Artykuł w czasopiśmie
Brak miniatury
Licencja

CC-BYCC-BY - Uznanie autorstwa
 

Ceruloplasmin in flatland: the relationship between enzyme catalytic activity and surface hydrophilicity

cris.lastimport.scopus2024-02-12T19:10:09Z
dc.abstract.enThe effective immobilization of the enzyme on the substrate surface plays a key role especially in biocatalysis, medicine or industry. Herein, we showed the influence of substrate hydrophilicity on the activity of the physically immobilized ceruloplasmin. To control the hydrophilicity of the substrate, thiols with various terminal groups were used. We have found that the effectiveness of the catalytic process of multimeric protein is the highest in the situation of application of the highly hydrophilic substrate. In the case of physical adsorption, the orientation of the enzyme is random, however the application of the appropriate modifying layer enforces the desired enzyme orientation. The quartz crystal microbalance with dissipation (QCM-D) results showed that the crucial parameter for the highest and most durable catalytic activity of the enzyme is the orientation, not the amount of the physically adsorbed enzyme.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorNowicka, Anna
dc.contributor.authorYu, Cong
dc.contributor.authorKowalczyk, Agata
dc.date.accessioned2024-01-24T19:05:17Z
dc.date.available2024-01-24T19:05:17Z
dc.date.copyright2022-09-06
dc.date.issued2022
dc.description.accesstimeAT_PUBLICATION
dc.description.financeŚrodki finansowe, o których mowa w art. 365 pkt. 2 ustawy
dc.description.number39
dc.description.versionFINAL_PUBLISHED
dc.description.volume12
dc.identifier.doi10.1039/D2RA04159F
dc.identifier.issn2046-2069
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/102820
dc.identifier.weblinkhttp://pubs.rsc.org/en/content/articlepdf/2022/RA/D2RA04159F
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofRSC Advances
dc.relation.pages25388-25396
dc.rightsCC-BY
dc.sciencecloudnosend
dc.titleCeruloplasmin in flatland: the relationship between enzyme catalytic activity and surface hydrophilicity
dc.typeJournalArticle
dspace.entity.typePublication