Immobilization of L-Asparaginase on Magnetic Nanoparticles


Varan N. E., Yücebilgiç G.

4th Eurasia Biochemical Approaches & Technologies, Antalya, Turkey, 3 - 06 November 2022, pp.250, (Summary Text)

  • Publication Type: Conference Paper / Summary Text
  • City: Antalya
  • Country: Turkey
  • Page Numbers: pp.250
  • Çukurova University Affiliated: Yes

Abstract

L-asparaginase (L-ASNase, EC3.5.1.1) can specifically catalyze L-asparagine conversion to ammonia and L-aspartic acid. Due to its antineoplastic ability, L-asparaginase has been widely studied as a potential treatment for acute lymphoblastic leukemia and lymphosarcoma. 1 Although it has the potential to be widely used in the food and pharmaceutical industries, free L-asparaginases have some disadvantages, such as short half-life, low stability at high temperature, and lack of reusability. Enzyme immobilization is a widely used technique to eliminate the drawbacks of free enzymes in industrial applications. Fe3O4 nanoparticles are widely used supports in enzyme immobilization since they have a large surface area and are easily separated from reaction system by magnet.2 In this study, L-asparaginase was covalently immobilized on modified Fe3O4 nanoparticles. The optimum pH and temperature of free and immobilized L-asparaginase preparations were determined as 8.5 and 50 C for the both preparations. The thermal stability experiments showed that the thermal stability of immobilized L-asparaginase increased by 30 folds at 50 °C compared to the free enzyme. The immobilized L-asparaginase remained 80% of its initial activity after 10 reuses.