Solubilization of Chicken Feather Keratin by Ammonium Copper Hydroxide (Schweitzer's Reagent)

Nagai, Yasushi; Nishikawa, Tetsusaburo

doi:10.1271/bbb1961.34.575

Cited by 5 publications

(6 citation statements)

References 2 publications

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“…When oxidation is applied to extract keratin, strong oxidants are used, such as hydrogen peroxide (Breinl & Baudisch, ), potassium permanganate (Lissizin, ), ammonium copper hydroxide (Nagai & Nishikawa, ), and organic peracids (de Guzman et al, ). The disulfide bonds are converted to sulfonic acid groups and cysteic acid derivatives are formed, which are referred to as “keratoses”:

RS - SR + true[normalO true] \to R - {SO}_{2} H + R - {SO}_{3} H

…”

Section: Solubilization Of Keratinsmentioning

confidence: 99%

Solubilization of keratins and functional properties of their isolates and hydrolysates

2018

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The keratinous wastes of the textile industry and poultry slaughterhouses may be used as sources of soluble keratins or hydrolysates. This review presents methods for processing raw keratin-based materials into bioproducts with functional and bioactive properties suitable for biomedical, cosmetic, food, and agricultural applications. Soluble keratin can be obtained by thermal treatment in some organic solvents, reduction, or oxidation of the disulfide bonds. Recent studies have shown that keratins contain amino acid sequences with high biological activities such as antioxidant, angiotensin I converting enzyme inhibitory, dipeptidyl peptidase IV inhibitory, and antimicrobial.Peptides containing these sequences may find numerous applications as value-added products in the food industry. More research devoted to development of methods for conversion of animal by-products to novel products is needed. Further technological investigations to create large-scale production methods are also necessary. Practical applicationsThe keratinous wastes represent a problematic by-product to the wool textile industry and poultry slaughterhouses due to the large volumes and their high pollutant load. They are usually incinerated or used for low value purposes such as fertilizers. This review focuses on the trends of application of keratin recovered from animal by-products. Biomaterials for regenerative medicine, cosmetic formulations, and biodegradable food packaging can be obtained as a result of keratin self-assembly. Several peptide sequences released by hydrolysis as bioactive peptides should be studied further for their in vivo antihypertensive, and antidiabetic effects, as well as functional ingredients in foods. K E Y W O R D Sbioactive peptides, functional properties, keratin hydrolysates, keratin isolates

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RS - SR + true[normalO true] \to R - {SO}_{2} H + R - {SO}_{3} H

…”

Section: Solubilization Of Keratinsmentioning

confidence: 99%

Solubilization of keratins and functional properties of their isolates and hydrolysates

2018

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“…9 There are several procedures available to dissolve feather keratin. For example, acid and alkali hydrolysis, 10 the reduction of disulfide bonds with alkaline sodium sulfide solutions, a combination of enzymatic and chemical treatment, 11 the use of ammonium copper hydroxide, 12 and the oxidation of disulfide bonds with performic acid. 13 These dissolution methods are in addition to peptide bond scission.…”

Section: Introductionmentioning

confidence: 99%

Study on effective extraction of chicken feather keratins and their films for controlling drug release

Yin

et al. 2013

Biomater. Sci.

129

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“…Several procedures are described in the literature to dissolve feather keratins. Solubilization methods with concomitant peptide bond scission include acid and alkali hydrolysis (Nagai and Nishikawa, 1970a), reduction of disulfide bonds with alkaline sodium sulfide solutions (Van Ingen et al, 1998), a combination of enzymatic and chemical treatment (Dalev, 1994;Virkki et al, 1995), and the use of ammonium copper hydroxide (Nagai and Nishikawa, 1970c;1970b). Procedures without significant peptide bond scission in which only disulfide bonds are split include sulfitolysis or oxidation of disulfide bonds with performic acid (Woodin, 1954;1956;Harrap and Woods, 1964a;1964b).…”

Section: Introductionmentioning

confidence: 99%

Partially Carboxymethylated Feather Keratins. 1. Properties in Aqueous Systems

Schrooyen

Dijkstra

Oberthür

et al. 2000

J. Agric. Food Chem.

129

105

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Feather keratins were extracted from chicken feathers with an aqueous solution of urea and 2-mercaptoethanol. The keratin solution obtained was dialyzed to remove the reagents. Upon dialysis, extensive protein aggregation occurred. To obtain stable solutions or dispersions in water, cysteine residues were modified prior to dialysis with iodoacetamide, iodoacetic acid, or bromosuccinic acid, thereby blocking free thiol groups and introducing hydrophilic groups. For the development of biodegradable materials with good mechanical properties from these biopolymers, disulfide bonds between the keratin molecules are needed. Therefore, cysteine residues were only partially modified by using different reagent/cysteine molar ratios. The reaction rate constants of iodoacetate with glutathione and 2-mercaptoethanol were successfully used to predict the degree of modification of keratin cysteine. It was shown that, for carboxymethylated keratin, fewer aggregates were formed for higher degrees of cysteine modification, while more protein was present as oligomers. Aggregates and oligomers were stabilized through intermolecular disulfide bonds.

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Solubilization of Chicken Feather Keratin by Ammonium Copper Hydroxide (Schweitzer's Reagent)

Cited by 5 publications

References 2 publications

Solubilization of keratins and functional properties of their isolates and hydrolysates

Solubilization of keratins and functional properties of their isolates and hydrolysates

Study on effective extraction of chicken feather keratins and their films for controlling drug release

Partially Carboxymethylated Feather Keratins. 1. Properties in Aqueous Systems

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