http://www.cnr.it/ontology/cnr/individuo/prodotto/ID193943
Physico-chemical characterization of protein-pigment interactions in tempera paint reconstructions: casein/cinnabar and albumin/cinnabar (Articolo in rivista)
- Type
- Label
- Physico-chemical characterization of protein-pigment interactions in tempera paint reconstructions: casein/cinnabar and albumin/cinnabar (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00216-011-5684-x (literal)
- Alternative label
Duce, Celia; Ghezzi, Lisa; Onor, Massimo; Bonaduce, Ilaria; Colombini, Maria P.; Tine', Maria R.; Bramanti, Emilia (2012)
Physico-chemical characterization of protein-pigment interactions in tempera paint reconstructions: casein/cinnabar and albumin/cinnabar
in Analytical & bioanalytical chemistry (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Duce, Celia; Ghezzi, Lisa; Onor, Massimo; Bonaduce, Ilaria; Colombini, Maria P.; Tine', Maria R.; Bramanti, Emilia (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- Elsevier (literal)
- ISI Web of Science (WOS) (literal)
- Scopus (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1. Ist Chim Composti Organo Metall ICCOM UOS Pisa, Natl Res Council Italy, CNR, Area Ric, I-56124 Pisa, Italy
2. Dipartimento Chim & Chim Ind, I-56127 Pisa, Italy (literal)
- Titolo
- Physico-chemical characterization of protein-pigment interactions in tempera paint reconstructions: casein/cinnabar and albumin/cinnabar (literal)
- Abstract
- In this work, we characterized paint reconstructions using ovalbumin and casein as binders, and cinnabar (HgS) as a pigment, before and after artificial ageing. Egg and casein are common paint binders that were used historically in the technique of tempera painting. Despite extensive research on the identification of proteinaceous binders in paintings, there is a substantial lack of knowledge regarding the ageing pathway of their protein content, and their chemical interaction with inorganic pigments. Thermogravimetric analysis, infrared spectroscopy and size-exclusion chromatography (SEC) were used to reveal the physico-chemical processes involved in the ageing of proteins in paintings. Taken together, the three techniques highlighted that proteins are subject to both cross-linking and hydrolysis upon ageing, and to a lesser extent, to oxidation of the side chains. Mercury-protein interactions were also revealed using a cold vapour generation atomic fluorescence spectrometer mercury-specific detector coupled to SEC. The study clearly showed that HgS forms stable complexes with proteins and acts as a sensitizer in cross-linking, hydrolysis and oxidation. (literal)
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- Autore CNR
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