[Hydrolysis of insoluble bone collagen by crystalline alpha-amylase from Aspergillus oryzae].

The paper deals with hydrolysis of bone collagen thrice recrystallized alpha-amylase. The enzyme action was estimated by the amount of released glycopeptides, free carbohydrates, alpha-amine groups and total nitrogen in the soluble part of the hydrolyzate. The protease admixture in the alpha-amylase preparation was found by means of the Aspergillus oryzae protease. The data obtained testify to the fact that hydrolysis of collagen under the effect of crystalline alpha-amylase occurs only due to the protease admixture in the amylolitic preparation. When an attempt was made to obtain acid-soluble collagen from bone insoluble collagen previously treated with the alpha-amylase preparation, it was found that under these conditions bone collagen, as distinct from skin collagen, is not solubilized in diluted acetic acid.