A novel trypsin, active and stable over a broad pH range, was purified to apparent homogeneity from S. basilisca viscera. The enzyme was found to be active and stable at alkaline pHs, as well as in the presence of non-ionic and ionic surfactants. Moreover, it showed excellent stability and compatibility with a wide range of commercial solid laundry detergents. These results suggest that the S. basilisca trypsin would be a potential candidate for certain food processing operations, and as a laundry detergents additive.