Simulation-guided enzyme discovery: A new microbial source of cellobiose 2-epimerase
2019
Abstract Cellobiose 2-epimerase (CE) is a promising industrial enzyme that can be utilized in the dairy industry. More thermostable CEs from different microorganisms are still needed for a higher lactulose productivity. This study demonstrated the feasibility to use molecular dynamics (MD) simulation as the preliminary computational filter for thermostable enzymes screening. Sequence information of eleven uncharacterized CEs were chosen to be analyzed by MD simulations. The CE from Dictyoglomus thermophilum (Dith-CE) was determined experimentally to be one of the most thermostable CEs with the highest epimerization (160 ± 6.5 U mg−1) and isomerization activities (3.52 ± 0.23 U mg−1) among all the reported CEs. This enzyme shows the highest isomerization activity at 85 °C and pH 7.0. The kinetic parameters (kcat and Km) of isomerization activity of this CE are 3.98 ± 0.3 s−1 and 235.2 ± 11.2 mM, respectively. These results suggest that the CE from Dith-CE is a promising lactulose-producing enzyme.
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