Mar 1, 1975

Hydrolysis of insoluble collagen of bull bones by Streptomyces griseus crystalline protease

Ukrainskiĭ biokhimicheskiĭ zhurnal
I F MyshuninI M Kuznetsova

Abstract

Hydrolysis of collagen was studied in the bull bone tissues by the Str. griseus crystalline protease. The amount of collagen hydrolyzed by it composed 6.6% and 16% after 4-hour and 6-hour hydrolysis, respectively. When the enzyme:substrate ratio is 1:50 hydrolysis proceeds most intensively; with a decrease in the ratio up to 1:1000 the average amount of peptides increase from 2.6 up to 4 amino acidic residua, respectively. Under conditions of denaturated collagen hydrolysis the content of hydroxyproline in solution as compared with the native one increases; in this case the links with the presence of imino-acids are easier to split, the more resistant being those formed by hydroxyproline. Within the limit of 20-45 degrees C hydrolysis of protein intensifies with a temperature rise. Within the pH range of 5.0-11.0 the maximal amount of alpha- NH2-groups and hydroxyproline is observed at pH 8.5, the minimal--at PH 5.0. Hydroxyproline in the composition of peptides appears at the beginning of hydrolysis whereas the free one of enzymes of the longer effect 24 h after the beginning of the experiment composes 12.2% of its total content in the solved products. In the insoluble part of the substrate after 3-hour hydrolysis tyrosine com...Continue Reading

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Mentioned in this Paper

Peptide Hydrolases
Zyderm
Streptomyces griseus
Bos indicus
Skeletal Bone
Hydrolysis
Hydrogen-Ion Concentration

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