Immobilization of l-asparaginase on aspartic acid functionalized graphene oxide nanosheet: Enzyme kinetics and stability studies
作者： Maryam Monajati , Sedigheh Borandeh , Anahita Hesami , Dorsa Mansouri , Ali Mohammad Tamaddon
DOI: 10.1016/J.CEJ.2018.08.058
关键词: Aspartic acid 、 Enzyme kinetics 、 Asparaginase 、 Nuclear chemistry 、 Nanosheet 、 Immobilized enzyme 、 Enzyme assay 、 Enzyme 、 Chemistry 、 Covalent bond
摘要: Abstract There is an increasing interest in using l -asparaginase medical fields and food processing industries. Enzyme immobilization attractive field to improve activity stability. Graphene oxide (GO) a promising candidate for enzyme due its large specific surface area. In this study, GO was first functionalized with -aspartic acid (GO-Asp), then immobilized on the GO-Asp either physically or through chemical conjugation. A significant loading achieved covalent (100% efficiency). Stability of free examined at various temperatures (20–60 °C) pH (5–9). The covalently showed higher than 8 maximum recovered 100%, 90.5% 40.6% after 24 h incubation 20 °C, 40 °C 60 °C, respectively. addition, 42% eight continuous reaction cycles 60 °C. kinetic parameters were also calculated, indicating no changes affinity results clearly reflect suitability as nanosheet support well usage future industrial applications.
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