Interaction of Dehydrogenase Enzymes with Nanoparticles in Industrial and Medical Applications, and the Associated Challenges: A Mini-review

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 NP-protein 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.

Automated summary

Nanoparticles are crucial for interactions with dehydrogenase enzymes, facilitating applications in biocatalysis and nanomedicine. The characteristics of NP-enzyme complexes are influenced by the chemistry of NP ligands, NP size, and labeling methods, impacting enzymatic activity.