Immobilization of Geobacillus pallidus RAPc8 nitrile hydratase (NHase) reduces substrate inhibition and enhances thermostability

Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance

“…However, immobilization may be a solution for inhibition problems just by pure chance. For example, distortion of the enzymes produced by any immobilization strategy may lead to an increase on the K i to a larger extent that it affects the K m of the enzyme, and that way reduce the impact of inhibition on the reaction course 124. This has occurred using different beta‐galactosidases in the hydrolysis of high concentrations of lactose,125 where the yields using immobilized enzyme reached almost 100% hydrolysis of 5% lactose solutions while free enzyme almost stopped the reaction when less than 90% of lactose had been hydrolyzed.…”

Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

“…[35] For this goal, a simple enzyme adsorption of the protein on an ion exchanger matrix may be enough, using adequate conditions to guide the enzyme on the support surface. [11] Among the improved features of enzymes after immobilization, we can highlight the following: (i) increased enantiospecificity or regioselectivity (e.g., lipases [41] or penicillin G acylase [42] ); (ii) improved performance in kinetically controlled synthesis (e.g., penicillin G acylase [43] or bgalactosidase [44] ); (iii) reduced inhibition (e.g., b-galactosidase, [45] proteases, [46] or nitrilile hydrolases [47] ); (iv) lower chemical modification by reactive by-products (e.g., caused by hydrogen peroxide [48] ); and (v) improved enzyme reactivation. [5] Immobilization by multipoint covalent attachment has revealed itself as a very powerful tool to improve enzyme stability, in many cases by a factor of several hundreds or thousands, with very high activity recovery.…”

“…Besides increasing enzyme stability, immobilization can also greatly improve other enzyme properties, due to protein rigidification, change of the enzyme environment, blocking of some pockets or the structural distortion that it may produce 11. Among the improved features of enzymes after immobilization, we can highlight the following: (i) increased enantiospecificity or regioselectivity (e.g., lipases41 or penicillin G acylase42); (ii) improved performance in kinetically controlled synthesis (e.g., penicillin G acylase43 or β‐galactosidase44); (iii) reduced inhibition (e.g., β‐galactosidase,45 proteases,46 or nitrilile hydrolases47); (iv) lower chemical modification by reactive by‐products (e.g., caused by hydrogen peroxide48); and (v) improved enzyme reactivation 49…”

Reconstruction of metabolic pathways in selected bacterial and yeast strains for the production of bio-ethylene from crude glycerol: A mini review

“…Heterologous gene expression is one of the most promising technologies found to deliver higher protein yields. For example, heterologous gene expression of nitrile hydratase in Escherichia coli (E. coli) offers rapid growth, high yields and economic production of recombinant products (Chiyanzu et al, 2010). Over the past two decades, a large number of researchers have focused on the expression of genes that encode efe for ethylene biosynthesis.…”