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SUMMARY
The exocellular chitinase system of Chytriomyces hyalinus Karling has been studied. The conditions necessary for obtaining a high yield of chitinase and a procedure for concentrating the enzyme are given.
The activity of the crude chitinase was assayed using a C14-chitin decomposition assay. This assay is based on the use of C14-chitin as the enzyme substrate. With the radioactivity of the substrate known, the amounts of radioactivity released into solution by chitinase under different conditions can be compared. The C14-chitin is obtained by growing the fungus Allomyces macrogynus (Emerson) Emerson & Wilson on C14-glucose. The fungus incorporates C14-chitin substrate.
The optimum temperature for chitinase activity is 25 C, the optimum pH is 5.5. The Michaelis constant of the crude chitinase is 5.7 μmoles of reducing sugar per mg of protein. Chitinase activity is not inhibited by N-acetylglucosamine or glucose. Copper and cadmium ions cause almost total inhibition. Potassium, sodium, magnesium, lithium and cobalt ions all cause some inhibition of chitinase activity.