Investigating the microstructure of keratin extracted from wool: Peptide sequence (MALDI-TOF/TOF) and protein conformation (FTIR)

Cardamone, Jeanette M.

doi:10.1016/j.molstruc.2010.01.048

Cited by 168 publications

(116 citation statements)

References 28 publications

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“…Waste wool processed using a conventional method generated hydrolyzed keratin with a protein content by 63.26% whereas that produced by the painting process had a protein content by 54.47%. According to Cardamone (2010), wool contains up to 95% by weight of pure keratin. The lower keratin content generated in this experiment may be caused by the age and species of the sheep (Sarkar, 1995).…”

Section: Protein Contentsmentioning

confidence: 99%

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Sheep wool-derived hydrolyzed keratin from tannery waste of the tanning industry using perhydrol

Prayitno¹,

Rahmawati²,

Griyanitasari³

2017

MKKP

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Sheep wool waste discharged from leather tanning industry recently has posed a problem in relation to its treatment because of its sizeable quantity and its difficulty to degrade. Wool is composed mainly of keratin. It is a protein with a high content of disulfide bonds which cause the protein keratin cannot dissolve in water and resist of diluted acids and alkalis. Keratin can be hydrolyzed to produce keratin hydrolysates which have many benefits such as for cosmetic additives. Research into the use of waste wool of sheep originated from the sheep leather tanning industry had been performed by using a hydrolyzed system to produce protein keratin. The waste wool used came from unhairing by painting and conventional unhairing. Hydrolysis was done using hydrogen peroxide 50% amounting to 70 ml for every 40 gr of wool. Hydrogen peroxide was added to wool immersed in the 0.5 M NaOH solution for three hours. The length of hydrolysis ranged from 4, 5, to 6 hours and the mix was stirred shortly every 1 hour followed by filtration using a coarse sieve. To precipitate the hydrolyzed keratin, the pH was decreased to 4-5 using the 2 M HCl solution and after separation of the precipitation, it was dried in the oven at a temperature not more than 50 o C for 2 days. The research findings showed that a maximum of 69.19% of keratin hydrolysates was generated using the raw material of waste wool through a conventional process with a total of hydrolysis time by 6 hours, whereas the maximum protein generated was 66.99% using waste wool through a conventional process with a total of hydrolysis time by 4 hours. The FTIR test showed the presence of groups of amides, cysteic acids, and cystine-S-monoxide.

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Section: Protein Contentsmentioning

confidence: 99%

“…According to Cardamone (2010), wool contains 95% w/w pure keratin and keratin derived from wool is clay, hard, and insoluble. According to Sarkar (1995), the amount of keratin in the skin varies according to species and age of the animal.…”

Section: Introductionmentioning

confidence: 99%

Sheep wool-derived hydrolyzed keratin from tannery waste of the tanning industry using perhydrol

Prayitno¹,

Rahmawati²,

Griyanitasari³

2017

MKKP

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“…To analyse the amide I band component, the second derivative spectra was curve fitted and used to identify the composite absorptions attributed to α-Helix, β-Sheet and disordered microstructural components, respectively, before and after 50 days of anaerobic digestion (Kong and Yu, 2007). The percentage of the α-Helix, β-Sheet and disordered microstructures were determined by adding the sum of absorptions for each and stating their sums as a fraction of total amide I band area (Cardamone, 2010).…”

Section: Methodsmentioning

confidence: 99%

Dry anaerobic digestion of lignocellulosic and protein residues

2015

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HIGHLIGHTSAD digestion/co-digestion of wool and wheat straw were evaluated with TS contents of between 6 to 30%.Methane yield of wheat straw was highest at TS of 21% and lowest at TS of 30%.Methane yield of wool textile was highest at TS of 13% and lowest at TS of 30%.The addition of enzyme on wool and wheat straw led to improvement in methane yield at TS of 13%.Synergetic effects were observed when these substrates were co-digested. Utilisation of wheat straw and wool textile waste in dry anaerobic digestion (AD) process was investigated. Dry-AD of the individual substrates as well as co-digestion of those were evaluated using different total solid (TS) contents ranging between 6 to 30%. Additionally, the effects of the addition of nutrients and cellulose-or protein-degrading enzymes on the performance of the AD process were also investigated. Dry-AD of the wheat straw resulted in methane yields of 0.081 -0.200 Nm 3 CH4/kgVS with the lowest and highest values obtained at 30 and 21% TS, respectively. The addition of the cellulolytic enzymes could significantly increase the yield in the reactor containing 13% TS (0.231 Nm 3 CH4/kg VS). Likewise, degradation of wool textile waste was enhanced significantly at TS of 13% with the addition of the protein-degrading enzyme (0.131 Nm 3 CH4/kg VS). Furthermore, the co-digestion of these two substrates showed higher methane yields compared with the methane potentials calculated for the individual fractions at all the investigated TS contents due to synergetic effects and better nutritional balance. © 2015 BRTeam. All rights reserved. Kabir et al. / Biofuel Research Journal 8 (2015) [309][310][311][312][313][314][315][316] Please cite this article as: Kabir M.M., Taherzadeh M.J., Sárvári Horváth I. Dry anaerobic digestion of lignocellulosic and protein residues. ARTICLE INFO ABSTRACT

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“…The peaks at 3380 cm -1 and 2920 cm -1 are hydroxyl stretching influenced by hydrogen bonding and methylene, respectively. In addition, the absorption peak at about 1000-900 cm -1 is sulfitolysis cleavage of the cysteine disulfide bond 29 . The results indicated that sericin and starch showed absorption peaks at the amide I region that were higher than the native keratin film.…”

Section: Secondary Structure Analysismentioning

confidence: 99%

Preparation and Characterization of Keratin Blended Films using Biopolymers for Drug Controlled Release Application

Thonpho¹,

Srihanam²

2016

Orient. J. Chem

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Keratin solution was separately blended with collagen, gelatin, sericin and starch for films preparation. All the blended films had smooth surfaces without phase separation, except the keratin/ starch blend film. The native keratin film showed small particles embedded in all the film surfaces that resulted in them being rough. The structure of the native keratin film changed from beta-sheet to random coil at high blend ratio of other substances. This result increased the dissolution of the films especially the keratin/starch blend. The results relate directly to the decreased thermal stability of this film. However, the changes in structure did not affect the chlorhexidine release pattern. It is possible that the interaction between the drug and blending substances, and the substances to water molecules are the main factor influencing the drug release pattern from the films.

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Investigating the microstructure of keratin extracted from wool: Peptide sequence (MALDI-TOF/TOF) and protein conformation (FTIR)

Cited by 168 publications

References 28 publications

Sheep wool-derived hydrolyzed keratin from tannery waste of the tanning industry using perhydrol

Sheep wool-derived hydrolyzed keratin from tannery waste of the tanning industry using perhydrol

Dry anaerobic digestion of lignocellulosic and protein residues

Preparation and Characterization of Keratin Blended Films using Biopolymers for Drug Controlled Release Application

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