Scholarly record
BEHAVIOUR OF ANIMAL-ORIGIN GELATINS TO ARTIFICIAL AGEING IN THE PROCESS OF RESTORING GILDED WOOD
Abstract
Animal-origin glues are adhesives made by boiling animal tissues for a long time, and from the chemical point of view they are gelatinous and albuminoid protein substances bearing different names. The most frequently used are gelatins. They are extracted from raw animal hide residues, from cartilages, tendons, and from the gelatinous matter extracted from bones, on which the name and quality of gelatin depends. The gelatin extracted from unhaired hide waste/pelt waste resulting from unhairing bovine hide from tanneries was used in this article to study the behaviour to accelerated ageing of two types of gelatins used for gilding some wood samples with gold leaf. In this paper we aimed to find the damaging effects of heat and relative humidity on the gelatines (extracted from bovine hide and rabbit skin) based adhesives used for wood gilding. Therefore, a gold leaf was applied to a fir wood (pine tree) conditioned for ten years using commercial gelatin extracted from rabbit skin as well as gelatin extracted from bovine hide by-products. The gilding technique followed the traditional recipe in which adhesive, multiple layers of plaster, bolus were employed in order to fix the gold leaf. The gilded wood prepared as such was artificially aged in a special Binder-type aging chamber at 60? for 7 days, followed by conditioning in an incubator at 70% R.H., at 25? for 2 days, in nine cycles. The physical-chemical changes of gelatin-based adhesives resulting from these conditions, as well as stratigraphic and microstructural characteristics of gilding layers were analyzed by applying optical microscopy, colorimetric measurements and infrared spectroscopy with attenuated total reflection (FTIR-ATR). The obtained results showed that both gelatins have very good adhesive and structural properties and could be successfully used in the field of conservation and restoration.
Publication Impact Profile
Publication details
References17
Sandu I.C.A., de Sa M.H., Pereira M.C., Ancient �gilded� art-objects from Europeancultural heritage: a review on different scales of characterization, Surface and InterfaceAnalysis, Special Issue dedicated to Cultural Heritage, 43/8, pp. 1134-1151, 2011. DOI: 10.1002/sia.3740
Carvalho A. P., Vaz M.F., Ferreira M.M., Pires J., Gilded Wood from the Organ ofthe Church of Santa Cruz (Coimbra), Journal of the Brazilian Chemical Society, 19/1,pp. 1653-1658, 2008. DOI: 10.1590/s0103-50532008000800029
Ebnesajjad S., Landrock A. H., Characteristics of Adhesive Materials, AdhesivesTechnology Handbook, pp. 84�159, 2015, DOI: 10.1016/b978-0-323-35595-7.00005-x.
Emblem A., Hardwidge M., Adhesives for packaging, Packaging Technology, pp.381�394, 2012, DOI: 10.1533/9780857095701.2.38. 1
Schellmann, N.C., Animal glues: a review of their key properties relevant toconservation, Stud Conserv, 2007, 52, 8, 55-66, https://doi.org/10.1179/ sic.2007.52.Supplement-1.55 DOI: 10.1179/sic.2007.52.supplement-1.55
Miu L., Niculescu M., Preliminary study on the adhesiveness properties of hide glue,Leather and Footwear Journal, vol 22 (2), 139-149, DOI: 10.24264/lfj.22.2.7
Gilchrist A., Nobbs J., Colorimetry, Theory, University of Leeds, 2017 Elsevier,328-333 DOI: 10.1016/b978-0-12-803224-4.00124-2
*** A guide of colorimetry, Cambridge, England, https://www.sherwoodscientific.com/
Sabatini F., Giugliano R., Degano I., Lluveras-Tenorio A., Sokolova R., Thoury M.,Colombini M.P., Development of a multi-analytical approach to investigate the fadingof eosin in painting matrices, Materials Science and Engineering 364 (2018) 012066DOI: 10.1088/1757-899X/364/1/012066
*** https://en.wikipedia.org/wiki/CIELAB_color_space
Barth A., Infrared spectroscopy of proteins, Biochimica et Biophysica Acta, 1767,pp. 1073-1101, 2007. DOI: 10.1016/j.bbabio.2007.06.004
Glassford S.E., Byrne B., Kazarian S.G., Recent applications of ATR FTIRspectroscopy and imaging to proteins, Biochimica et Biophysica Acta, 1834, pp. 2849�2858. 2013, DOI: 10.1016/j.bbapap.2013.07.015.
Derkach S. R., Kuchina Y. A., Baryshnikov A.V., Kolotova D.S., Voron�ko N.G.,Tailoring Cod Gelatin Structure and Physical Properties with Acid and AlkalineExtraction, Polymers 11/10. 1724, 2019, DOI: 10.3390/polym11101724.
Cappa F., Paganoni I., Carsote C., Schreiner M., Badea E. Studies on the effect ofdry-heat ageing on parchment deterioration by vibrational spectroscopy and micro hottable method, Polymer Degradation and Stability 182:109375, 2020,DOI: 10.1016/j.polymdegradstab.2020.109375.
Vichi A., Eliazyan G., Kazarian S.G., Study of the degradation and conservation ofhistorical leather book covers with Macro Attenuated Total Reflection-FourierTransform Infrared Spectroscopic Imaging. ACS Omega. 3 pp. 7150�7157, 2018. DOI: 10.1021/acsomega.8b00773
Koochakzaei A., Determination of sulfuric acid effects on degradation andstructural changes of gelatin using Fourier-transform infrared spectroscopy and peakdeconvolution analysis, Advances in Infrared Spectroscopy, 38/S8, pp. 5-11, 2023,DOI: 10.56530/spectroscopy.tw7684z4.
Rabotyagova O.S., Cebe P., Kaplan D.L. Collagen structural hierarchy andsusceptibility to degradation by ultraviolet radiation, Materials Science and EngineeringC, 28, pp. 1420�1429, 2008, DOI: 10.1016/j.msec.2008.03.012.
View or Download full articleAccess options
SWS access login
Login as SWS Scientific CommitteeLogin as SWS Scientific PartnerLogin as SWS AuthorAuthors and approved SWS contributors will read and export their own linked papers after identity matching by SWS profile, email and SGEM GlobalID.
For librarian assistance: [email protected]
Purchase Instant Access
- Article can be downloaded after successful payment.
- Article may be used according to SWS library access terms.
- Article cannot be redistributed.

