/intervallo_pagine:65–73/volume:116
Publication Year :
2015
Publisher :
Elsevier BV, 2015.

Abstract

The naturalized dyes (ND) and the traditional acid dyes (ADs) were compared by studying the different behavior during the leather dyeing process. NDs are glyconjugated compounds synthesized by the covalent union of a dye species with a natural sugar (e.g. lactose) able to confer water-soluble properties to the dye molecule as a whole. The interactions between the dyes and the leather proteins were studied by FT-IR spectroscopy and thermogravimetric (TG) analyses. The protein cross-linking of the dyed leather samples was investigated by studying the 1654/1690 cm(-1) peak height ratio and a deconvolution procedure of the amide I peak. The helix secondary structure was the predominant component of the leather proteins of the samples dyed with low concentrations of NDs (2%), while the beta-sheets prevailed when leather samples were dyed with the traditional ADs and high concentrations of NDs (>5%). The data were discussed with respect to TG results. (C) 2015 Elsevier Ltd. All rights reserved.

Details

ISSN :
01437208
Volume :
116
Database :
OpenAIRE
Journal :
Dyes and Pigments
Accession number :
edsair.doi.dedup.....c20c5eb12f28d8b43f3e4ea0f791b0eb
Full Text :
https://doi.org/10.1016/j.dyepig.2015.01.012