Green and Sustainable Technology for High-Efficiency and Low-Damage Manipulation of Densely Crosslinked Proteins

Helan Xu, Kaili Song, Bingnan Mu, Yiqi Yang

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A two-step technology using nontoxic and eco-friendly chemicals is developed for the durable setting of densely/highly crosslinked proteins, such as wool and hair. Currently, most technologies for morphological modification are effective only for materials from non-highly-crosslinked proteins and cellulose. Before their morphological change, only water is needed to interrupt hydrogen bonds and ionic linkages, which stabilize the relative positions of molecules in non-highly-crosslinked proteins and cellulose. However, highly crosslinked proteins contain disulfide crosslinks, which are insusceptible to water. Thus, the controlled cleavage of disulfide bonds is required for creating new morphologies of highly crosslinked protein materials, such as hair and wool. Herein, cysteine and citric acid (CA) were used for the two-step setting of highly crosslinked proteins. This recipe showed better morphological change and less mechanical loss than commercial hair styling products. A reaction between CA and keratin was proposed, and verified via NMR and Raman spectra and titration. This technology could be a prospective alternative to achieve durable hair setting, anticrease finishing of wool textiles, and other durable morphological changes needed for highly crosslinked proteins.

Original languageEnglish (US)
Pages (from-to)1760-1768
Number of pages9
JournalACS Omega
Volume2
Issue number5
DOIs
StatePublished - May 31 2017

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Proteins
Wool
Citric acid
Citric Acid
Cellulose
Disulfides
Keratin
Water
Keratins
Titration
Cysteine
Raman scattering
Textiles
Hydrogen bonds
Nuclear magnetic resonance
Molecules

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Green and Sustainable Technology for High-Efficiency and Low-Damage Manipulation of Densely Crosslinked Proteins. / Xu, Helan; Song, Kaili; Mu, Bingnan; Yang, Yiqi.

In: ACS Omega, Vol. 2, No. 5, 31.05.2017, p. 1760-1768.

Research output: Contribution to journalArticle

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