Larvicidal potential of purified protease inhibitor from Solanum aculeatissimum Jacq. against Odoiporus longicollis Oliver.

Meenu VG Krishnan, Murugan K

Abstract


Protease inhibitor was isolated from the fruits of Solanum acculeatissimum Jacq. (SAPI) and purified by four steps. PI activity was assayed by estimating the residual hydrolytic activity of trypsin and chymotrypsin towards the substrates BAPNA (N-benzoyl-L-arginine-p-nitroanilide) and BTPNA (N-benzoyl-L-tyrosyl-p-nitroanilide), respectively, at pH 8.0 after pre-incubation with inhibitor. Molecular mass of  purified PI was evaluated as 22.2 kDa by SDS–PAGE.  Affinity column chromatography yielded a single prominent elution peak. The purity was further checked by RP-HPLC showing a single peak, coinciding with the protein peak. Specific activities of purified PI were 502 TlU and 433.7 CIU U/mg, towards the substrates of trypsin and chymotrypsin respectively with 0.95 mg protein content. Overall, the specific activities increased to 92.6 and 82.9 folds with 9.8 and 8.77 % yield with respect to the substrates. Subsequently, the larvicidal potential of different concentrations of purified SAPI was evaluated against the banana pest Odoiporus longicollis following the treatment on third, fourth and fifth instars larvae. The results of the total percent mortality (from 3rd to 5th instar and adult) demonstrated that the mortality rate progressively increased with the concentrations of SAPI (50 to 250 µM). A minimum of 8% mortality was observed with 50 µM concentration of the PI. It was significant to note that the percent deformity of adults noticed from 50 µM onwards was more than 2%. Thus, the present data suggests an eco-friendly approach for the control of agricultural pest, O. longicollis. Further studies are planned to trace the molecular mechanism of larvicidal potential of SAPI against the pest.

Keywords


Solanum acculeatissimum; Purification; Larvicidal activity; Odoiporus longicollis; Protease inhibitor; Mortality.

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References


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