Making hydrogen peroxide greener
A promising new technology capitalizes on the enzymes from an extremophile bacterium.
Researchers at the U.S. Department of Energy’s Idaho National Laboratory (INL) reported in October that they have discovered a way to improve the utility of hydrogen peroxide as an environmentally benign agent for industrial bleaching, cleaning, and disinfection processes.
The new technology relies upon an enzyme produced by an extremophile bacterium, Thermus brockianus, which is found in the hot springs of Yellowstone National Park. This catalase enzyme was discovered and developed by INL chemical engineer Vicki Thompson and biologists William Apel and Kastli Schaller. It has a much longer industrial half-life than comparable commercial catalase enzymes—15 days rather than 15 seconds.
The enzyme is able to remove hydrogen peroxide by breaking it down after it has been used to treat wastewater. The INL team believes that the new enzyme may prove useful for industrial food processing, because hydrogen peroxide is increasingly being used to eliminate salmonella, E. coli, and other toxic bacteria on fresh produce, as well as for pasteurizing dairy products and sterilizing paper food packages, such as juice boxes. Textile and paper manufacturers are also switching from chlorine bleach to the safer hydrogen peroxide to whiten and disinfect products.
INL’s tests have shown that wastewater needs no additional treatment to remove hydrogen peroxide after the enzymatic treatment is used. In fact, they have also shown that the enzyme can be reused to treat multiple batches of wastewater. The team is pursuing collaborations for industrial development with major enzyme manufacturers.
