Fourier transform infrared spectroscopy to detect thermal degradation of vegetable and chrome-tanned leather

被引:8
作者
Hassan, Rushdya Rabee Ali [1 ]
机构
[1] Cairo Univ, Fac Archaeol, Restorat & Conservat Dept, Gamaa St, Giza 12613, Egypt
关键词
Amide I; amino acids; amino group; hydrogen bond; peptide; AMINO-ACID-ANALYSIS; EDIBLE OILS; BEHAVIOR;
D O I
10.1080/00387010.2019.1623262
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
The present experimental study determined the thermal degradation stages for vegetable and chrome-tanned leathers (goat and sheep) at 90, 100, and 130 degrees C by using Fourier transform infrared spectroscopy (FTIR) and differential thermal analysis. Infrared spectra revealed that a temperature of 90 degrees C affected the adsorbed water band at 3400 cm(-1). Moreover, this temperature slightly reduced the vibrations of amide II and amid III (1340 cm(-1)) confirming the preliminary decomposition of protein folds, but it is worth noting that the aliphatic side chains remained stable at this stage of aging. At 100 degrees C, there was a sharp rupturing in the phenolic-OH bond and side-by-side N-H vibrations decreased dramatically. The peak decomposition occurred at 130 degrees C, where the amide I and amide III intensities significantly increased, which can be considered indicative of protein unfolding. Those changes are substantiation of protein denaturation. Thermal analysis demonstrated that thermal aging significantly reduced the required temperature for the process of oxidation. The oxidation occurred at 217 degrees C in goat sample aged at 90 degrees C. Nevertheless, the reference sample suffered from oxidation at about 220 degrees C, while with increasing aging temperatures (at 100 and 130 degrees C), endothermic reactions were observed. Such reactions are usually associated with protein denaturation.
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页码:288 / 296
页数:9
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