Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein

Commercial hair perming uses strong reducing agents and harms hair fiber's quality even human health. In this study, tyrosine is adopted as a cross-linking agent between thiols and/or amines as the shape-changing of hair involves the breakage of disulfide bonds and the rearrangement of new bond...

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Bibliographic Details
Published in:Journal of natural fibers Vol. 20; no. 1; pp. 1 - 12
Main Authors: Li, Yu, Su, Jing, G. Castro, Tarsila, Cavaco-Paulo, Artur
Format: Journal Article
Language:English
Published: Abingdon Taylor & Francis 24-04-2023
Taylor & Francis Ltd
Taylor & Francis Group
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Summary:Commercial hair perming uses strong reducing agents and harms hair fiber's quality even human health. In this study, tyrosine is adopted as a cross-linking agent between thiols and/or amines as the shape-changing of hair involves the breakage of disulfide bonds and the rearrangement of new bonds between keratin molecules. To investigate the mechanism of keratin cross-linking, bovine serum albumin (BSA) is used as a model protein. Disulfide bonds in BSA are successfully reduced by L-cysteine to provide free thiols. Four new cross-linked peptides are formed inter- or intra-BSA monomers, indicating that tyrosine can be adopted as a cross-linking agent not only between amines but also between thiols. Moreover, curling of Asian hair is conducted using tyrosine as a perming agent by the laccase-assisted reaction. The optimized operational conditions are hair with L-cysteine pre-treatment (50.0 mM) followed by laccase-assisted grafting with 3.0 mM tyrosine. The reshaped hair performed a better perming performance than commercial perming product before washing, although a lower perming efficiency after washing. The curling process could be accomplished without strength loss of hair fibers and with a blow-drier easily. Hence, this new methodology may lead to the development of a gentle and user-friendly approach in the hair care industry.
ISSN:1544-0478
1544-046X
DOI:10.1080/15440478.2023.2187506