Magnetically controlled enzymatic
composites have received much
attention for both therapeutic and industrial applications. Until
now, such materials have been composed of at least four components:
the enzyme, magnetic nanoparticles, their stabilizing components,
and an organic or inorganic (or hybrid) matrix as a carrier. However,
such compositions affect the magnetic response and the enzymatic activity,
and also pose obstacles for intravenous administration, because of
regulatory restrictions. Here, we present a methodology for the creation
of magnetic bioactive nanocomposites composed of only two biocompatible
components: an enzyme and magnetite nanoparticles. A series of magnetic
biocomposites with a full set of therapeutical and industrial proteins
(carbonic anhydrase, ovalbumin, horseradish peroxidase, acid phosphatase,
proteinase, and xylanase) were successfully created by the direct
entrapment of the proteins within a sol–gel magnetite matrix
specially developed for these aims. The activity of the entrapped
enzymes was studied at different temperatures and concentrations,
and it was found that they showed remarkable thermal stabilization
induced by the ferria matrix. For instance, entrapped carbonic anhydrase
catalyzed the decomposition of p-nitrophenylacetate
at a temperature of 90 °C, while free enzyme completely loses
activity and denaturates already at 70 °C. Magnetic characterization
of the obtained biomaterials is provided.