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5927429 
Journal Article 
Modifying bio-catalytic properties of enzymes for efficient biocatalysis: a review from immobilization strategies viewpoint 
Bilal, M; Zhao, Y; Noreen, S; Shah, SZH; Bharagava, RamN; Iqbal, HMN 
2019 
Yes 
Biocatalysis and Biotransformation
ISSN: 1024-2422 
37 
3 
159-182 
WOS:000463851800001 
Enzyme-based catalysis has become one of the most important disciplines in organic synthesis and plays a noteworthy role in the establishment of many chemical industries, e.g. fine chemicals, food or energy, textiles, agricultural, cosmeceutical, medicinal and pharmaceutical industries. However, pristine enzymes fail to demonstrate requisite functionalities for an industrial setting where extremely specific and stable catalysts are required. Immobilization enhances the catalytic stability and activity of enzymes and trims the overall cost burden of the enzyme. Therefore, it widely endeavours for proficient, sustainable, and environmentally responsive catalytic processes. Amongst several immobilization strategies, e.g. (1) supports-assisted, i.e. physical or covalent coupling and (2) supports-free techniques, i.e. cross-linked enzyme crystals (CLECs) or aggregates are the most promising ones and widely pursued for enzyme immobilization purposes. This perspective review focuses on up-to-date developments in the area of enzyme immobilization and presents their potentialities to upgrade and/or modify enzyme properties. Both types of immobilization strategies, i.e. supports-assisted and supports-free techniques are discussed with particular reference to CLECs or aggregates and protein-coated microcrystals. Also, several useful traits achieved after immobilization are also discussed in the second half of the review. 
Biocatalysis; enzyme immobilization; catalytic stability; cross-linked enzyme crystals or aggregates; protein-coated microcrystals; combi-protein-coated microcrystals