The action of protease in
Bacillus Natto on the sericin fractions A and B, prepared by means of MOSHER'S method, has been investigated under the same plan as in the previous report. The results obtained are, as the following, considerably different from those on the latter.
1) Although the activity-pH-curves of both fractions resemble each other in their form, they do not overlap, i. e. the maximum of the A curve lies on pH 7.8 and that of B on pH 7. 2.
2) The curves of activity-substrate concentration of both fractions show, contrary to the case of sericinase, a bell form, and moreover they are different from each other. The maximum zone of the curves of A and B lies on the concentration of the total nitrogen of about 40mg% and 50mg% respectively.
3) The extent of hydrolysis of A and B fractions by Natto-protease is almost the same at the respective optimal pH and substrate concentration of fractions, therefore the conclusion of the splitting ability of one fraction should not be immediately drawn, whatever it may be attached preferably under a certain condition.
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