Rhodococcus ruber strain gtl, possessing nitrile hydratase activity, was immobilized by adsorption on carbon supports differing in structure and porosity. The adsorption capacity of the supports towards cells, the substrate of the nitrile hydratase reaction (acrylonitrile), and the product (acrylamide) was studied. Also, the effect of immobilization and nitrile hydratase activity of bacteria was investigated, and the operational stability of the immobilized biocatalyst was determined. It was shown that crushed and granulated active coals were more appropriate for immobilization than fibrous carbon adsorbents.
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Article Synopsis
- This study focuses on improving the enzyme Fe-type Nitrile hydratase (Fe-type NHase) from Pseudomonas fluorescens by mutating a specific residue (Q86) in its substrate access tunnel, which enhanced its catalytic performance.
- The modified enzyme, PfNHase-αQ86W, demonstrated significantly increased catalytic activity towards various nitrile substrates, with a notable 17.32-fold improvement in efficiency for benzonitrile compared to the wild type.
- Structural analyses revealed changes in the enzyme's entrance tunnel and substrate-binding pocket, which contributed to a shift in substrate preference from aliphatic to aromatic nitriles, supported by molecular dynamics simulations.
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