Biotechnology of functional proteins and peptides for hair cosmetic formulations

Tinoco, Ana; Martins, Madalena; Cavaco-Paulo, Artur; Ribeiro, Artur

doi:10.1016/j.tibtech.2021.09.010

Cited by 21 publications

(18 citation statements)

References 37 publications

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“…However, human and animal-based products face ethical and health concerns, and their use is limited by regulations [ 62 ]. Due to this, proteins obtained from vegetable sources are highly appealing raw materials for the development of cost-effective and sustainable haircare formulations [ 63 ]. Plant-derived proteins, such as those derived from quinoa, jojoba, baobab, soy, or rice, can be used as conditioning agents in cosmetic formulations [ 5 ].…”

Section: Hair Conditionersmentioning

confidence: 99%

On Hair Care Physicochemistry: From Structure and Degradation to Novel Biobased Conditioning Agents

et al. 2023

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Hair is constantly exposed to various adverse external stimuli, such as mechanical or thermal factors, that may cause damage or cause it to lose its shine and smooth appearance. These undesirable effects can be minimized by using hair conditioners, which repair the hair and restore the smooth effect desired by the consumer. Some of the currently used conditioning agents present low biodegradability and high toxicity to aquatic organisms. Consumers are also becoming more aware of environmental issues and shifting their preferences toward natural-based products. Therefore, developing novel, sustainable, natural-based derivatives that can act as conditioning agents in hair care products and thus compete with the traditional systems obtained from non-renewable sources is highly appealing. This paper presents the key physicochemical aspects of the hair conditioning process, including hair structure and degradation, and reviews some of the new alternative conditioning agents obtained from natural resources.

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Section: Hair Conditionersmentioning

confidence: 99%

On Hair Care Physicochemistry: From Structure and Degradation to Novel Biobased Conditioning Agents

et al. 2023

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“…A large number of amino groups in chitosan and carboxyl groups in gelatin produced strong electrostatic interactions, which directly affected the viscosity of the antique ink. Additionally, the brush, which was made from animal hair, was also a protein and had a composition similar to that of the gelatin [22,23], which made it easy to produce physical bonds involving electrostatic interactions and hydrogen bonding between the ink and the brush upon addition of chitosan and collagen; these were firmly absorbed by the brush and enabled the brush to retain the ink.…”

Section: Analyses Of the Properties Of Gelatin Chitosan And Inksmentioning

confidence: 99%

Reproducing ancient Chinese ink depending on gelatin/chitosan and modern experimental methodology

Liu

2022

Herit Sci

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Chinese ink has very special significance for presentation of artistic effects and preservation of works of art; however, wasted nonrenewable resources, potential toxicity, and complex and inefficient production technologies have limited the development of inks for traditional Chinese culture. Herein, environmentally friendly, practical and antibacterial Chinese ink was prepared by facile heating-stirring of gelatin and the natural polysaccharide chitosan. The internal composition, viscosity, morphology, particle size and antibacterial properties of the ink were characterized by Fourier transform-infrared spectroscopy, X-ray photoelectron spectroscopy, scanning electron microscopy and bacteriostatic zone tests. The results showed that commercial ink (CM) spread easily on Xuan paper and led to imperfect artwork, while the chitosan and gelatin ink (CG) showed good adhesion and stability on Xuan paper. Based on this study, we believe that the good performance of CG ink should be attributed to restrictions arising from its internal chitosan and gelatin network, which restrict diffusion. Finally, the author used CG ink to display traditional Chinese calligraphy and landscape painting and believes that it has significant application prospects and will be used in large-scale production.

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“…Peptides are a class of biomolecules with established importance in industries including agriculture [ 1 ], pharmaceuticals [ 2 ], food [ 3 ], and cosmetics [ 4 ]. While many peptides can be produced using solid phase peptide synthesis [ 5 ], ribosomally synthesized peptides may be produced for research or industrial purposes using bacterial fermentation, as this method is relatively economical, green, and scalable [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

Simplified cloning and isolation of peptides from “sandwiched” SUMO-peptide-intein fusion proteins

Lamer

Vederas

2023

BMC Biotechnol

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Background Some peptides are targets for degradation when heterologously expressed as fusion proteins in E. coli, which can limit yields after isolation and purification. We recently reported that peptide degradation may be prevented by production of a “sandwiched” SUMO-peptide-intein (SPI) fusion protein, which protects the target peptide sequence from truncation and improves yield. This initial system required cloning with two commercially available vectors. It used an N-terminal polyhistidine tagged small ubiquitin-like modifier (SUMO) protein and a C-terminal engineered Mycobacterium xenopii DNA Gyrase A intein with an inserted chitin binding domain (CBD) to create “sandwiched” fusion proteins of the form: His6-SUMO-peptide-intein-CBD. However, the major drawback of this previously reported fusion protein “sandwich” approach is the increased time and number of steps required to complete the cloning and isolation procedures, relative to the simple procedures to produce recombinant peptides in E. coli from a single (non-“sandwiched”) fusion protein system. Results In this work we generate the plasmid pSPIH6, which improves upon the previous system by encoding both the SUMO and intein proteins and allows facile construction of a SPI protein in a single cloning step. Additionally, the Mxe GyrA intein encoded in pSPIH6 contains a C-terminal polyhistidine tag, resulting in SPI fusion proteins of the form: His6-SUMO-peptide-intein-CBD-His6. The dual polyhistidine tags greatly simplify isolation procedures compared to the original SPI system, which we have here demonstrated with two linear bacteriocin peptides: leucocin A and lactococcin A. The yields obtained for both peptides after purification were also improved compared to the previous SPI system as a result of this streamlined protocol. Conclusions This modified SPI system and its simplified cloning and purification procedures described here may be generally useful as a heterologous E. coli expression system to obtain pure peptides in high yield, especially when degradation of the target peptide is an issue.

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Biotechnology of functional proteins and peptides for hair cosmetic formulations

Cited by 21 publications

References 37 publications

On Hair Care Physicochemistry: From Structure and Degradation to Novel Biobased Conditioning Agents

On Hair Care Physicochemistry: From Structure and Degradation to Novel Biobased Conditioning Agents

Reproducing ancient Chinese ink depending on gelatin/chitosan and modern experimental methodology

Simplified cloning and isolation of peptides from “sandwiched” SUMO-peptide-intein fusion proteins

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