Thermal and structural characterization of poly(ethylene-oxide)/keratin blend films

Tonin, Claudio; Aluigi, Annalisa; Vineis, Claudia; Varesano, Alessio; Montarsolo, Alessio; Ferrero, Franco

doi:10.1007/s10973-006-7557-7

Cited by 114 publications

(66 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This method gives a keratin extraction yield about 30% of the total protein content of the original wool [17]. Table 1 shows the amino acid composition of keratin extracted from wool regenerated from water (KW) and from formic acid (KF), with respect to the amino acid composition of the original wool.…”

Section: Chemical Characterization Of Keratin Regenerated From Water mentioning

confidence: 99%

Study on the structure and properties of wool keratin regenerated from formic acid

Aluigi

Zoccola

Vineis

et al. 2007

International Journal of Biological Macromolecules

Self Cite

226

146

View full text Add to dashboard Cite

Section: Chemical Characterization Of Keratin Regenerated From Water mentioning

confidence: 99%

Study on the structure and properties of wool keratin regenerated from formic acid

Aluigi

Zoccola

Vineis

et al. 2007

International Journal of Biological Macromolecules

Self Cite

226

146

View full text Add to dashboard Cite

“…Reduction of keratin by 2-mercaptoethanol, dithiothreitol (DTT) or dithioerythritol, thioglycolic acid, glutathione, sulphites, and bisulphite generates free cysteine residues, and the resulting cysteine-containing derivatives are called ''kerateines'' [7,[15][16][17][18]. They are less polar and more stable in acidic and alkaline solutions than the oxidized derivatives, and they contain amino acid residues capable of re-crosslinking.…”

Section: Introductionmentioning

confidence: 99%

Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers

Sinkiewicz

Śliwińska

Staroszczyk

et al. 2016

Waste Biomass Valor

129

View full text Add to dashboard Cite

Huge amount of keratinous waste, especially birds' feathers, demands more value-added application instead of dumping. The present work reports the results of experiments aimed at preparing soluble keratin useful for novel bioproduct formation. The effect of thermo-chemical treatments with various reducing agents, i.e. 2-mercaptoethanol, dithiothreitol, sodium m-bisulphite, and sodium bisulphite, as well as sodium hydroxide, on the yield of keratin extracted from chicken feathers was determined. It was shown that after 2-h reduction with 2-mercaptoethanol and sodium bisulphite, the yield of soluble keratin was about equal and amounted to 84 and 82 %, respectively. The cheaper and harmless sodium bisulphite additionally decreased the extraction time to 1 h with the same yield. Moreover, treatment of the feathers with 2.5 % NaOH further improved the extraction effectiveness by increasing the yield up to 94 %. The results of the study demonstrate the viability of hydrolytic processes to obtain soluble keratin useful for biodegradable film formation for food application, that are harmless and more effective than solubilization by reduction of the disulphide bonds. Graphical Abstract

show abstract

“…Ultimately, the nature, strength of these interactions and knowledge of the degradation rates will help design of matrices for release of active compounds that are suitable for future biomedical applications [77]. Apart from natural biopolymers, the interaction between keratin and synthetic polymers has also been investigated [78,79] and Tonin et al explored the relationship between poly (ethylene oxide) (PEO) and keratin blended films in order to develop a keratin-based material with improved structural properties. Morphological, structural and thermal analyses of the keratin-PEO films revealed that keratin inhibits PEO crystallization and PEO interferes with the keratin self-assembly at appropriate level by inducing β-sheet secondary protein structure with high thermal stability.…”

Section: Keratin Filmsmentioning

confidence: 99%

“…Morphological, structural and thermal analyses of the keratin-PEO films revealed that keratin inhibits PEO crystallization and PEO interferes with the keratin self-assembly at appropriate level by inducing β-sheet secondary protein structure with high thermal stability. The improved structural properties of keratin-PEO blends helps in the development of keratin materials for their possible usage as scaffolds in cell growth wound dressings and drug delivery membranes [78,80]. Researchers have also investigated alternative fabrication techniques for creating keratin films with more suitable mechanical properties in addition to creating blended keratin systems with natural or synthetic polymers.…”

Section: Keratin Filmsmentioning

confidence: 99%

Untitled

2013

J Food Processing & Beverages

View full text Add to dashboard Cite

A great deal of environmental concerns, oil price hike, and rapid oil consumption with finite nature of oil reserves in addition to consumer demand is driving research into renewable, biodegradable, inexpensive, and abundantly available biopolymers in material chemistry. Poultry feathers consist of keratin protein with several amino acids especially cysteine as a major component. Keratin is an original raw material that has great potential to be used in the development of novel fibrous composite materials. Being very effective biopolymer, keratin possesses numerous functional properties, bioactivities, and chemical applications in material chemistry, for example, keratin based gels, films, nano/micro-particles, and beads are of paramount importance. Modified keratin also serves as a biosorbent for removing toxic metal ions from water resources on account of exceptionally important role of functional groups for keratin-metal binding. This review focuses on the recent advances of keratin in material chemistry including its significant role as biosorbent in green chemistry.

show abstract

Thermal and structural characterization of poly(ethylene-oxide)/keratin blend films

Cited by 114 publications

References 20 publications

Study on the structure and properties of wool keratin regenerated from formic acid

Study on the structure and properties of wool keratin regenerated from formic acid

Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers

Untitled

Contact Info

Product

Resources

About