Production and Characterization of Human Hair Keratin Bioplastic Films With Novel Plasticizers

January 2024 in “ Scientific reports (Nature Publishing Group) ”

A. Shubha, Gupta Sharmita, Lakhani Anita

keratin bioplastic films ethanediol di-ethylene glycol tri-ethylene glycol glycerol keratinophilic fungal strain A. oryzae X-ray FTIR ethylene glycol glycerin

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Keratin →

Glycerin →

Studysummary This study explored using keratin extracted from human hair waste to create biodegradable bioplastic films, revealing promising potential for applications in packaging and disposable items due to their uniform surface morphology and ability to degrade with keratinophilic fungi.

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The study used keratin from human hair waste to create bioplastic films, or 'kertics', with the help of novel plasticizers such as ethanediol, di-ethylene glycol, tri-ethylene glycol, and glycerol. The films were 190-220 µm thick, had an area of about 4.54 ± 0.2 cm2, and their water uptake varied between 4.8% and 6.3%. X-ray and FTIR studies confirmed the presence of non-degraded keratin. The films were found to be biodegradable in studies involving a keratinophilic fungal strain of A. oryzae. The study suggests these films could be used in the packaging industry, disposable items manufacturing, and biomaterial generation.

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Research cited in this study

4 / 4 results

research Development of a Mechanically Stable Human Hair Keratin Film for Cell Culture

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research Unique Amino Acid Signatures That Are Evolutionarily Conserved Distinguish Simple-Type, Epidermal, and Hair Keratins

76 citations , December 2011 in “Journal of Cell Science”

This study found that keratins have evolutionarily conserved and domain-selectively enriched amino acids, which likely reflect their unique structural roles, with distinct patterns observed among epidermal, hair, and simple-type epithelial keratins.

research Mechanical and Biological Properties of Keratose Biomaterials

140 citations , August 2011 in “Biomaterials”

This study observed that keratose, derived from human hair, integrated well in mouse tissue and remodeled with collagen, suggesting potential as a non-toxic biomaterial for regenerative applications.

research A Rapid Extraction Procedure of Human Hair Proteins and Identification of Phosphorylated Species

226 citations , January 2002 in “Biological and Pharmaceutical Bulletin”

This study developed a rapid method to extract proteins from human hair, revealing phosphorylation on serine and threonine residues in alpha-keratins and matrix proteins.