Abstract
This study focused on the purification and characterization of chitinase from alfalfa (Medicago sativa L.) infected by CP-MLO. Chitinase (EC 3.2.1 14) was purified from leaves and shoots of MLO-infected alfalfa plants by ammonium sulfate precipitation, chitin affinity chromatography and Sephadex column chromatography. Three chitinase isoenzymes were identified and shown to have molecular masses of approximately 40, 35 and 30 kilodaltons as determined by SDS-polyacrylamide gel electrophoresis, while only one chitinase isoenzyme was detected in healthy plants. The endochitinase activity in CP-MLO infected plants was 24 times higher than that in healthy plants. The optimum temperature range of the enzyme activity was from 35°C to 50°C. Ag and Hg ions significantly inhibited the enzyme activity.
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