Covalent immobilization of xylanase and lysing complex into polymer scaffolds with long-term activity retention / Ryan W. Baker-Branstetter in JOURNAL OF COATINGS TECHNOLOGY AND RESEARCH, Vol. 20, N° 3 (05/2023)  

[article]  inJOURNAL OF COATINGS TECHNOLOGY AND RESEARCH > Vol. 20, N° 3 (05/2023) . - p. 973-978 Titre : Covalent immobilization of xylanase and lysing complex into polymer scaffolds with long-term activity retention Type de document : texte imprimé Auteurs : Ryan W. Baker-Branstetter, Auteur ; Mairead E. Bartlett, Auteur ; Scott A. Shuler, Auteur ; Reid E. Messersmith, Auteur Année de publication : 2023 Article en page(s) : p. 973-978 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Chimie click Complexe de lyse Hydrolyse enzymatique Revêtements antisalissures Xylanase Index. décimale : 667.9 Revêtements et enduits Résumé : Existing antifouling coatings for marine environments rely on the toxicity of copper and small-molecule additives to prevent organism growth. These come with a myriad of environmental and health-related risks, as these additives inevitably leach into seawater. Enzyme-based antifouling polymers have tremendous potential as part of an environmentally innocuous antifouling strategy, but have not yet been commercially realized. Biofouling begins with small molecules and polymers that initiate settlement for larger organisms. Using an enzymatic coating to rapidly hydrolyze these compounds could reduce the surface concentration of these attractive polymers and prevent organism growth. Here, antifouling xylanase and lysing complex enzymes were covalently tethered to surfaces using isoindolinone groups and click chemistry. We found that xylanase and lysing complex continue to hydrolyze xylosidic bonds in hemicellulose polysaccharides after covalent tethering, and the coating maintained activities of >  80% and  >  50%, respectively, after 2 months while submerged in artificial seawater, demonstrating this material’s potential as an eco-friendly antifouling coating. Note de contenu : - General - Alkyne-Azide mixture - OPA linker solution - Enzyme assays DOI : https://doi.org/10.1007/s11998-022-00717-8 En ligne : https://link.springer.com/content/pdf/10.1007/s11998-022-00717-8.pdf?pdf=button% [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=39441 [article]

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