Title:Interaction of Dehydrogenase Enzymes with Nanoparticles in Industrial and Medical Applications, and the Associated Challenges: A Mini-review
Volume: 21
Issue: 11
Author(s): Samaneh J. Porzani, Adriana S. Lorenzi, Masoumeh Eghtedari and Bahareh Nowruzi*
Affiliation:
- Department of Biology, Science and Research Branch, Islamic Azad University, Tehran,Iran
Keywords:
Dehydrogenase enzymes, Protein-ligand interaction, Immobilization, Magnetic nanoparticles, Quantum dots,
Nanotechnology, Biosensors.
Abstract:
Background: Nanoparticles (NPs) are a group of particles with at least one dimension
ranging from 1 nm to 100 nm in diameter and a surrounding interfacial layer. The NP-protein interactions
include covalent and non-covalent bonds. Several dehydrogenase enzymes (e.g., alcohol dehydrogenase,
lactate dehydrogenase, alanine dehydrogenase, glutamate dehydrogenase, leucine dehydrogenase,
phenylalanine dehydrogenase, and malate dehydrogenase) are used for immobilization by
NPs. Also, magnetic NPs and quantum dots are promising model systems for the design of bioanalytical
sensors and biological enzyme assemblies. In this overview, we aimed to improve the current
knowledge of interactions between dehydrogenase enzymes and NPs and to introduce dehydrogenases
with industrial and medical applications. Also, bioconjugation of NPs with dehydrogenase enzymes
has broad applications in biocatalysis and nanomedicine in the field of drug discovery. However, studies
on the characterization of NP-enzyme complexes show that the anatomy and activity of enzymes
are dependent on the chemistry of NP ligands, NP size, and labeling methods. Moreover, the NPprotein
conjugates show increased/decreased enzymatic activities, depending on the NP features.
Conclusion: In this study, we reviewed the findings related to NP-enzyme interactions for nanotechnology
applications and conjugation techniques. We also highlighted several challenges associated
with the NP-enzyme interactions, including the stability and reusability of enzymes in NP-enzyme
formation.
