title: [Hydrolysis of insoluble bone collagen by crystalline alpha-amylase from Aspergillus oryzae].
abstract: 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.
mesh_terms: D000681:Amylases / Q000378:metabolism*; D000818:Animals; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D001842:Bone and Bones / Q000378:metabolism*; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D003460:Crystallization; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000378:metabolism; D012867:Skin / Q000378:metabolism; D012995:Solubility
chemical_list: D003094:Collagen; D000681:Amylases; D010447:Peptide Hydrolases
vernacular_title: Hidroliz nerozchynnoho kolahenu kistok krystalichnoiu al'fa-amilazoiu z Aspergillus oryzae