Submitted to: Journal of Industrial Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/10/1996
Publication Date: N/A
Citation: N/A Interpretive Summary: Due to environmental concerns, there has been a worldwide increase in the use of phosphate-free detergent formulations. Typically, the cleaning power of phosphate-free formulations needs to be strengthened by the addition of environmentally friendly enzymes. The added enzyme must be rather unique in that it must be able to withstand the harsh conditions (by enzyme standards) of a wash solution. Therefore, new and better enzymes are needed. In this report, a protease (enzyme that degrades stains) was isolated from a novel marine organism and was tested in cleansing formulations. The protease outperformed currently utilized enzymes in several applications. It was also discovered that this protease was extremely stable in the presence of oxidants, which are often used as brighteners in detergents. This feature makes the enzyme a very attractive candidate for commercial production. Two drawbacks for industrial utilization were also identified and possible solutions were discussed. If the solutions are successful, this work will benefit industrial enzyme producers, detergent manufacturers, as well as the general public which is concerned about cleaner water (not contaminated with high levels of phosphate).
Technical Abstract: An alkaline protease, previously isolated from a symbiotic bacterium found in the gland of Deshayes of marine shipworm, was evaluated as a cleansing additive. The protease nearly doubled the cleaning power of a standard phosphate detergent at temperatures up to 50 deg C as determined by fabric swatch assays. The enzyme was, however, ineffective at 70 deg C. In both fresh and seawater, it was also an efficient presoak. The cleaning power of a non-phosphate detergent was significantly improved by added protease, independent of the pH range 10 to 12. The enzyme degraded lysozyme, the major protein contaminant of contact lenses, more efficiently than subtilisin and was effective in solutions containing hydrogen peroxide, often employed to sterilize lenses. The protease was unusually stable in sodium perborate, as well as hydrogen peroxide, and retained good activity in the presence of sodium hypochloride.