Abstract

The proteolytic activity of an enzyme preparation from the pyloric caeca of redfish (Sebastes marinus) was studied and measured colorimetrically by the biuret reaction. The optimum temperature of this preparation was found to be 51–52 °C. A statistical study of the data showed the optimum pH to be 8.75, or slightly higher than the optimum pH of trypsin. A comparison of the actions of a commercial leather bate, hog intestinal mucosa, papain, pancreatin, trypsin and the caecal enzyme of redfish on casein led to the conclusion that the pyloric caeca of redfish would furnish a suitable material from which to prepare a leather bate.

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