Enhanced Enzyme Activity with Ferritin Nanocages

Year 2018, , 115 - 118, 29.06.2018

Eylem Turan

https://doi.org/10.17350/HJSE19030000081

Cited By: 1

Abstract

I n this study, a novel enzyme system based on ferritin nanocages was designed. α-Amylase was covalently crosslinked on surface of ferritin nanocages by EDC/NHS. The activity of immobilized enzyme was monitored by using UV-vis spectrophotometer. The optimum temperature of immobilized enzyme shifted from 50 oC to 70 oC due to the ferritin nanocages. In addition, The Km and Vmax values of immobilized enzymes were 5.19 mg mL-1 and 3.3x10-5 U mg-1, respectively. This novel enzyme system displayed higher catalytic activity and enhanced stability

Keywords

Ferritin nanocages, α-amylase, Enzyme immobilization, EDC/NHS, Covalently crosslinked

References

• 1. Bou-Abdallah F, Zhao G, Biasiotto G, Poli M, Arosio P, Chasteen ND, Facilitated diffusion of iron(II) and dioxygen substrates into human H-chain ferritin. A flourrescence and absorbance study employing the ferroxidase center substitution Y34W. JACS, 130 (2008) 17801-17811.
• 2. Bulvik BE, Berenshtein E, Meyron-Holtz EG, Konijn AM, Chevion M, Cardiac protection by preconditioning is generated via an iron-signal creatd by proteasomal degradation of iron proteins. PLoS ONE, 7 (2012), 1-9.
• 3. Ullrich A, Horn S, Structural investigations on differently sized monodisperse iron oxide nanoparticles synthesized by remineralization of apoferritin molecules. J. Nanopart. Res. 15 (2013), 1-9.
• 4. Zhen ZP, Tang W, Guo CL, Ferritin nanocages to encapsulate and deliver photosensitizers for efficient photodynamic therapy against cancer. ACS Nano, 7 (2013) 6988-6996.
• 5. Tang Z, Wu H, Zhang Y, Li Z, Lin Y, Enzyme-Mimic Activity of Ferric Nano-Core Residing in Ferritin and Its Biosensing Applications. Anal. Chem. 83 (2011) 8611-8616.
• 6. Tedesco AC, Oliviera DM, Lacava ZGM, Azevedo RB, Lima ECD, Morais PC, Investigation of the binding constant and stoichiometry of biocompatible cobalt ferrite-based magnetic fluids to serum albümin. Journal of Magnetism and Magnetic Materials. 272–276 (2004) 2404–2405.
• 7. Powell JJ, Bruggraber SFA, Faria N, Poots LK, Hondow N, Pennycook TJ, Latunde-Dada GO, Simpson RJ, Brown AP, Pereira DIA, A nano-disperse ferritin-core mimetic that efficiently corrects anemia without luminal iron redox activity. Nanomedicine: Nanotechnology, Biology, and Medicine 10 (2014) 1529-1538.
• 8. Rakshit T, Mukhopadhyay R, Tuning band gap of holoferritin by metal core reconstitution with Cu, Co and Mn. Langmuir 27 (2011) 9681-9686.
• 9. Zhao J, Liu ML, Zhang YY, Li HT, Lin YH, Yao SZ, Apoferritin protein nanoparticles dually labeled with aptamer and horseradish peroxidase as a sensing probe for thrombin detection. Anal. Chim. Acta 759 (2013) 53-60.
• 10. Soppimath KS, Aminabhavi TM, Kulkarni AR, Rudzinski WE, Biodegradable polymeric nanoparticles as drug delivery devices. J. Control. Release 70 (2001) 1-20.
• 11. Mundargi RC, Babu VR, Rangaswamy V, Patel P, Aminabhavi TM, Nano/micro Technologies for delivering macromolecular therapeutics using poly(D,L-lacticide-co-glycolide) and its derivatives. J. Control. Release 125 (2008) 193-209.
• 12. Chomoucka J, Drbohlavova J, Huska D, Adam V, Kizek R, Hubalek J, Magnetic nanoparticles and targeted drug delivering. Pharmacol. Res., 62 (2010) 144-149.
• 13. Tümtürk H, Yüksekdağ H, Acetylcholinesterase immobilized onto PEI-coated silica nanoparticles. Artifi cial Cells, Nanomedicine, and Biotechnology 44 (2016) 443-447.