The Benz-Neburase is a genetically engineered endonuclease from Serratia marcescens used as a DNA eraser in the purification processes of biological molecules. The enzyme cleaves all forms of DNA and RNA into smaller nucleotides of around 5-8 base pairs. Benz-Neburase requires divalent cation, preferably Mg2+ for activity, displays a broad pH tolerance, ranging from pH 6 to pH10, with an optimal pH of 8-8.5, and has a wide temperature tolerance, ranging from 35? to 44?. The nuclease is a physiologic homodimer and functions more progressively than the monomer. Two disulfide bonds in the nuclease are crucial to its activity and stability. The enzyme is active in a broad range of conditions and is free of proteolytic activity. This makes the enzyme especially useful for biopharmaceutical applications with contaminating DNA residue, such as lysed host cells in viral vector manufacturing processes.