Peroxidase enzymes contain iron atoms (Fe2+) in their active sites. They use peroxides such as hydrogen peroxide (H2O2) to receive electrons, making water as a product. After donating an electron to peroxide, their activated iron can accept electrons from a variety of organic and inorganic compounds with a variety of consequences. This activity has been proposed for a number of uses such as removal of contaminants from wastewater or for organic polymer synthesis. These uses will be discussed in subsequent papers.
Several categories of peroxidase enzymes are known. They vary in size and activity spectrum. Of particular interest to Infinite Enzymes, LLC is the manganese peroxidase originally from the white rot fungus, Phanerochaete chrysosporium. The wonderful enzymes in this fungus are quite good at degrading the phenolic compounds produced by the plant during its growth—all that woody brown stuff that makes the plant stand up under the force of gravity. However, the fungus only makes little bits of these enzymes as it needs them for growth. If the industrial community is going to use this enzyme ( in particular) we must have a way to make buckets of it inexpensively. Thus, a recombinant system is the likely solution—making them in a non-native host system that will allow a large accumulation of protein in spite of its strong production of oxidants. (Remember how we like to eat anti-oxidants to keep us healthy?)
This article is provided by Elizabeth Hood, Ph.D., Lipscomb Distinguished Professor of Agriculture at Arkansas State University and the Founder of Infinite Enzymes.
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