[Substrate specificity of collagenase of Streptomyces sp. 1349 and keratinase of Streptomyces sp. 1382].

The paper determines the action specificity concerning the bonding type of collagenases of Strepomyces sp. 1349 and keratinases of Streptomyces sp. 1382. Experimental data obtained evidence for the wide specificity of the obtained enzymatic drugs. It has been established that both collagenases and keratinases display high specificity in respect of the bonds made by the residues of hydrophobic amino acids. Collagenases of Streptomyces sp. 1349, as to their wide action specificity, differed from collagenase of Clostridium histolyticum described in literature, that was confirmed by the results of double immunodiffusion in agar by Ouchterloni. Preparations of streptomycete collagenase obtained by the authors did not interact with serum obtained for highly purified collagenase of C. histolyticum of the firm "Merck". Investigation of the feather keratin lysates by the fractions of keratinases 1 and 2 have shown the difference in the content of amino acids released after hydrolysis that may be determined by different specificity of the enzymes action. Cysteine in the amount of 3.8% was also found in keratin lysate of the enzymatic fraction 1, that may evidence for the capacity of the fraction 1 to break the disulphide bonds in keratin molecule.