Alkali Solubilization of Chicken Feather Keratin

Nagai, Yasushi; Nishikawa, Tetsusaburo

doi:10.1080/00021369.1970.10859572

Cited by 12 publications

(10 citation statements)

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“…). It has also been reported that the number of cysteine residues tends to decrease during solubilization (Goddard & Michaelis ; Nagai & Nishikawa ). Therefore, it was suggested that hydrolysis led to a decrease in the amount of cysteine in both HFK and HWK.…”

Section: Resultsmentioning

confidence: 93%

Properties of alkaline‐hydrolyzed waterfowl feather keratin

Tsuda

Nomura

2013

Animal Science Journal

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The properties of hydrolyzed feather keratin (HFK) were compared to those of hydrolyzed wool keratin (HWK) with the aim of developing better ways to utilize feather keratin waste. Amino acid analysis showed that HFK contained more hydrophobic amino acids did than HWK. Although gel permeation chromatography indicated that HFK and HWK had more low-molecular weight peptides than their intact sources, Fourier transform infrared spectroscopy indicated that both hydrolyzed keratins retained their original secondary structure. The physical properties of HFK were evaluated by treating HFK to human hair fibers. HFK treatment enhanced significantly the surface hydrophobicity and strength of fibers, and HFK was more permeable into hair fibers. These results suggest that HFK is suitable for industrial applications to improve fibers. In addition, HFK may be suitable for raw material of products requiring both flexibility and hydrophobicity, such as films and biodegradable plastics.

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Section: Resultsmentioning

confidence: 93%

Properties of alkaline‐hydrolyzed waterfowl feather keratin

Tsuda

Nomura

2013

Animal Science Journal

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“…12 This is one of the main drawbacks of this method that can affect the quality of the final product due to loss of water-soluble protein material containing valuable amino acids such as cysteine. 30,31 The alkali method had the lowest keratin extraction yield (≅25%) and protein yield (≅63%) compared to the other methods which were probably due to extensive hydrolysis of the protein polypeptides and degradation of amino acids including cysteine residues [32][33][34][35] Therefore, a large amount of protein content would be lost during dialysis. Nagai and Nishikawa 34 observed that half of the starting material was lost during the process which probably occurred during the dialysis process.…”

Section: Extraction and Protein Yieldmentioning

confidence: 99%

Evaluation of keratin extraction from wool by chemical methods for bio-polymer application

Shavandi

Bekhit

Carne

et al. 2016

Journal of Bioactive and Compatible Polymers

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This study investigated some physicochemical properties of keratin extracted from Merino wool using five chemical extraction methods: alkali hydrolysis, sulfitolysis, reduction, oxidation, and extraction using ionic liquid. The ionic liquid method produced the highest protein yield (95%), followed by sulfitolysis method (89%), while the highest extraction yield was obtained with the reduction method (54%). The lowest yield was obtained with the oxidation method (6%). The oxidation extract contained higher molecular weight (>40 kDa) protein components, whereas the alkali hydrolysis extract contained protein material of <10 kDa. The sulfitolysis, reduction, and ionic liquid extracts contained various protein components between 3.5 and 60 kDa. Keratin obtained from various extraction methods had different yield, morphology, and physicochemical properties. None of the samples were toxic to L929 fibroblast cells up to a concentration of 2.5 mg/mL. Apart from the alkali hydrolysis extract, all other keratin extracts (reduction, sulfitolysis, ionic liquid, and oxidation) showed Fourier transform infrared adsorption peaks attributed to the sulfitolysis–oxidation stretching vibrations of cysteine-S-sulfonated residues, with the oxidation extract showing the highest content of cysteine-S-sulfonated residues. This study indicates that the properties of the keratin extract obtained vary depending on the extraction method used, which has implications for use in structural biomaterial applications.

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“…Determination of the molecular weight of peptides by SDS-PAGE (19) Electrophoretic pro les of hydrolysates obtained revealed subtle differences. While two peptide fractions of 130 and 250 kDa molecular weights were dominated in all hydrolysates, in that of No.…”

Section: Solubility Properties Of Hydrolysatesmentioning

confidence: 99%

An Optimal Designed Experiment for the Alkaline Hydrolysis of Feather Keratin

Dąbrowska

Sommer

Sinkiewicz

et al. 2021

Preprint

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Feathers, burdensome waste from the poultry industry, can be a cheap source of keratin, a protein with excellent physicochemical, biological and mechanical properties. The high yield of the keratin isolation is ensured by alkaline hydrolysis. This study aimed at assessing the statistically significant effect of input variables in the alkaline hydrolysis of keratin from chicken feathers on the process yield and on the molecular weight of peptides obtained. The volume ratio of 1M NaOH to the feathers mass, the hydrolysis time and the shaking speed of the reaction mixture were analyzed. The use of statistical analysis at the design step of experiment allowed to reduce of the trials number from 27 to 9. Among the input variables analyzed, only the volume ratio of 1M NaOH to the feathers mass had a significant effect on the process yield, while none of them significantly affected the molecular weight of the peptides obtained. All hydrolysates were dominated by two peptides fractions, with molecular weights of ca. 130 and 250 kDa, and mixture of many peptides of weight close to 10 kDa and smaller. Alkaline hydrolysis of feather keratin yielded protein hydrolysates soluble over a wide pH range.

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Alkali Solubilization of Chicken Feather Keratin

Cited by 12 publications

References 0 publications

Properties of alkaline‐hydrolyzed waterfowl feather keratin

Properties of alkaline‐hydrolyzed waterfowl feather keratin

Evaluation of keratin extraction from wool by chemical methods for bio-polymer application

An Optimal Designed Experiment for the Alkaline Hydrolysis of Feather Keratin

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