RT info:eu-repo/semantics/article
T1 Influence of three commercial graphene derivatives on the catalytic properties of a lactobacillus plantarum α-l-Rhamnosidase when used as immobilization matrices
A1 Antón Millán, Noemí
A1 García Tojal, Javier
A1 Marty Roda, Marta
A1 Garroni, Sebastiano
A1 Cuesta López, Santiago
A1 Tamayo Ramos, Juan Antonio
K1 ATR-FTIR
K1 biocatalysis
K1 graphene
K1 immobilization
K1 TEM
K1 α-l-rhamnosidase
K1 Química inorgánica
K1 Chemistry, Inorganic
K1 Materiales
K1 Materials
AB 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.
PB American Chemical Society
SN 1944-8244
YR 2018
FD 2018-05
LK http://hdl.handle.net/10259/4867
UL http://hdl.handle.net/10259/4867
LA eng
NO European Union’s H2020research and innovation program under the Marie Skłodowska-Curie grant agreement No. 691095, Ministerio de Economiá yCompetitividad (CTQ2016-75023-C2-1-P, CTQ2015-70371-REDT MetDrugs Network), and Junta de Castilla y Leon-FEDER grants BU076U16, BU079U16 and UBU-11-A.
DS Repositorio Institucional de la Universidad de Burgos
RD 01-may-2024