Region-Directed Enzyme Immobilization through Engineering Protein Surface with Histidine Clusters.

ABSTRACT: Enzyme immobilization is a key enabling technology for a myriad of industrial applications, yet immobilization science is still too empirical to reach highly active and robust heterogeneous biocatalysts through a general approach. Conventional protein immobilization methods lack control over how enzymes are oriented on solid carriers, resulting in negative conformational changes that drive enzyme deactivation. Site-selective enzyme immobilization through peptide tags and protein domains addresses the orientation issue, but this approach limits the possible orientations to the N- and C-termini of the target enzyme. In this work, we engineer the surface of two model dehydrogenases to introduce histidine clusters into flexible regions not involved in catalysis, through which immobilization is

SUBMITTER: Zeballos N 

PROVIDER: S-EPMC10788835 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature