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dc.date.accessioned 2023-11-08T14:20:34Z
dc.date.available 2023-11-08T14:20:34Z
dc.date.issued 2023-09-26
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/159933
dc.description.abstract The adsorption of the lipase B from Candida antarctica (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW),was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of rac-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g−1 was obtained, achieving productivity of 0.298 mmol min−1 mg−1 . Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications. en
dc.language en es
dc.subject Biocatálisis es
dc.subject Enzimas es
dc.subject Polietilentereftalato es
dc.subject Polipropileno es
dc.subject Bis(2-hidroxietil)tereftalato es
dc.subject Química verde es
dc.subject Profenos es
dc.title Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste en
dc.type Articulo es
sedici.identifier.other http://dx.doi.org/10.3390/catal13101324 es
sedici.identifier.issn 2073-4344 es
sedici.creator.person Llerena Suster, Carlos Rafael es
sedici.creator.person Fuentes, Cynthia Analía es
sedici.creator.person Sambeth, Jorge Enrique es
sedici.creator.person José, Carla es
sedici.subject.materias Química es
sedici.description.fulltext true es
mods.originInfo.place Centro de Investigación y Desarrollo en Ciencias Aplicadas es
mods.originInfo.place Centro de Investigación de Proteínas Vegetales es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution 4.0 International (CC BY 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Catalysts es
sedici.relation.journalVolumeAndIssue vol. 13, no. 10 es


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Creative Commons Attribution 4.0 International (CC BY 4.0) Excepto donde se diga explícitamente, este item se publica bajo la siguiente licencia Creative Commons Attribution 4.0 International (CC BY 4.0)