PURIFICATION AND CHARACTERIZATION OF CHITINASE FROM SEVERAL WHEAT CULTIVARS INDUCED BY Trichoderma

The goal of this study was to purify and characterise the chitinase enzyme produced by the fungus Trichoderma longibrachiatum T1 in numerous wheat varieties. The wheat cultivar Iba 99 had the highest effect of chitinase induction, with 1.77 units / ml, followed by the cultivar Abu Ghraib with 1.72 units / ml and 0.62 units / ml, and the controlled treatment for the same variety with 0.61 units / ml. The Rabia cultivar had the lowest effect of 1.36 units/ml, whereas the controlled treatment had the lowest effect of 0.48 units/ml. The induced Iba 99 was used to purify the enzyme. The enzyme yield was 72.47 percent after sedimentation with 80 percent ammonium sulphate salt, DEAE - Cellulose Ion exchange chromatography, and Sephadex G-100 gel filtration chromatography. The specific activity after the last step was 43.13 units / mg protein, the number of purification times was 70.22, and the number of purification times was 70.22. The chitinase enzyme was then characterised, with the Km and maximum velocity Vmax values of 12.65 mg / ml and 6.95 u / ml, respectively, as shown by the results. The activity of the chitinase enzyme was best at pH levels of 5 and 6. For the chitinase enzyme, the pH range for stability was 5 to 6. The chitinase enzyme was thermally stable for one hour between 10 and 20 degrees Celsius. The enzyme's activity was best at temperatures between 30 and 40 degrees Celsius. The isolated enzyme had a molecular weight of 30.2 KDa.

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