Taken from a microbe that thrives in the depths of a Yellowstone National Park hot springs pool, a newly discovered enzyme may be the key to transforming industrial bleaching from environmentally problematic to environmentally green.
Chemical engineer Vicki Thompson and biologists William Apel and Kastli Schaller from the U.S. Department of Energy's Idaho National Engineering and Environmental Laboratory discovered that the catalase enzyme from a Thermus brockianus microbe flourishes in both a high temperature and high pH (basic or alkaline) environment.
Catalase enzymes chemically alter hydrogen peroxide into natural products water and oxygen. Industry is increasingly using peroxide in industrial bleaching processes and needs an environmentally friendly process to handle process wastes. The T. brockianus catalase works well in the hot, alkaline process wastewater where commercially available catalase enzymes do not, so it could be an answer.
Thompson will present this work at the American Society of Microbiologists annual meeting in Washington, D.C. on May 20, 2003. A paper on this research was recently accepted for publication in Biotechnology Progress and will appear in print this summer.
The work is part of the INEEL's efforts to support the DOE mission in environmental research and development.
Industries such as textile and pulp and paper have started shifting away from toxic, carcinogenic chemical bleaching processes to more environmentally friendly hydrogen peroxide-based bleaching. Until INEEL discovered the T. brockianus enzyme, there were only a few options for dealing with the wastewater.
Industry can chemically treat the water to break hydrogen peroxide down, but that practically cancels out the environmental benefit. Or they can heavily dilute wastewater with even more water, but t
Contact: Deborah Hill
DOE/Idaho National Laboratory