Evaluation of Various Magnetic Ferrite Nanoparticles for Methionine γ-Lyase (MGL) Immobilization: Enhanced Stability and Catalytic Performance of Nanoenzyme Carriers

High Resolution Image Download MS PowerPoint Slide Methionine γ-lyase (MGL), a methionine-starvation enzyme, has garnered significant attention for its potential applications in targeting methionine-dependent cancer cells. Here, we report the successful immobilization of His-tagged MGL onto magnetic ferrite nanoparticles (MF MNPs) supports functionalized with modified Nα, Nα-bis(carboxymethyl)- l -lysine (Ni-mANTA), exploiting both the magnetic core and surface complexation to enhance MGL’s stability and catalytic performance. Ferrite support cores containing Ni 2+, Fe 2+, Co 2+, and Zr 4+ were synthesized and characterized using XRD, VSM, BET, EDS, ICP-OES, FTIR, XPS, TGA, and DLS analysis and then for MGL immobilization (MGL@Ni-mANTA/MF MNPs). Among the prepared systems, Ni-mANTA/NiF MNPs demonstrated the highest adsorption capacity (11,800 mg g –1 ) and retained at least 65% of their activity after 15 days at 4 °C, while exhibiting thermal stability up to 55 °C with pH 7–8 and remarkable recyclability across ten reuse cycles. The XPS spectra revealed the existence of Ni 2+ –N bonds, thereby providing a robust interaction of the His-tagged molecules following immobilization. Moreover, DFT calculations demonstrated that the support Ni-mANTA/NiF MNPs exhibit a dual surface affinity. This significantly enhances their binding to the His-tagged MGL compared to NiF MNPs alone, attributed to the improved stability and performance of MGL. This study offers a foundation for developing stable nanoenzyme carriers. These findings highlight the potential of tailored MNPs to advance the development of robust enzymatic systems for therapeutic applications of MGL. The findings provide a foundation for MGL@Ni-mANTA/MFs’ further therapeutic potential in biological conditions.