Application of Fourier-transform infrared and Raman spectroscopy to study degradation of the wool fiber keratin

Wojciechowska, Elżbieta; Włochowicz, A.; Wesełucha–Birczyńska, Aleksandra

doi:10.1016/s0022-2860(99)00173-8

Cited by 195 publications

(139 citation statements)

References 8 publications

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“…After thermo-chemical pretreatment the proportion was shifted towards a-helix domination (65 %), further increased through substrate hydrolysis (82 %). Similar correspondence of secondary structures is typically observed between unhydrolysed and hydrolysed keratins of hair-type appendages, however unlike in the case of feather keratin, where b-sheet and other structures prevail [49,52].…”

Section: Resultssupporting

confidence: 68%

“…8). The disordered and other structures were not included in the components resolution, since their share was below 3 % in all tested samples, similarly to characteristics of wool keratin presented by Wojciechowska et al [52]. After thermo-chemical pretreatment the proportion was shifted towards a-helix domination (65 %), further increased through substrate hydrolysis (82 %).…”

Section: Resultsmentioning

confidence: 68%

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Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

Łaba

Chorążyk

Pudło

et al. 2016

Waste Biomass Valor

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Purpose The aim of the study was to apply and optimize the process of bioconversion of pig bristle waste using keratinolytic enzymes of Bacillus cereus PCM 2849, and to evaluate the amino acid composition of the resultant hydrolysate. Methods Hydrolysis with concentrated culture fluid of B. cereus was applied for bioconversion of pig bristles, after thermo-chemical pretreatment with sulfite. The effect of substrate concentration, sulfite concentration during pretreatment and reaction temperature on the release of amino acids was determined using Box-Behnken design. Amino acid composition of the obtained hydrolysate was determined by HPLC. Structural condition and substructural changes of the residual substrate were evaluated with SEM microscopy and FTIR spectroscopy. Results The applied enzymatic preparation for bristle biodegradation was verified to contain multiple proteases of a wide molecular weight range. A regression model was developed, in which influential parameters were: linear effect of substrate concentration, followed by quadratic effects of reaction temperature, substrate concentration and pretreatment. Optimum reaction conditions were also determined. The resultant hydrolysate was rich in branched-chain amino acids. Residual substrate was detriorated and sulfitolytic cleavage of disulfides and alteration of protein secondary structures was confirmed. Conclusions Application of B. cereus crude keratinase allowed for partial hydrolysis of pig bristles, preceded by sulfitolytic pretreatment. A regression model was built to describe the process of hydrolysis to release free amino acids, at constant enzyme load. Hydrolysis in given conditions allowed to obtain hydrolysate rich in branched chain amino acids. The presented process poses an alternate way of management over pig bristles, a hard-to-degrade keratinous waste.

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Section: Resultssupporting

confidence: 68%

Section: Resultsmentioning

confidence: 68%

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

Łaba

Chorążyk

Pudło

et al. 2016

Waste Biomass Valor

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“…Rather such groups are often identified through Raman spectroscopy [15][16][17][18], where such bands are typically stronger than in FTIR and NIR. Though useful in following chemical changes that occur in wool proteins [19][20][21][22], FTIR-ATR is ultimately destructive, requiring sacrificial samples that are not always accessible in historic collections. For historic tapestries, it is not possible to take samples from the front of the tapestry.…”

Section: Chemical Stability and The Oxidation Of Historic Wool Fibresmentioning

confidence: 99%

Developing a non-invasive tool to assess the impact of oxidation on the structural integrity of historic wool in Tudor tapestries

et al. 2017

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Near infrared spectroscopy (NIR) can be a useful diagnostic tool in the assessment of quality in textile, agricultural and various other industries. In cultural heritage applications, NIR as a non-invasive assessment tool is advantageous for understanding the composition or degradation of fragile historic objects that cannot be sampled. The direct interpretation of measured NIR spectra is complicated by overlapping bands produced from overtone and combination bands of chemical bonds. However, in combination with multivariate partial least squares (PLS) models and principal component analysis, the physicochemical properties of historic materials can potentially be identified by calibrating against a measured component. In this research, wool fibres from a sacrificial collection of historic tapestry fragments housed at Hampton Court Palace were analysed. The cystine oxidation products of historic wools which can be related to the embrittlement of fibres and ultimately fibre loss, were recorded using Fourier transform infrared (FTIR) spectroscopy. A PLS predictive model was then developed using previously measured NIR spectra for the same historic tapestry fragments to predict the ratios of the cystine oxidation species in historic wools measured in this research. The prediction of a validation set of historic tapestry fragments with known oxidation product ratios was found to be accurate to root mean squared errors of prediction (RMSEP) of 0.11 for cysteic acid/cystine dioxide, 0.03 for an oxidation ratio of cysteic acid/cystine monoxide and 0.06 for cystine dioxide/cystine monoxide. The model was applied successfully to an independent set of historic tapestry fragments with unknown oxidation ratios with an M-distance pass limit of 3. The models were also applied to NIR measurements of historic tapestries on open display with limited success. Alternative methods to investigate and account for errors in this research are proposed. The potential for NIR to be used by conservators as a non-invasive tool for the assessment of textiles, complementing current condition audit practices in use at heritage institutions is also discussed.

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“…Natural wool and feather have regular α-helix and β-sheet structures, which are converted into a random coil structure by disrupting the bond network and protein structure using chaotropes (Fig.1). A random coil is a looser structure of protein and hence more sites are available for pollutant absorption [31][32][33] . However, the pollutant absorption depends on a range of factors such as composition of absorbent and its amount, specific surface area and activity, physical form of absorbent, solution pH, initial concentration of pollutants, temperature, and also the presence of other pollutants and their concentrations.…”

Section: Mechanisms Of Pollutant Removalmentioning

confidence: 99%

Keratinous Materials as Novel Absorbent Systems for Toxic Pollutants

Ghosh¹,

Collie²

2014

DSJ

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Application of Fourier-transform infrared and Raman spectroscopy to study degradation of the wool fiber keratin

Cited by 195 publications

References 8 publications

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

Developing a non-invasive tool to assess the impact of oxidation on the structural integrity of historic wool in Tudor tapestries

Keratinous Materials as Novel Absorbent Systems for Toxic Pollutants

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