Publicação
Simple adsorption-based immobilization of l-asparaginase on boron-doped diamond film
| Resumo: | 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 ◦C, 0.06 mg/mL ASNase, and 1 h immobilization on 5 × 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 |
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| Autores principais: | Tavares, Bernardo L. |
| Outros Autores: | Fernandes, Diogo R.; Rodrigues-Freitas, Leandro; Nunes, João C.F.; Girão, Ana V.; Neves, Márcia C.; Fernandes, António J.S.; Santos-Ebinuma, Valéria C.; Neto, Miguel A.C.; Tavares, Ana P.M. |
| Assunto: | Boron-doped diamond HFCVD L-asparaginase Adsorption Immobilization |
| Ano: | 2025 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade de Aveiro |
| Idioma: | inglês |
| Origem: | RIA - Repositório Institucional da Universidade de Aveiro |
| Resumo: | 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 ◦C, 0.06 mg/mL ASNase, and 1 h immobilization on 5 × 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 |
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