06.07.2020: New Publication: More enzyme stability by immobilization technology

Our recent HOTZYMES publication showcases the co-immobilization of a multimeric enzyme with magnetic nanoparticles  within composite nanoparticles made of biomimetic silica.

B-glucuronidase was the enzyme of choice: it catalyzes the breakdown of complex carbohydrates. The enzyme is used for drug metabolism studies or as a tool in enzyme prodrug therapy where it enables for a conversion of inert and inactive prodrugs. The potential for biocatalytic applications in pharmaceutical and food industry is huge and can even be increased!

The method described in this publication is a solution to overcome previous problems related to the use of b-glucuronidase in its soluble form and was obtained through collaboration between the research groups of our HOTZYMES partner Dr. Valeria Grazú (ICMA, CSIC) and our collaborator Dr. Lorena Betancor (Universidad ORT Uruguay, Montevideo, Uruguay). With the immobilization approach a better specific activity can be achieved. The research team adopted a recent trend, namely the use of combined materials for immobilization: the biomimetic synthesized silica have the advantage of mild and fast reaction, stability and the suitability for reuse of the enzyme. In combination with magnetic nanoparticles, the material can be easily separated by applying a magnetic field.

These results demonstrate the potential and versatility of this mixed matrix, composed of biomimetic silica and magnetic nanoparticles, for the co-entrapment of an enzyme with a more complex 3D structure (multimeric) than the one previously co-entrapped (monomeric) using the same strategy. This clearly enables for the next step: remote activation of a thermophilic enzymes upon application of an alternate magnetic field.

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