Enzyme-Support Interactions of <i>Burkholderia cepacia</i> Lipase Immobilized on Silica Using Molecular Docking and Multitechnique Characterization.

ABSTRACT: The influence of the microenvironment within enzyme-support complexes on the activity of Burkholderia cepacia lipase (BCL) immobilized on silica (SiO₂-BCL) remains insufficiently understood. Without data on these interactions, it is challenging to determine whether modifications to the support material or immobilization protocols are needed for optimal enzyme activity and stability. Besides evaluating catalytic performance in esterification reactions, enzyme-support interactions were characterized using ²⁹Si NMR, FTIR, BET, DSC, TGA, SEM-EDS, and molecular docking simulations. In this study, NMR²⁹Si-based structural analysis revealed significant protein-surface (pore wall) interaction networks. The immobilization resulted in 88.6% efficiency and a pr

SUBMITTER: Rodrigues CA 

PROVIDER: S-EPMC12464904 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature