abstract
L-asparaginase is an enzyme with diverse and significant applications, such as reducing acrylamide formation in starchy food processing and as a biopharmaceutical for treating acute lymphoblastic leukaemia. However, the free enzyme is susceptible to external factors, leading to reduced stability compared to its immobilized forms. Lasparaginase was adsorbed onto both amine- and oxygen-terminated boron-doped diamond surfaces under controlled conditions (pH 8, 37 degrees C, 0.06 mg/mL ASNase, and 1 h immobilization on 5 x 5 mm boron-doped diamond surfaces). Boron-doped diamond surfaces were grown from hot-filament chemical vapor deposition. The results show a successful enzyme immobilization, with the amine- and oxygen-terminated surfaces exhibiting an enhanced immobilization yield of up to 68 %, compared to just 17 % on untreated as-grown boron-doped diamond. Notably, amine-terminated boron-doped diamond surface maintained 54 % of its initial relative activity after three cycles of reaction, outperforming other diamond surfaces. This work demonstrates the potential of boron-doped diamond surfaces for immobilizing and reuse of L-asparaginase through simple adsorption, which could be valuable for future biosensing applications.
keywords
SURFACE TERMINATION; CVD DIAMOND; CARBON; FUNCTIONALIZATION; ELECTRODES; INTERFACE; BIOSENSOR; RAMAN
subject category
Chemistry; Materials Science; Physics
authors
Tavares, BL; Fernandes, DR; Rodrigues-Freitas, L; Nunes, JCF; Girao, A; Neves, MC; Fernandes, AJS; Santos-Ebinuma, VC; Neto, MAC; Tavares, APM
our authors
Ana Paula Mora Tavares
Assistant Professor
Ana Violeta Girão
Junior Researcher
Bernardo Loureiro Tavares
PhD Student
João C. F. Nunes
Research Fellowship
Márcia Carvalho Neves
Junior Researcher
Miguel Ângelo da Costa Neto
Principal ResearcherGroups
G3 - Electrochemical Materials, Interfaces and Coatings
G5 - Biomimetic, Biological and Living Materials
acknowledgements
Ana Tavares and Ma