Structural analysis of enzymes used for bioindustry and bioremediation

Abstract

Microbial enzymes have been widely applied in the large-scale, bioindustrial manufacture of food products and pharmaceuticals due to their high substrate specificity and stereoselectivity, and their effectiveness under mild conditions with low environmental burden. At the same time, bioremedial techniques using microbial enzymes have been developed to solve the problem of industrial waste, particularly with respect to persistent chemicals and toxic substances. And finally, structural studies of these enzymes have revealed the mechanistic basis of enzymatic reactions, including the stereoselectivity and binding specificity of substrates and cofactors. The obtained structural insights are useful not only to deepen our understanding of enzymes with potential bioindustrial and/or bioremedial application, but also for the functional improvement of enzymes through rational protein engineering. This review shows the structural bases for various types of enzymatic reactions, including the substrate specificity accompanying cofactor-controlled and kinetic mechanisms.

Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications

“…Enzymes are complex proteins that are produced by living organisms to bring about the specific biochemical reactions that are necessary to develop and maintain life. Although enzymes are produced by living cells, they can also be extracted from organisms and used for industrial, pharmaceutical and biotechnological applications [ 1 , 2 , 3 ]. Compared to classical chemical catalysts, the use of enzymes offers various advantages, as they: (i) specifically direct the reaction course toward a predetermined product, thus reducing the risk of side reactions; (ii) work under mild conditions of temperature and pH; (iii) avoid the production of toxic end-products.…”

Converting the 3‐quinuclidinone reductase from Agrobacterium tumefaciens into the ethyl 4‐chloroacetoacetate reductase by site‐directed mutagenesis

“…Glu197 was located on the α‐helix of the small domain, and it was also on the pathway of the substrate to the active site. The carboxyl group of Glu197 could interact with the tertiary amino group of 3‐quinuclidinone through an ionic bond 20 . Thus, Glu197 may be the key residue to determine substrate specificity.…”

“…The carboxyl group of Glu197 could interact with the tertiary amino group of 3-quinuclidinone through an ionic bond. 20 Thus, Glu197 may be the key residue to determine substrate specificity. Glu197 was subjected to saturation mutations, and…”

Mini Review: Advances in 2-Haloacid Dehalogenases

“…These enzymes can be used to obtain chiral hydroxy acids and haloalkanoic acids with low molecular weights; these small organic acids generally act as intermediates for synthesizing agrochemicals, medicines, and other important chemicals (Leemans Martin et al, 2020;Gurushankara, 2021). Hence, 2-haloacid dehalogenases are promising and potentially highly valuable for their application in environmental remediation and chemical synthesis (Bommarius, 2015;Tanokura et al, 2015;Zhang et al, 2018); here, we discuss the main fields in which they could be applied.…”