Glycogenolytic Enzymes of Cod (Gadus callarias) Muscle

Abstract

Some properties of the enzymes amylase, phosphorylase, and phosphoglucomutase in homogenates of cod muscle have been investigated. Amylase is activated by a short period of autolysis and by chloride ions; hydrolyses cod muscle glycogen at about half the rate it hydrolyses mussel glycogen; has an optimum temperature of 52 C for up to 5 hr incubation; and has a wide range of activity with maxima around pH 5.1 and between pH. 7.0 and 7.5. Using phloridzin, an estimate of the relative importance of hydrolytic and phosphorolytic cleavage of polysaccharide in cod muscle homogenates has been made. Phosphorylase shows two activity maxima at pH 5.5 and 6.7. The properties of phosphoglucomutase, with the exception of its pH activity, in cod muscle are similar to those reported for this enzyme in other tissues. Cod muscle phosphoglucomutase has maximum activity between pH 8 and 9.