الفهرس 
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Abstract
• Chitinase enzyme was purified by using chitin affinity techniques. In Phaseolus vulgaris var. Paulista, the purification techniqu results displayed that the enzyme was purified 2.47-fold with a specific activity of 1.93 U/mg protein after ammonium sulphate precipitation. utilising the chitin affinity binding, the enzyme purified to 5.61-fold with a specific activity of 4.38 U/mg protein. .
• In Phaseolus vulgaris var. Nebraska, the purification procedure results proved that the enzyme was purified 2.07 -fold with a specific activity of 2.039 U/mg protein after ammonium sulphate precipitation, while, Following the purification stage including chitin affinity binding, the enzyme achieved a 6.51-fold purification and 6.389 U/mg protein specific activity.
• The molecular weight of the produced chitinase was determined using SDS-PAGE. 32.500 KDa In Phaseolus vulgaris var. Paulista, while in Phaseolus vulgaris var. Nebraska The molecular weight of the obtained chitinase was calculated34. 000 KDa.
• The optimum PH value was 5.4 In Phaseolus vulgaris var. Paulista, while In Phaseolus vulgaris var. Nebraska the optimum PH value was 4. A significant DROP in chitinase activity would result with either a small pH increase or fall, about 5.4 or 4 in both types.
• In both varities (Phaseolus vulgaris var. Paulista, Phaseolus vulgaris var. Nebraska) the chitinase activity indicated the optimum at a temperature of 45°C, below and above this temperature there were a reduction in the enzyme activity.
• Purified chitinase in both varities (Phaseolus vulgaris var. Paulista, Phaseolus vulgaris var. Nebraska) were stable from 45°C to 50°C. Incubation at 55°C for 30 min. in both varities resulted in approximately half loss of the enzyme activity. There were rapidly inactivated when they incubated at a temperature above 65°C.
• In both varities (Phaseolus vulgaris var. Paulista, Phaseolus vulgaris var. Nebraska.) increasing concentration of metal ions exhibited an increase in the enzyme activity in case of (CaCl2 , MgCl2, NaCl, and KCl), whereas (MnCl2, ZnCl2) did not show any remarkable effects. However, the highest inhibition activity was obtained by using (PbCl2 and HgCl2) which showed less than 40% relative activity in both varities.
• The purified chitinase enzyme’s antifungal activity from (Phaseolus vulgaris var. Paulista and Phaseolus vulgaris var. Nebraska) were tested against a collection of fungi through crescents of inhibition around wells and clear zones around disks, they exhibited a very remarkable effects against Alternaria alternate, Fusarium moniliform, Fusarium oxysporum, followed by Fusairum solani and Candida albicans.
• Chitinase showed antibacterial efficacy against the pathogenic microorganisms Staphylococcus aureus and Pseudomonas aeruginosa in both tested plant varities. We found that, In Phaseolus vulgaris var. Paulista the inhibition zone diameter of Staphylococcus aureus is (4mm), while in the Pseudomonas aeruginosa is (3.8mm). In Phaseolus vulgaris var. Nebraska the inhibition zone diameter of Staphylococcus aureus (4.75 mm) and in the Pseudomonas aeruginosa is (4.25mm).
• One crucial indicator of chitinase potency is its capacity to break down several polysaccharides. When the enzyme’s ability to digest six different substrates was evaluated, it was clear that colloidal chitin provided superior digestion. followed by chitin powder than other polysaccharides under the same assay conditions in two varieties of Phaseolus vulgaris (var. Paulista and var. Nebraska).