Enzyme engineering: Reshaping the biocatalytic functions

Abstract

Enzyme engineering is a powerful tool to fine‐tune the enzymes. It is a technique by which the stability, activity, and specificity of the enzymes can be altered. The characteristic properties of an enzyme can be amended by immobilization and protein engineering. Among them, protein engineering is the most promising, as in addition to amending the stability and activity, it is the only way to modulate the specificity and stereoselectivity of enzymes. The current review sheds light on protein engineering and the approaches applied for it on the basis of the degree of knowledge of structure and function of enzymes. Enzymes, which have been engineered are also discussed in detail and categorized on the basis of their respective applications. This will give a better insight into the revolutionary changes brought by protein engineering of enzymes in various industrial and environmental processes.

Single‐Point Mutant Inverts the Stereoselectivity of a Carbonyl Reductase toward β‐Ketoesters with Enhanced Activity

“…Protein engineering is a powerful tool for creating enzymes with desired properties [7] . Numerous successful examples have been reported in the modification of enzyme stereoselectivity, [8] improvement of catalytic capability, [9] and expansion of the substrate spectrum [10] .…”

Flow biocatalysis 101: design, development and applications

“…Nowadays, the increasing number of protein libraries and in silico tools such as protein modelling and dynamic simulations is speeding up the optimization and development of process-specific biocatalysts. 21 Moreover, new computational tools that take advantage of bioinformatic analysis specifically for protein immobilization (i.e. CapiPy) 22 are opening new possibilities to apply semi-rational approaches to enhance the performance of immobilized biocatalysts.…”

Addressing the Selectivity of Enzyme Biosensors: Solutions and Perspectives

“…Protein engineering was recently used as an efficient tool for modifying the stability, activity, substrate specificity and stereoselectivity of enzymes based on site-directed mutagenesis (rational engineering), directed evolution and combined (semi-rational) approaches [ 89 , 90 ]. Using structure–function relationships of corroborated functional characteristics and crystallographic enzyme data, a rational engineering approach considers mutation of specific residues leading to altered kinetics for various substrates [ 91 ].…”