2026-04-28T17:10:57Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/48672024-07-24T11:39:50Zcom_10259_9476com_10259.4_106com_10259_2604com_10259_3596com_10259_5086col_10259_9477col_10259_3597

Antón Millán, Noemí 28 600 García Tojal, Javier 221 500 0000-0003-3816-0483 Marty Roda, Marta 350 500 0000-0002-5440-1454 Garroni, Sebastiano 227 500 0000-0001-7686-6589 Cuesta López, Santiago 133 500 0000-0002-7401-3889 Tamayo Ramos, Juan Antonio 547 500 0000-0002-7071-002X 2018-07-25T11:12:12Z 2019-06-01T02:45:06Z 2018-05 1944-8244 http://hdl.handle.net/10259/4867 10.1021/acsami.7b18844 The modification of carbon nanomaterials with biological molecules paves the way toward their use in biomedical and biotechnological applications, such as next-generation biocatalytic processes, development of biosensors, implantable electronic devices, or drug delivery. In this study, different commercial graphene derivatives, namely, monolayer graphene oxide (GO), graphene oxide nanocolloids (GOCs), and polycarboxylate-functionalized graphene nanoplatelets (GNs), were compared as biomolecule carrier matrices. Detailed spectroscopic analyses showed that GO and GOC were similar in composition and functional group content and very different from GN, whereas divergent morphological characteristics were observed for each nanomaterial through microscopy analyses. The commercial α-l-rhamnosidase RhaB1 from the probiotic bacterium Lactobacillus plantarum, selected as a model biomolecule for its relevant role in the pharma and food industries, was directly immobilized on the different materials. The binding efficiency and biochemical properties of RhaB1–GO, RhaB1–GOC, and RhaB1–GN composites were analyzed. RhaB1–GO and RhaB1–GOC showed high binding efficiency, whereas the enzyme loading on GN, not tested in previous enzyme immobilization studies, was low. The enzyme showed contrasting changes when immobilized on the different material supports. The effect of pH on the activity of the three RhaB1-immobilized versions was similar to that observed for the free enzyme, whereas the activity–temperature profiles and the response to the presence of inhibitors varied significantly between the RhaB1 versions. In addition, the apparent Km for the immobilized and soluble enzymes did not change. Finally, the free RhaB1 and the immobilized enzyme in GOC showed the best storage and reutilization stability, keeping most of their initial activity after 8 weeks of storage at 4 °C and 10 reutilization cycles, respectively. This study shows, for the first time, that distinct commercial graphene derivatives can influence differently the catalytic properties of an enzyme during its immobilization. European Union’s H2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No. 691095, Ministerio de Economiá y Competitividad (CTQ2016-75023-C2-1-P, CTQ2015-70371- REDT MetDrugs Network), and Junta de Castilla y Leon- FEDER grants BU076U16, BU079U16 and UBU-11-A. application/pdf eng American Chemical Society ACS Applied Materials & Interfaces. 2018, V. 10, n. 21, p. 18170–18182 https://doi.org/10.1021/acsami.7b18844 info:eu-repo/grantAgreement/EC/H2020/691095 info:eu-repo/grantAgreement/MINECO/CTQ2016-75023-C2-1-P info:eu-repo/grantAgreement/MINECO/CTQ2015-70371- REDT info:eu-repo/grantAgreement/JCyL/BU079U16 info:eu-repo/grantAgreement/JCyL/BU076U16 UBU-11-A ATR-FTIR biocatalysis graphene immobilization TEM α-l-rhamnosidase Química inorgánica Materiales Chemistry, Inorganic Materials Influence of three commercial graphene derivatives on the catalytic properties of a lactobacillus plantarum α-l-Rhamnosidase when used as immobilization matrices info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion info:eu-repo/semantics/openAccess THUMBNAIL Anton-AMI_2018.pdf.jpg Anton-AMI_2018.pdf.jpg IM Thumbnail image/jpeg 3875 https://riubu.ubu.es/bitstream/10259/4867/4/Anton-AMI_2018.pdf.jpg 81ac4ef2952a76db72656880ab2e30bc MD5 4 ORIGINAL Anton-AMI_2018.pdf Anton-AMI_2018.pdf application/pdf 6118446 https://riubu.ubu.es/bitstream/10259/4867/1/Anton-AMI_2018.pdf be4f8073c9087eb1c920e028f567b947 MD5 1 LICENSE license.txt license.txt text/plain; charset=utf-8 998 https://riubu.ubu.es/bitstream/10259/4867/2/license.txt aa90105e1c90a1b4fe810649aa967b7d MD5 2 TEXT Anton-AMI_2018.pdf.txt Anton-AMI_2018.pdf.txt Extracted text text/plain 76854 https://riubu.ubu.es/bitstream/10259/4867/3/Anton-AMI_2018.pdf.txt bede057f677621eacb924bc32feb99c7 MD5 3 10259/4867 oai:riubu.ubu.es:10259/4867 2024-07-24 13:39:50.912 Repositorio Institucional de la Universidad de Burgos bubrep@ubu.es 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