In vitro effect on the proteolytic activity of papain with proteins of the skin as substrate / Thalles Canton Trevisol in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 44, N° 5 (10/2022)  

[article]  inINTERNATIONAL JOURNAL OF COSMETIC SCIENCE > Vol. 44, N° 5 (10/2022) . - p. 542-554 Titre : In vitro effect on the proteolytic activity of papain with proteins of the skin as substrate Type de document : document électronique Auteurs : Thalles Canton Trevisol, Auteur ; Rosana Oliveira Henriques, Auteur ; Karina Cesca, Auteur ; Ana Júlia Antunes Souza, Auteur ; Agenor Furigo, Auteur Année de publication : 2022 Article en page(s) : p. 542-554 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Biotechnologie Cosmétiques Formulation (génie chimique) -- Stabilité Papaïne La papaïne est une protéase à cystéine qui catalyse le clivage des liaisons peptidiques avec une spécificité assez faible, mais toutefois une préférence pour l'hydrolyse des sites ayant un résidu d'acide aminé portant une grande chaîne latérale hydrophobe en position P2 et pas de résidu de valine en position P1'. On trouve cette enzyme dans le latex de la papaye (Carica papaya). Elle est l'exemple-type de la famille des papaïnes dite famille C1, dont d'autres enzymes se retrouvent dans l'ananas et de très nombreux végétaux. (Wikipedia) Peau -- Anatomie Statistiques Index. décimale : 668.5 Parfums et cosmétiques Résumé : - Objective : This work aims to evaluate the effects of enzyme concentration, pH, temperature and time course degree of hydrolysis (DH) of papain regarding further development of pharmaceutical and cosmetic formulations. - Methods : The hydrolysis of casein, collagen, keratin and porcine skin at pH and temperature ranges of the human skin was evaluated. Also, low contact times of enzyme-substrate were studied. The incorporation of 3mM of cysteine improved the caseinolytic (PU), collagenolytic (CU) and keratinolytic (KU) activities of papain. - Results : In general, the increase from 0.1 to 1.0 or 2.0 mgmL−1 of papain improved PU, CU and KU. When 2.0 mgmL−1 of papain was used, the highest DH of casein, collagen and keratin was obtained at 240min (14%, 35% and 6% respectively). The decrease in pH and temperature reduced all proteolytic activities, but papain maintained at least 50% and 40% of its activity at 26°C and pH 4.5 respectively. Scanning electron micrographs of the surface of the skin showed that papain application had exfoliating activity. - Conclusion : This preformulation study demonstrated that papain concentration, time of application and pH of the product should be evaluated when developing a product to promote the hydrolysis of the proteins of the skin. Note de contenu : - MATERIALS AND METHODS : Materials - Caseinolytic activity assay - Effects of cysteine concentration during the reaction - Collagenolytic activity assay - Keratinolytic activity assay - Effects of cysteine and sodium sulphite in the keratinolytic activity - Determination of degree of hydrolysis (DH) - In vitro evaluation of the topical application of the enzyme on skin substrate - Statistical analysis - RESULTS AND DISCUSSION : Effect of cysteine concentration on caseinolytic activity of papain - Influence of papain concentration on caseinolytic activity and degree of hydrolysis of casein - Influence of papain concentration on collagenolytic activity and degree of hydrolysis of collagen - Influence of papain concentration on keratinolytic activity and degree of hydrolysis of keratin - Effect of pH on the proteolytic activity of papain with casein, collagen and keratin as substrates - Effect of temperature on the proteolytic activity of papain with casein, collagen and keratin as substrates - Visual aspect of the topical application of papain on skin substrate - - Table 1 : Effect of cysteine concentration on the caseinolytic activity of papain - Table 2 : Effect of papain concentration on the proteolytic activity of casein, collagen and keratin as substrates - Table 3 : Effect of the addition of reducing agents in the keratinolytic activity of papain DOI : https://doi.org/10.1111/ics.12805 En ligne : https://drive.google.com/file/d/1LJj2z8pLoZzpFna_tyQ9yNz8Zj4TPIaI/view?usp=shari [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=38152 [article]

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