Biocatalytic Self-Cleaning Polymer Membranes

dc.bibliographicCitation.firstPage1837eng
dc.bibliographicCitation.issue9eng
dc.bibliographicCitation.journalTitlePolymerseng
dc.bibliographicCitation.lastPage1849eng
dc.bibliographicCitation.volume7eng
dc.contributor.authorSchulze, Agnes
dc.contributor.authorStoelzer, Astrid
dc.contributor.authorStriegler, Karl
dc.contributor.authorStarke, Sandra
dc.contributor.authorPrager, Andrea
dc.date.accessioned2022-07-01T08:31:04Z
dc.date.available2022-07-01T08:31:04Z
dc.date.issued2015
dc.description.abstractPolymer membrane surfaces have been equipped with the digestive enzyme trypsin. Enzyme immobilization was performed by electron beam irradiation in aqueous media within a one-step method. Using this method, trypsin was covalently and side-unspecific attached to the membrane surface. Thus, the use of preceding polymer functionalization and the use of toxic solvents or reagents can be avoided. The resulting membranes showed significantly improved antifouling properties as demonstrated by repeated filtration of protein solutions. Furthermore, the biocatalytic membrane can be simply “switched on” to actively degrade a fouling layer on the membrane surface and regain the initial permeability. The membrane pore structure (pore size and porosity) was neither damaged by the electron beam treatment nor blocked by the enzyme loading, ensuring a stable membrane performance.eng
dc.description.versionpublishedVersioneng
dc.identifier.urihttps://oa.tib.eu/renate/handle/123456789/9474
dc.identifier.urihttps://doi.org/10.34657/8512
dc.language.isoengeng
dc.publisherBasel : MDPIeng
dc.relation.doihttps://doi.org/10.3390/polym7091485
dc.relation.essn2073-4360
dc.rights.licenseCC BY 4.0 Unportedeng
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/eng
dc.subject.ddc540eng
dc.subject.otherEnzyme immobilizationeng
dc.subject.otherFouling reductioneng
dc.subject.otherSelf-cleaningeng
dc.subject.otherSurface modificationeng
dc.titleBiocatalytic Self-Cleaning Polymer Membraneseng
dc.typeArticleeng
dc.typeTexteng
tib.accessRightsopenAccesseng
wgl.contributorIOMeng
wgl.subjectChemieeng
wgl.typeZeitschriftenartikeleng
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