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Isolation, Purification and Characterization of a Trypsin-Like Protease From the Root-Knot Nematode, Meloidogyne Incognita

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For more content, see Nematology.

Trypsin-like protease from second-stage larvae of the root-knot nematode, Meloidogyne incognita, was isolated, purified and characterized. The enzyme was purified through a number of steps including ammonium sulfate precipitation, gel filtration of Sephadex G-75 and DEAE-Sephadex A-50. About 38-fold purification from the crude extract was obtained at the final step with high specific activity. The purified enzyme preparation was considered to be homogeneous as revealed by polyacrylamide disc electrophoretic studies. The enzyme was most active in a slightly alkaline medium at pH 7.5-8.5, anionic, unstable at lower pH and had a molecular weight of 23,200 as estimated by gel filtration method. Synthetic substrates including αN-benzoyl-L-arginine ethyl ester (BAEE) and p-tosyl-L-arginine methyl ester (TAME) were readily hydrolyzable by the enzyme at optimal pH 8.0-8.5. The rate of hydrolysis was as fast as that of bovine trypsin when synthetic substrates (BAEE and TAME) were used. The enzyme was inhibited by soybean trypsin inhibitor, ovomucoid and diisopropylflurophosphate (DFP), however, not by L-1-tosylamide-2-phenylethyl-chloromethyl ketone (TPCK). Inhibition studies indicate that the enzyme belongs to the 'serine proteases'. Root-knot nematode trypsin-like enzyme did not require calcium for stabilization. No evidence of a zymogen form of the enzyme was detected.

Affiliations: 1: Division of Nematology, Indian Agricultural Research Institute, New Delhi-110012, India


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