2024-03-29T14:50:37Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/48672023-03-31T12:31:46Zcom_10259_4759com_10259_2604com_10259_3596com_10259_5086col_10259_4760col_10259_3597
Influence of three commercial graphene derivatives on the catalytic properties of a lactobacillus plantarum α-l-Rhamnosidase when used as immobilization matrices
Antón Millán, Noemí
García Tojal, Javier
Marty Roda, Marta
Garroni, Sebastiano
Cuesta López, Santiago
Tamayo Ramos, Juan Antonio
ATR-FTIR
biocatalysis
graphene
immobilization
TEM
α-l-rhamnosidase
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.
2018-07-25
2019-06-01
2018-05
info:eu-repo/semantics/article
1944-8244
http://hdl.handle.net/10259/4867
10.1021/acsami.7b18844
eng
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
info:eu-repo/semantics/openAccess
American Chemical Society