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 bonds bet...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2023-04-01
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| Series: | Journal of Natural Fibers |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/15440478.2023.2187506 |
| _version_ | 1797674607530999808 |
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| author | Yu Li Jing Su Tarsila G. Castro Artur Cavaco-Paulo |
| author_facet | Yu Li Jing Su Tarsila G. Castro Artur Cavaco-Paulo |
| author_sort | Yu Li |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T22:02:31Z |
| format | Article |
| id | doaj.art-3970cee096034f94aed542c84b95a8dd |
| institution | Directory Open Access Journal |
| issn | 1544-0478 1544-046X |
| language | English |
| last_indexed | 2024-03-11T22:02:31Z |
| publishDate | 2023-04-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Natural Fibers |
| spelling | doaj.art-3970cee096034f94aed542c84b95a8dd2023-09-25T10:29:00ZengTaylor & Francis GroupJournal of Natural Fibers1544-04781544-046X2023-04-0120110.1080/15440478.2023.21875062187506Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model ProteinYu Li0Jing Su1Tarsila G. Castro2Artur Cavaco-Paulo3Jiangnan UniversityJiangnan UniversityUniversity of MinhoUniversity of MinhoCommercial 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.http://dx.doi.org/10.1080/15440478.2023.2187506hair curlingtyrosine graftinglaccasebsamolecular dynamics |
| spellingShingle | Yu Li Jing Su Tarsila G. Castro Artur Cavaco-Paulo Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein Journal of Natural Fibers hair curling tyrosine grafting laccase bsa molecular dynamics |
| title | Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein |
| title_full | Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein |
| title_fullStr | Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein |
| title_full_unstemmed | Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein |
| title_short | Mechanism of Hair Curling via Laccase-Assisted Tyrosine Grafting Using BSA as a Model Protein |
| title_sort | mechanism of hair curling via laccase assisted tyrosine grafting using bsa as a model protein |
| topic | hair curling tyrosine grafting laccase bsa molecular dynamics |
| url | http://dx.doi.org/10.1080/15440478.2023.2187506 |
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