Abstract
ABSTRACTMeasurements of properties relating to the physical integrity of heat‐processed fish gels varied among samples obtained over a 1‐yr period or subjected to various processing temperatures. Such gel properties correlated well with the heat‐stable protease (alkaline protease) activity measured in the raw samples. A significant inhibitor concentration‐dependent relationship was noted between the addition of a potato derived protease inhibitor and gel strength. These observations support the causative role of an erzymic proteolytic agent in the weakening of gel integrity at processing temperatures near 60°C.
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