Enzymatic characterization of highly stable human alpha-galactosidase A displayed on magnetic particles

The human α-galactosidase A (EC 3.2.1.22, GLA), a lysosomal enzyme with important biotechnological and biomedical applications, has been successfully immobilized for the first time onto different versions of micro-sized magnetic particles by means of alternative coupling chemistries (covalent and metal affinity adsorption). The immobilized enzyme shows higher specific activity than its soluble counterpart and its enhanced stability as well as the magnetic-controlled positioning and reusability provided by coupling make these new bioconjugates excellent platforms for the presentation of highly active and pure versions of human GLA for both in vitro catalysis and therapeutic applications.

► The human α-galactosidase A enzyme has been coated onto magnetic microparticles. ► His-tag directed anchoring results in better performance than covalent conjugation. ► Immobilized enzyme shows better activity and stability than the soluble form. ► Coating onto magnetic carriers allows the recycling of the immobilized catalyst.