Physicochemical properties of the elastolytic enzyme complex of Bacillus subtilis
Bondarchuk, A.A.; Vasilevskaya, I.A.; Sergeichuk, M.G.
Mikrobiolohichnyi Zhurnal 44(4): 8-11
1982
ISSN/ISBN: 0201-8462 PMID: 6813658 Document Number: 189467
Two enzymic preparations with caseinolytic activity were isolated from the culture fluid of B. subtilis by ammonium sulfate salting out (40 and 80% saturation for the 1st and 2nd preparations, respectively). The ability to hydrolyze elastin is peculiar only to the first preparation. Isoelectrofocusing of the preparation in the borate-polyol system induced division of the 1st preparation into 5 protein groups, 4 of them being caseinolytically active. Proteins with pI 4.8 and 6.0 also hydrolyzed elastin. Data on disc-electrophoresis showed that the group of proteins with pI 6.0 contained up to 14 protein components. Proteins of the 2nd enzymic preparation with the caseinolytic activity were focused at the pH value of pH 7.3; this group contains up to 9 protein components.