Collagenases are endopeptidases that digest native collagen in the triple types of collagen pdf region. Collagens are the major fibrous component of animal extracellular connective tissue.
In 1959, the first commercially available collagenase isolated from Clostridium histolyticum was offered by Worthington. At that time, only one preparation of crude enzyme was offered. After collagenases from Clostridium histolyticum were first prepared by Mandl et al. 1950s to the mid 1980s found that several separable collagenases exist and these fractions’ specificities and stabilities were partially characterized. Grant and Alburn 1959, Mandl et al. 1964, Yoshida and Noda 1965, Kono 1968, Seifter and Harper 1970, Harper and Kang 1970, Lwebuga-Mukusa et al.
Until 1962, most interest in collagenases centered on clostridial collagenases. Schoellmann and Fisher 1966, Welton and Woods 1973 and 1975, Keil et al. Further studies of collagenases from human and other mammalian sources were reported on, and continue to be actively studied in order to better understand the pathology and treatment of human diseases. Abe and Nagai, 1973, Kruze and Wojtecka 1972, Bauer et al.
1973 and 1975, Alaho et al. The hyper-reactive sites where the Class I and Class II enzymes initially attack all three collagen types were identified by French et al. Clostridial collagenases’ ability to digest native, triple-helical types I, II, and III collagens into a mixture of small peptides is its primary distinguishing factor. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. The colG gene codes for type I collagenase, a 936 amino acid peptide.
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