Asparaginase immobilized, magnetically guided, and bubble-propelled micromotors. (September 2021)

• Record Type: Journal Article
• Authors: Evli, Sinem; Öndeş, Baha; Uygun, Murat; Uygun, Deniz Aktaş
• Is Part Of: Process biochemistry. Volume 108(2021)
• Page Start: 103
• Page End: 109
• Publication Date: 2021-09
• Subjects: l-asparaginase -- Micromotors -- Leukemia -- Immobilization; Biochemical engineering -- Periodicals; Biotechnology -- Periodicals; Biochemistry -- periodicals; Biotechnology -- periodicals; Chemical Engineering -- periodicals; Génie biochimique -- Périodiques; Biotechnologie -- Périodiques; Biochemical engineering; Biotechnology; Periodicals; 660.63
• DOI: 10.1016/j.procbio.2021.06.009
• Languages: English
• ISSNs: 1359-5113

Abstract

Graphical abstract: Expected Route for the efficient leukemia treatment concept by using self-propelled magnetic guided L-asparaginase immobilized micromotors, which degrade the vital amino acid L-asparagine for cancer cell growth. Highlights: L-asparaginase immobilized micro motors are used as an anti-leukemic drug concept. Pt layer produced O2 bubbles by the decomposition of H2 O2 to move the motors. Ni segment enables remote control of the motors. Improved and efficient activities were captured by immobilization onto the micromotor. Abstract: In this study, tubular poly(3, 4-ethylene dioxythiophene)-polypyrrole/Ni/ Pt (PEDOT-PPy-COOH/Ni/Pt) micromotors were prepared and modified with L-asparaginase, which is an anti-leukemic drug. Inner Pt layer of the micromotor decomposes H2 O2 to produce O2 and allows the motor for self-propulsion, while the Ni segment enables remote control of the motors via a magnetic field. These tiny motors have self-propulsion capability and can be easily controlled by an external magnetic field. By immobilizing asparaginase, these enzyme-carrying motors demonstrated improved activity for the L-asparagine hydrolysis. At the end of the immobilization process, the enzyme showed improved thermal and pH stability, ascending protease resistance, longer storage time, and reusability. Kinetic parameters of free and immobilized asparaginase were also evaluated. It was shown that affinity for asparaginase towards its substrate did not change significantly upon immobilization. Besides Vmax value of immobilized L-asparaginase was found to be higher than that of free enzyme. Stability against protease trypsin was also tested and it was demonstrated that immobilized L-asparaginase was more stable for trypsin than free L-asparaginase. Finally, artificial serum experiments were also constructed to show the possible in vivo usage, and it was realized that L-asparaginase immobilized micromotor exhibited higher activity than free enzyme and control static micromotor experiments.