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Article

The Influence of Natural Aging Exerting on the Stability of Some Proteinaceous Binding Media Commonly Used in Painted Artworks

by
Zhenzhen Ma
1,2,3,
Lu Yang
4,5,6,
Liqin Wang
4,5,6,
Václav Pitthard
7,
Tatjana Bayerova
8,
Gabriela Krist
8 and
Xichen Zhao
1,2,3,*
1
Department of Conservation Research, Shaanxi Academy of Archaeology, Xi’an 710054, China
2
Key Scientific Research Base of On-Site Conservation, State Administration for Cultural Heritage, Xi’an 710054, China
3
Shaanxi Key Laboratory of Archaeological Conservation, Xi’an 710054, China
4
China-Central Asia “the Belt and Road” Joint Laboratory on Human and Environment Research, Xi’an 710054, China
5
Key Laboratory of Cultural Heritage Research and Conservation, Northwest University, Ministry of Education, Xi’an 710054, China
6
School of Cultural Heritage, Northwest University, Xi’an 710054, China
7
Department of Conservation Science, Kunsthistorisches Museum Wien, 1010 Vienna, Austria
8
Department of Conservation and Restoration, University of Applied Arts Vienna, 1010 Vienna, Austria
*
Author to whom correspondence should be addressed.
Coatings 2022, 12(10), 1522; https://doi.org/10.3390/coatings12101522
Submission received: 25 July 2022 / Revised: 21 September 2022 / Accepted: 8 October 2022 / Published: 11 October 2022
(This article belongs to the Special Issue Coatings for Cultural Heritage: Cleaning, Protection and Restoration)
Browse Figures
Review Reports Versions Notes

Abstract

:
Natural aging plays a key role in the degradation of proteinaceous binders which are important dispersers and stabilizers of painting layers. Knowledge about the natural aging influence on the stability of binders is important for exploring the deterioration mechanisms of painted artworks. Pig glue, whole egg, egg white, egg yolk, casein, and mixtures with ultramarine were aged for 10 years in natural conditions. GC-MS and FTIR were applied to explore the changes in the binders at a molecular level. Our experiment revealed that the less stable Met (Methionine), Lys (Lysine), Ile (Isoleucine), Ser (Serine), Asp (Aspartic acid), Glu (Glutamic acid), Hyp (Hydroxyproline), especially aromatic Phe (Phenylalanine), and Tyr (Tyrosine) were damaged, thus the contents of the stable Ala (Alanine), Gly (Glycine), Val (Valine), Leu (Leucine), and Pro (Proline) increased. The broadening of Amide A and the declining amount of α-helix, along with the increasing contents of β-sheet and random coils, all showed that the binders had transformed into disordered states. What is more, we found that pig glue had better natural aging resistance, ultramarine could speed up the aging process and lipids in egg were more easily degraded. The mechanisms of the changes of primary structures and secondary structures are also discussed in the paper.

1. Introduction

Proteinaceous binding media play an important role in scattering and consolidating pigments, which ultimately affects the permanence of paint [1]. As typical organic biopolymers, binders are degraded by light and heat, which could cause irreversible photooxidation, photochemistry, and decomposition reactions, resulting in diseases such as efflorescence and detachment in painted artworks. Despite extensive research into proteinaceous binders under short-term artificial aging [2,3,4], there is a substantial lack of knowledge regarding the long-term natural aging influence on proteinaceous binders. In this paper, five common proteinaceous binders of painted artwork (pig glue, whole egg, egg white, egg yolk, and casein), as well as mixtures with ultramarine, were aged for 10 years in natural conditions. GC-MS and FTIR were applied to study the changes in primary structures (amino acids) and secondary structures (α-helix, parallel β-sheet, anti-parallel β-sheet, random coils, and β-turns) of the proteins at a molecular level in an attempt to explore their stability characteristics for resisting natural aging. This research is of great significance to the study of the degradation mechanism of painted artworks. Furthermore, it will help with decisions regarding proper conservation materials following the artwork conservation principle, “original materials, original technique”.

2. Materials and Methods

2.1. Reagents and Chemicals

The reagents and chemicals used were pig glue (German Kremer, 63000, Aichstetten, Germany); egg (egg white and egg yolk were acquired by separating whole egg) from the market; casein (German Kremer, 63200, Aichstetten, Germany); ultramarine (German Kremer, 45040, Aichstetten, Germany); KBr. AAS 18 mixed standard amino acid solution (Sigma-Aldrich, St. Louis, MO, USA); L-Norleucine (Sigma-Aldrich, St. Louis, MO, USA); MTBSTFA (Sigma-Aldrich, St. Louis, MO, USA); pyridine (Guangfu Chemical Research Institute, Tianjin, China); ammonium hydroxide (Guangfu Chemical Research Institute, Tianjin, China); HCl (Xilong Chemical Company, Sichuan, China); He (99.999%, Messer Company, Sichuan, China); and ultrapure water (Master-S Hitech Science, Shanghai, China) [5].

2.2. Apparatus

GC-MS analysis was performed with a 7890A-5975C GC-MS (Agilent,, USA); ABJ220-4NM balance (Kern, Germany); an MS 3 DS25 vortex oscillator (IKS Klingelnberg GmbH); a KQ-50E ultrasonic cleaner (Kunshan Ultrasonic Instrument, Suzhou, China); an Anke LXJ-IIB centrifuge Anting Scientific Instrument Factory, Shanghai, China); QYN100-2 nitrogen purging apparatus (Qiaoyue Electrical Company, Shanghai, China); an MDS-8G microwave hydrolyzer (Xinyi Microwave Chemical Technology, Shanghai, China); a 10 µL injector (Agilent, Palo Alto, CA, USA); and an LS120A balance (Precisa, Zurich, Switzerland). FTIR analysis was performed with a Thermo Scientific Nicolet iN10 MX FTIR (Nicolet, Waltham, MA, USA), and a tablet press (Specac, Kent, UK), while a SOL 2 Xenon artificial aging box (Dr K. Hönle, Frickingen, Germany) was the aging apparatus.

2.3. Samples and Aging

Two sets of 3% (the proper concentration to mix pigments and paint with) pig glue, whole egg, egg white, egg yolk, and casein were deposited onto glass slides to form dry films. A third set of each binder with ultramarine was also made in the same way (simulating the painted layer composed of pigment and binders). The first set of the five pure binders was used at fresh standards, while the other two sets were aged under the SOL 2 Xenon artificial aging box, which had similar to daylight energy with a spectrum range of 300~800 nm. Illuminance was 120 lux, irradiation intensity was 910 W·m−2, lamp temperature was 50 °C, and aging time was 900 h (approximately 2 years’ natural aging). After artificial aging, the aged samples were placed in the daily environment in the Kunsthistorisches Museum. Illuminance was 30~50 lux, irradiation intensity was 230~380 W·m−2, temperature was 16~32 °C, and aging time was 10 years.

2.4. Methods

2.4.1. GC-MS

EI positive mode (70 eV) was chosen in the MS spectrometer and the MS ion source temperature was 230 °C. The MS transfer line temperature was set at 280 °C and the MS quadrupole temperature at 150 °C. A HP-5MS fused silica capillary column (30 m × 0.25 mm × 0.25 μm) was applied for the separation, and the carrier gas flowed at 1.5 mL/min. The temperature oven program was performed from 100 °C (2 min) to 280 °C at 6 °C/min in spitless mode. The pretreatments of the samples made use of previously published working methodology and the five main steps (ammonia extraction of the protein, clean-up of the upper extraction with the C4 sorbent pipette tip, hydrolysis, derivatization, and injection) followed those laid out in [6] by our research group.

2.4.2. FTIR

The extraction of the fresh, aged–pure and aged–mixed binders was performed with 2 mL 2.5 mol/L ammonia for 1.5 h. The supernatant was then acquired after being centrifuged at 5000 rpm for 5 min, twice, which was then dried on KBr pellets for use. The measuring resolution was 4 cm−1 in a range of 675~4000 cm−1, 64 times. The atmospheric interference was firstly deducted with Ominic 8.2 for baseline correction, then deconvolution of the Amide I band was performed (band enhancement factor: 3, FWHM: 42.2 cm−1). By using a seven-point Savitzky-Golay function, the second order derivatives of the spectrogram could be obtained, after which the peaks of the five secondary structures (α-helix, parallel β-sheet, anti-parallel β-sheet, random coils, and β-turns) were identified. Finally, the contents of each secondary structure were calculated with the Gaussian curve fitting method.

3. Results and Discussion

3.1. GC-MS Results

3.1.1. Individual Amino Acids

The chromatograms of the five fresh, natural-aged pure and mixed proteinaceous binders are shown in Figure 1. Met, Lys, and Tyr all disappeared after aging, in accordance with the conclusions of Prof. Colombini [2] and Prof. Shuya Wei [4].
The average contents of the 11 amino acids are illustrated in Table 1. It could be observed that the contents of Ala, Gly, Val, Leu, and Pro showed climbing trends with a rough average increase of 2% and a maximum of 2.94% in Pro. The contents of Ile, Ser, Phe, Asp, Glu, and Hyp all decreased with the most obvious decline of 3.88% in Phe. What is more, we observed the most changes in amino acid content in egg yolk (−5.91%~4.62%), followed by egg white (−4.49%~3.59%), whole egg (−4.41%~3.35%), and casein (−4.31%~2.93%), and the fewest in pig glue (−1.55%~1.85%). What should also be stressed is that the contents of most amino acids changed more obviously in the mixed binders than in the pure ones.

3.1.2. Different Categories of Amino Acids

Normally, amino acids can be divided into seven groups according to their characteristics (hydrophilic amino acids: Asp, Glu, Ser, Hyp; electriferous hydrophilic amino acids: Asp, Glu; electrically neutral hydrophilic amino acids: Ser, Hyp; hydrophobic amino acids: Ala, Gly, Val, Leu, Ile, Pro, Phe; aliphatic amino acids: Ala, Gly, Val, Leu, Ile, Ser, Asp, Glu; aromatic amino acids: Phe; imino amino acids: Pro, Hyp) [7,8]. Their total content fluctuations were calculated and then shown in Figure 2. These calculations were in accord with the values reported in Table 1. The contents of hydrophilic, electriferous hydrophilic, electrically neutral hydrophilic amino acids, and aromatic amino acids were lowered with average deductions of 6.70%, 3.93%, 2.77%, and 3.88%, respectively. Whereas the contents of the hydrophobic, aliphatic (the increase of Ala, Gly, Val, Leu > the decrease of Ile, Ser, Asp, Glu), and imino amino acids (the increase of Pro > the decrease of Hyp) rose with average amounts of 6.70%, 1.17%, and 2.71%, respectively. Similar to the individual amino acids’ changing trends, the variation range in egg yolk was the biggest (±10.80%), with those of whole egg (±7.91%), casein (±6.56%), and egg white (±6.13%) being smaller, and pig glue the smallest (±4.63%).

3.1.3. Mechanisms of the Changes in Amino Acids

Light Aging

The chemical bonds in proteins would break down when the light energy exceeded the intermolecular hydrogen bond energy and the covalent bond energy between atoms, which would result in the denaturation and degradation of proteins [9]. Table 2 shows that the energy of the light wave ranging from 280 nm to 438 nm could destroy chemical bonds such as C–N, C–S, C–C, C–O, N–H, and C–H in the main and side chains of proteins and P–O in phosphoric acids [10]. Photolytic and photooxidation reactions would thus be caused [11] and the long chains would break into short chains, resulting in the decrease of their molecular weights.
Moreover, free radicals (H, O, C, N, OH, CH3) of high activity were produced during the above reactions and they could accelerate the deterioration process. For example, Davies found that the active oxygen radical would act with all side chains in amino acids and its concentration was positively correlated with the degree of destruction [12]. Among the 11 amino acids, the benzene ring in aromatic Phe and Tyr and the element S in Met enabled them to have high reactivity towards the free radicals [13]. What is more, it was easier for Phe and Tyr to absorb ultraviolet rays, perform dehydrogenation reactions, form color rendering conjugated systems, and result in obvious photooxidation reactions, due to their benzene rings [14]. Consequently, the content of Phe decreased markedly, and Tyr almost disappeared. In addition, yellow products with carbonyl structure were formed. Baltova and Vassileva also believed that the etiolation degree kept a linear correlation with the content of carbonyl structure [15]. It is important that related research has proven that the degradation of Phe and Tyr were the key factors resulting in light aging [16], inducing diseases such as yellowing and brittleness in artworks [17]. In addition, Phe could not absorb too many photons and thus degraded less [18], but the photons absorbed by Tyr could be transported to Phe and other amino acids, promoting even more deterioration actions and obvious light aging [19].

Thermal Aging

Long-term thermal aging could destroy the structure of protein and cause diseases such as denaturation, shrinkage, brittleness, and yellowing [20]. Large amounts of research have illustrated that the thermal stabilities of the common amino acids are (Val, Leu) > Ile > Tyr > Lys > Met > Ser > (Asp, Glu) [21]. Consequently, the content of Asp, Glu, Ser, Met, Lys, Tyr, and Ile decreased while that of Val and Leu increased. The specifics are as follows: (1) The electriferous amino acids were more quickly aged than the aliphatic amino acids [22]. The stabilities of the proteins were correspondingly weakened with the decline of Asp, Glu, and Lys [23]. (2) The –OH and phenolic hydroxyl group in Ser and Tyr contributed to oxidation, which would aggravate deterioration [24]. The degradation of serine phosphate was also an important factor in the decline of Ser (Ser existed in the form of serine phosphate in egg and casein). (3) Hyp was much easier to be degraded due to oxidation caused by active –OH. (4) The experiment showed that there was a relationship between Met and the thermal stability of proteins. The sulfydryl in Met helped to form a disulfide bond which could maintain spatial conformation and contribute to thermal stability; the higher the content of S-containing amino acids, the better the thermal stability [25]. However, due to the aging process, the disulfide bonds would break down which was not helpful in stabilizing the proteins.
Based on the above light and thermal aging discussions, the contents of Ile, Ser, Asp, Glu, Lys, Hyp, Met, and especially aromatic Phe and Tyr, showed decreasing trends, while those of Ala, Gly, Val, Leu, and Pro climbed. The aliphatic (the increase of Ala, Gly, Val, Leu > the decrease of Ile, Ser, Asp, Glu) and imino amino acids (the increase of Pro > the decrease of Hyp) also increased from a combinative view. As for the decrease in hydrophilic and the increase in hydrophobic amino acids, it was speculated that the latter were surrounded by the former when the fresh proteins were in liquid states. With long-term dryness and aging, the hydrophilic amino acids outside were degraded so that the inner hydrophobic amino acids were exposed gradually [26]. Meanwhile, the decreasing amounts of the negative-charged Asp and Glu were higher than those of the positive-charged Lys. Hence, the original charge distribution was disturbed, which harmed the stability of the proteins.
Of particular interest was that the contents of those unstable amino acids Phe, Met, and Tyr in collagen were rather low compared with egg and casein. Hence, collagen’s ability to resist the natural aging process was best due to it having the highest amount of stable amino acids [27]. Other research has also pointed out that the appearance of collagen did not change obviously after light aging and it behaved the best towards natural aging [2,4,28].

The Aging-Accelerating Role of Pigment

A previous study has shown that metal ions could induce ligand–receptor reaction and change the structure and activity of proteins by acting as ligands with atoms such as S, O, and N. They then sped up the aging process and resulted in the fracture of silk fiber and a reduction in strength [29]. Karpowicz also indicated that pigment could promote aging since it was an important sensitizer [26]. As a result, it was reasonable that the contents of amino acids in the mixed binders changed more obviously than those of the corresponding pure binders.

3.2. FTIR Results

3.2.1. Spectral Changes

Figure 3 shows the FTIR comparative results of pig glue, whole egg, egg white, egg yolk, and casein before and after natural aging. The absorbance characteristics are specified in Table 3 [30,31,32]. It could be speculated that: (1) The consistent stair-step pattern formed by Amide I (1633~1663 cm−1), Amide II (1533~1562 cm−1), and Amide III (1232~1242 cm−1) of the five pure binders demonstrates that they still possessed the typical protein FTIR absorbance features [33]. However, the peaks in Amide II declined remarkably and those of Amide III disappeared in the mixed binders, suggesting that the mixed binders had lost the protein’s FTIR characteristics and ultramarine could speed up aging. (2) The Amide A regions (3281~3451 cm−1) all broadened and shifted. Doyle indicated that the broadening of Amide A illustrated that the helix structure had become dissociated [34]. Moreover, hydrogen bond, as one substantial factor for maintaining helix structure, was destroyed with aging, which would result in the shift of this absorbance [35,36]. (3) The lipid typical peaks (CH2 asymmetric stretch, CH2 symmetric stretch, and C=O stretch) in whole egg (2855~2925 cm−1, 1745~1712 cm−1) and egg yolk (2854~2925 cm−1, 1746~1712 cm−1) shifted and become weaker. Binders with ultramarine changed even more intensely, for instance, C=O in the whole egg mixed binder had completely gone, stressing the accelerated aging function of ultramarine. (4) The glucosidic bonds in whole egg and egg white showed evident changes; 1167, 1095 cm−1 became merged in 1198 cm−1 in whole egg, while 1159 and 1074 cm−1 showed blue shifts to 1184 cm−1 and 1076 cm−1, which was consistent with an early study indicating that the glucosidic bond was closely related to the stability of proteins [37]. (5) Except for in the pure pig glue, there were marked enhancements in CH3 symmetric bending vibration peaks (1377~1403 cm−1), which were important signs of aging [38].

3.2.2. Contents of the Secondary Structures

The attributions and contents of the secondary structures [39,40,41] are illustrated in Table 4. By calculating the variations of the six secondary structures (β-sheet = parallel β-sheet+ anti parallel β-sheet), it could be concluded that: (1) the contents of α-helix dramatically decreased, with the minimum reduction exceeding 20% and a maximum of 40.67% (AEWU); (2) the contents of β-sheet showed increasing trends with an average increment of 16.63%; (3) the contents of random coils climbed by an average increasing amount of 14.06% with a maximum of 23.39% (AEWU); (4) β-turns decreased at a range of −9.63%~−2.20%; (5) the contents of the secondary structures in the mixed binders changed more than those in the pure binders.
Large amounts of research have proven that light and thermal aging would result in the decrease of α-helix, the increase of β-sheet, and random coils [42,43,44,45]. This signifies that the ordered structure of proteins transforms into disordered states, partially because the bonds’ vibrations are intensive, the stretching and bending energy are increasing, and the spatial structure becomes loose with the increase in temperature. The reasons why the secondary structures showed the above changes were various. (1) α-helix would transform into β-sheet and random coils since the entropy was climbing [46,47]. (2) α-helix was more likely to be degraded because it located in the vulnerable amorphous region [48], while β-sheet was non vulnerable since it was in the stable crystalline region [49]. (3) It was confirmed that Pro impeded α-helix [50,51], while Pro, Gly, Asp, and Ser were applied more in β-turns [52,53]. Hence, α-helix decreased due to the climb of Pro while β-turns were lowered, probably attributed to the reduction of Asp. Ser exerted more influence than the increase of Pro and Gly. (4) The interactive function between protein and metal ions could change conformations. For instance, cinnabar (HgS) could form stable complexes with proteins and act as a sensitizer in cross-linking, hydrolysis, and oxidation [54]. Several pigments were known to catalyze binder deterioration [55] while finer grained pigments could provoke organic–inorganic interaction [56]. Hence, crosslinking would be induced, which would destroy the original spatial structure. It was thus speculated that the contents of the secondary structures of the mixed binders varied more.

4. Conclusions

After 10 years’ natural aging, the energy and free particles produced in reactions resulted in the breaking down of the unstable Met, Lys, Ile, Ser, Asp, Glu, and Hyp (especially aromatic Phe and Tyr), and thus a slight rise in the stable Ala, Gly, Val, Leu, and Pro in the five proteinaceous binders. The unbalanced distribution of the positive and negative charged amino acids, the broadening of Amide A, the decrease of α-helix, and the increase of β-sheet and random coils all illustrated that the ordered structures of the proteins had experienced deteriorations and transformed into disordered states.
Due to the small amount of the unstable Phe, Tyr, Met, and Lys, pig glue had better resistance towards natural aging with less content fluctuation of amino acids and secondary structures, compared with egg and casein. Ultramarine could accelerate the process of natural aging, revealing, by evident variations in the contents of amino acids and secondary structures, FTIR spectra changes and the appearance of CH3 symmetric bending vibrations. It was also found that lipids in egg were more likely to be degraded during the aging process.

Author Contributions

Conceptualization, Z.M.; methodology, L.W.; software, L.Y.; validation, L.W.; formal analysis, Z.M.; investigation, T.B.; resources, V.P.; data curation, L.Y.; writing—original draft preparation, Z.M.; writing—review and editing, L.W.; visualization, Z.M.; supervision, X.Z.; project administration, G.K.; funding acquisition, X.Z. All authors have read and agreed to the published version of the manuscript.

Funding

This research was funded by [National Natural Science Foundation of China] grant number [No. 52072228], [National Key R&D Program of China] grant number [No. 2019YFC1520100], [China Scholarship Council] grant number [No. 201506970013] and [Shaanxi Key Industry Innovation Chain Project] grant number [No. 2021ZDLSF06-05].

Institutional Review Board Statement

Not applicable.

Informed Consent Statement

Not applicable.

Data Availability Statement

Not applicable.

Conflicts of Interest

The authors declare no conflict of interest.

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Coatings 12 01522 g001a 550Coatings 12 01522 g001b 550
Figure 1. Chromatograms of the five fresh, natural-aged binders ((A) fresh pig glu-FPG, (B) aged pig glue-APG, (C) aged pig glue with ultramarine-APGU,(D): fresh whole egg-FWE, (E): aged whole egg-AWE, (F): aged whole egg with ultramarine-AWEU, (G): fresh egg white-FEW, (H): aged egg white-AEW, (I): aged egg white with ultramarine-AEWU, (J): fresh egg yolk-FEY, (K): aged egg yolk-AEY, (L): aged egg yolk with ultramarine-AEYU, (M): fresh casein-FC, (N): aged casein-AC, (O): aged casein with ultramarine-ACU).
Figure 1. Chromatograms of the five fresh, natural-aged binders ((A) fresh pig glu-FPG, (B) aged pig glue-APG, (C) aged pig glue with ultramarine-APGU,(D): fresh whole egg-FWE, (E): aged whole egg-AWE, (F): aged whole egg with ultramarine-AWEU, (G): fresh egg white-FEW, (H): aged egg white-AEW, (I): aged egg white with ultramarine-AEWU, (J): fresh egg yolk-FEY, (K): aged egg yolk-AEY, (L): aged egg yolk with ultramarine-AEYU, (M): fresh casein-FC, (N): aged casein-AC, (O): aged casein with ultramarine-ACU).
Coatings 12 01522 g001aCoatings 12 01522 g001b
Coatings 12 01522 g002 550
Figure 2. The content fluctuations of the seven groups of amino acids in the five fresh and aged binders.
Figure 2. The content fluctuations of the seven groups of amino acids in the five fresh and aged binders.
Coatings 12 01522 g002
Coatings 12 01522 g003a 550Coatings 12 01522 g003b 550
Figure 3. The FTIR spectra of the five fresh and aged binders ((A) pig glue; (B) whole egg; (C) egg white; (D) egg yolk; (E) casein).
Figure 3. The FTIR spectra of the five fresh and aged binders ((A) pig glue; (B) whole egg; (C) egg white; (D) egg yolk; (E) casein).
Coatings 12 01522 g003aCoatings 12 01522 g003b
Table
Table 1. The average contents of the 11 amino acids in the five fresh and aged binders.
Table 1. The average contents of the 11 amino acids in the five fresh and aged binders.
SamplesAlaGlyValLeuIleSerProPhe AspGluHyp
FPG11.4929.824.044.682.012.5611.992.457.7912.0111.17
APG12.3530.625.715.871.381.4013.121.107.1411.1210.18
APGU12.7531.025.476.091.031.1113.840.906.9411.009.86
FWE9.685.736.3112.914.3912.165.797.9916.5218.520.00
AWE12.068.078.7114.992.969.118.923.7714.9216.490.00
AWEU11.948.479.1015.473.018.699.143.5814.6315.960.00
FEW9.185.356.9213.625.2910.215.189.1217.0918.050.00
AEW10.446.898.7216.264.208.178.105.6415.2616.310.00
AEWU10.607.609.4015.853.937.488.774.6315.6616.080.00
FEY10.696.125.9811.414.5513.586.996.9315.1518.620.00
AEY12.7010.049.2514.723.3510.1010.601.2512.2715.720.00
AEYU13.369.879.5715.082.959.8311.601.0211.6215.100.00
FC5.203.128.7113.037.234.3515.587.1510.1225.530.00
AC7.434.4711.0014.976.092.3218.053.738.5723.380.00
ACU7.154.8211.6315.176.652.1018.302.838.4722.870.00
Table
Table 2. The energy of the different wavelengths and the chemical bonds in proteins.
Table 2. The energy of the different wavelengths and the chemical bonds in proteins.
WavelengthEnergyChemical BondsBond Energy
/nm/KJ·mol−1/KJ·mol−1
438273C–S272
392305C–N305
356336P–O335
346346C–C346
334358C–O358
308388H–N386
290412H–C411
Table
Table 3. The absorbance characteristics of the five fresh and aged binders.
Table 3. The absorbance characteristics of the five fresh and aged binders.
RegionWavenumber/cm−1Characteristics
FPGAPGAPGUFWEAWEAWEUFEWAEWAEWUFEYAEYAEYUFCACACU
Amide A330433063436329433013281329032933451328932843314331933083286N–H stretch, O–H stretch
Amide B30673074/30643071/3073307832113071/////C–N stretch
293729392931292529302940293529352926292529252929292729212932CH2 asymmetric stretch
287828792850285528582855287528762854285428552857286028522878CH2 symmetric stretch
///17451712////174617371712///C=O stretch
Amide I166016601651165816331656165916601657165716541663165916551653C=O stretch
Amide II153315361550154015371562153315331548154015421539153715381543N–H bend, C–N stretch
14491450145014621449/144914491457146514591454144714581447CH3 asymmetric bend
140614061386137914001396139814001387137713791400140314001400CH3 symmetric bend
Amide III1334133412741312//13111308////131313121316CH2 in-plane bend
1239124312411238//12391237123812381232/123912321242N–H bend
11651182/11671198/11591184 116411711185116811661163Ala, Glucoside
1083108411091095/110910741076107410941083/107410911097C–O stretch/C–N–C stretch, Glucoside
10341037103310611047////106310591059///Gly–Gly peptide chain
///972968/940945/969969972///Gly–Ala peptide chain
874875/////////////C–C stretch of Hyp
Table
Table 4. The attributions and contents of the five secondary structures of the five fresh and aged binders.
Table 4. The attributions and contents of the five secondary structures of the five fresh and aged binders.
BindersSecondary StructuresFreshAged PureAged Mixture
WavenumberContentsWavenumberContentsWavenumberContents
/cm−1/%/cm−1/%/cm−1/%
Pig glueparallel β-sheet1631.0819.631629.1818.231623.2115.18
random coils1643.132.771643.1212.531643.1515.66
α-helix1658.7941.821657.519.581662.9717.23
anti parallel β-sheet1683.3231.351678.9347.421674.7150.12
β-turns1695.764.431694.952.231691.181.81
Whole eggparallel β-sheet1629.588.321620.519.531626.8610.33
random coils1643.5912.721634.726.651642.6628.64
α-helix1660.3550.051654.2325.961657.222.98
anti parallel β-sheet1675.2418.191671.9132.481675.1536.96
β-turns1693.7910.711690.765.391692.851.08
Egg whiteparallel β-sheet1629.537.811623.856.071630.136.95
random coils1647.298.341639.8829.981645.4331.74
α-helix1669.0759.21663.5224.141666.5118.53
anti parallel β-sheet1686.4417.211679.3737.041679.8341.05
β-turns1699.677.441689.962.761692.751.73
Egg yolkparallel β-sheet1624.159.261622.1813.431628.4912.1
random coils1635.0714.881637.2924.981644.0426.45
α-helix1651.540.271658.8719.581661.8515.86
anti parallel β-sheet1671.8820.211675.6429.341677.4932.75
β-turns1693.1815.381690.3612.671692.812.83
Caseinparallel β-sheet1621.7516.741626.913.841625.7811.8
random coils1639.7315.541645.8326.931641.6925.51
α-helix1659.5727.931662.125.311662.045.23
anti parallel β-sheet1674.6829.481676.1346.821676.0451.21
β-turns1693.3210.311688.47.11686.746.25
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Ma, Z.; Yang, L.; Wang, L.; Pitthard, V.; Bayerova, T.; Krist, G.; Zhao, X. The Influence of Natural Aging Exerting on the Stability of Some Proteinaceous Binding Media Commonly Used in Painted Artworks. Coatings 2022, 12, 1522. https://doi.org/10.3390/coatings12101522

AMA Style

Ma Z, Yang L, Wang L, Pitthard V, Bayerova T, Krist G, Zhao X. The Influence of Natural Aging Exerting on the Stability of Some Proteinaceous Binding Media Commonly Used in Painted Artworks. Coatings. 2022; 12(10):1522. https://doi.org/10.3390/coatings12101522

Chicago/Turabian Style

Ma, Zhenzhen, Lu Yang, Liqin Wang, Václav Pitthard, Tatjana Bayerova, Gabriela Krist, and Xichen Zhao. 2022. "The Influence of Natural Aging Exerting on the Stability of Some Proteinaceous Binding Media Commonly Used in Painted Artworks" Coatings 12, no. 10: 1522. https://doi.org/10.3390/coatings12101522

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