Tiny Beads Protect Enzymes from Damaging Effects of Plasma Co-substrate

A biology research team from the Ruhr University Bochum found that immobilization protects enzymes from plasma-mediated inactivation.

In general, the researchers aimed to use plasmas (charged gas particles that produce reactive species) to drive enzymes using hydrogen peroxide to actually convert substrates into more valuable products. However, enzymes are sensitive to this treatment and are inactivated briefly. This issue was interestingly resolved with enzyme immobilization by attaching tiny beads with porous surfaces to them. Creating a protective zone between the plasma phase at the top (via buffer solution at the enzyme’s top) and the enzyme below (via beads lying at the sample’s bottom), enzymes had varying survival rates through different immobilization methods. Considering this, the discussed study aimed to study the effects of various methods on plasma stability using a larger set of enzymes among which some convert hydrogen peroxide. Additionally, various types of beads were tested. Following immobilization and the subsequent plasma treatment, the research study found that beads with resin surfaces performed the best, forming the strongest covalent bonds with the enzymes that couldn’t be disassociated. 

It was rather interesting to learn that immobilization allows for enzymes to be vastly more protected from the damaging effects of plasma treatment and the reactive species it produces, allowing the enzyme to be infinitesimally more stable and less susceptive to plasma-mediated deactivation. Through this knowledge, it makes it possible for various enzymes to be treated to produce more valuable substances industrially for consumer culture (i.e. the fragrance (R)-1-phenylethanol) and various other applications.

For more information regarding the study, view the news article linked here and the published journal article linked here.