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Enzyme immobilization onto the nanomaterials: Application in enzyme stability and prodrug-activated cancer therapy

Nanoparticles (NPs) have been widely used for immobilization of wide ranges of enzymes. However, the stabilization of enzymes on NPs is a major challenge, crucial for regulating enzymatic activity and their medical applications. To overcome these challenges, it is necessary to explore how enzymes at...

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Bibliographic Details
Published in:International journal of biological macromolecules 2020-01, Vol.143, p.665-676
Main Authors: Sharifi, Majid, Sohrabi, Mohammad Javad, Hosseinali, Sara Haji, Hasan, Anwarul, Kani, Pegah Hashemi, Talaei, Amir Jouya, Karim, Abdulkarim Yasin, Nanakali, Nadir Mustafa Qadir, Salihi, Abbas, Aziz, Falah Mohammad, Yan, Bing, Khan, Rizwan Hassan, Saboury, Ali Akbar, Falahati, Mojtaba
Format: Article
Language:English
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Summary:Nanoparticles (NPs) have been widely used for immobilization of wide ranges of enzymes. However, the stabilization of enzymes on NPs is a major challenge, crucial for regulating enzymatic activity and their medical applications. To overcome these challenges, it is necessary to explore how enzymes attach to nanomaterials and their properties are affected by such interactions. In this review we present an overview on the different strategies of the enzyme immobilization into the NPs and their corresponding stability against temperature and pH. The effects of surface charge, particle size, morphology, and aggregation of NPs on the stability of immobilized enzymes were summarized. The activity of immobilized enzyme into the NPs was reviewed to disclose more detail regarding the interaction of biomolecules with NPs. The combination of enzyme immobilization with prodrugs was also reviewed as a promising approach for biomedical application of enzyme in cancer therapy. Finally, the current challenges and future applications of NPs in enzyme immobilization and the utilization of immobilized enzyme toward prodrug activation in cytoplasm of cancer cells were presented. In conclusion, this review may pave the way for providing a perspective on development to the industrial and clinical translation of immobilized enzymes.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2019.12.064