Arginine-to-lysine substitutions influence recombinant horseradish peroxidase stability and immobilisation effectiveness.

ABSTRACT:

Background

Horseradish Peroxidase (HRP) plays important roles in many biotechnological fields, including diagnostics, biosensors and biocatalysis. Often, it is used in immobilised form. With conventional immobilisation techniques, the enzyme adheres in random orientation: the active site may face the solid phase rather than bulk medium, impeding substrate access and leading to sub-optimal catalytic performance. The ability to immobilise HRP in a directional manner, such that the active site would always face outwards from the insoluble matrix, would maximise the immobilised enzyme's catalytic potential and could increase HRP's range of actual and potential applications.

Results

We have replaced arginine residues on the face of glycan-free recombinant HRP opposite to the acti

SUBMITTER: Ryan BJ 

PROVIDER: S-EPMC2234406 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature