The discovery of DNase I dates back to the early 20th century. In 1903, Araki demonstrated the ability of certain tissue extracts to liquefy gels of alpha-nucleic acid . Over the following decades, various researchers identified enzymes capable of cleaving nucleotides, which were given different names such as nucleinase, nucleogelase, and desoxyribonuclease . In 1950, Kunitz crystallized the enzyme and named it deoxyribonuclease .
Bovine pancreatic DNase I exists in four isozymes, designated A, B, C, and D, with isoelectric points of 5.22, 4.96, 5.06, and 4.78, respectively . The predominant form is isozyme A, with smaller amounts of B and C, and only a minor amount of D . The enzyme’s structure includes two central β-sheets, each composed of six β-strands, surrounded by extensive loop and α-helical regions .
DNase I has a wide range of applications in molecular biology and medicine:
The production of DNase I involves the extraction and purification of the enzyme from bovine pancreas. Advances in biotechnology have also enabled the cloning and expression of the DNase I gene in microorganisms such as Escherichia coli . This recombinant production method ensures a consistent and high-quality supply of the enzyme for various applications.