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Review Article

Multi-point enzyme immobilization, surface chemistry, and novel platforms: a paradigm shift in biocatalyst design

ORCID Icon, , , & ORCID Icon
Pages 202-219 | Received 29 Apr 2018, Accepted 06 Sep 2018, Published online: 04 Nov 2018
 

Abstract

Engineering enzymes with improved catalytic properties in non-natural environments have been concerned with their diverse industrial and biotechnological applications. Immobilization represents a promising but straightforward route, and immobilized biocatalysts often display higher activities and stabilities compared to free enzymes. Owing to their unique physicochemical characteristics, including the high-specific surface area, exceptional chemical, electrical, and mechanical properties, efficient enzyme loading, and multivalent functionalization, nano-based materials are postulated as suitable carriers for biomolecules or enzyme immobilization. Enzymes immobilized on nanomaterial-based supports are more robust, stable, and recoverable than their pristine counterparts, and are even used for continuous catalytic processes. Furthermore, the unique intrinsic properties of nanomaterials, particularly nanoparticles, also confer the immobilized enzymes to be used for their broader applications. Herein, an effort has been made to present novel potentialities of multi-point enzyme immobilization in the current biotechnological sector. Various nano-based platforms for enzyme/biomolecule immobilization are discussed in the second part of the review. In summary, recent developments in the use of nanomaterials as new carriers to construct robust nano-biocatalytic systems are reviewed, and future trends are pointed out in this article.

Acknowledgements

This work was financially supported by the National Natural Science Foundation of China [No. 21877078]. All authors are grateful to their representative institutes for providing literature facilities.

Disclosure statement

We do not have any conflicting, competing, and financial interests in any capacity.

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