Microreactor
technology is being increasingly utilized in the field
of biocatalysis, offering cost-effectiveness and environmental sustainability.
On the other hand, enzyme immobilization on nanomaterials can provide
biocatalytic systems with the operational stability demands of an
intensified bioprocess. Combining the methodology for ZnO nanowire
growth on glass surfaces with enzyme immobilization techniques, we
developed a novel continuous-flow microbioreactor system, with β-glucosidase
activity. Morphological, spectroscopic, and biocatalytic characterization
of the developed enzyme microreactor is presented. The immobilized
enzyme exhibited almost 100% remaining hydrolytic activity after 1000
cycles of continuous use and more than 70% residual activity after
24 h of exposure to different organic solvents. The system productivity
was enhanced up to 10 times compared to the free enzyme form and 30
times compared to the batch immobilized system. Compared to previous
studies in batch reactor systems, the enzyme microbioreactor exhibited
a productivity enhancement of 315 and 12 times, respectively, for
the continuous glycosylation of the natural compounds perillyl alcohol
and tyrosol toward the synthesis of their bioactive glycosylated derivatives.
The entire arrangement seems to provide a proper microenvironment
for enzyme stabilization, under the scope to broaden the biocatalyst’s
potentiality.