Indian Journal of Agricultural Research

  • Chief EditorT. Mohapatra

  • Print ISSN 0367-8245

  • Online ISSN 0976-058X

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Indian Journal of Agricultural Research, volume 47 issue 3 (june 2013) : 263-266

ISOLATION OF PROTEINASE INHIBITORS FROM OKRA FOR INHIBITING THE HELICOVERPA ARMIGERA (HUBNER) GUT PROTEINASES

Shilpa K. Udamale, M.P. Moharil, T.B. Ugale*, J.M. Mankar
1Biotechnology Centre, Dr. Panjabrao Deshmukh Agricultural University, Akola- 444 104, India

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Cite article:- Udamale K. Shilpa, Moharil M.P., Ugale* T.B., Mankar J.M. (2024). ISOLATION OF PROTEINASE INHIBITORS FROM OKRA FOR INHIBITING THE HELICOVERPA ARMIGERA (HUBNER) GUT PROTEINASES. Indian Journal of Agricultural Research. 47(3): 263-266. doi: .

ABSTRACT

Experiment was conducted to estimate the protein content and inhibitory potential of different genotypes of okra and its wild relatives towards trypsin and chymotrypsin in in vitro. The wild relatives of okra possessed high protein content as compared to the cultivated genotypes. From wild relatives A. tuberculatus (90396 and 90515) contained high protein content up to 3.31 mg g-1 and 3.27 mg g-1 seed flour, respectively. The wild relatives of okra PIs from A. tuberculatus (90396 and 90515) inhibited the maximum trypsin activity i.e. upto  68.1 and 66.9 per cent, whereas, the chymotrypsin activity was found to be 68.4 and 65.8 per cent respectively. On the other hand VRO-3 and  AKO-102  exhibited 63.3 and 62.2 per cent trypsin activity, also least chymotrypsin activity found upto 62.4  and 61.1 per cent. Since the proteinase inhibitors of wild relatives of okra possessed higher trypsin inhibitory potential than cultivated ones.

REFERENCES

  1. Bradford, M.M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
  2. Broadway R.M. and Duffey S.S. (1986). Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua. J Insect Physiol 32: 827-833.
  3. Casaretto J.A. and Corcuera L.J. (1995). Plant proteinase inhibitors: A defensive response against insects. Biol. Res. 28(4): 239-49.
  4. Chougule N.P., Hivrale V.K., Chhabda P.J. and Giri A.P. (2003). differential inhibition of Helicoverpa armigera gut proteinase-by-proteinase inhibitors of pigeonpea (Cajanus cajan) and its wild relatives. Photochemistry 64: 681-687.
  5. Giri A. P., Harsulkar A. M., Deshpande V. V., Sainani M. N., Gupta V. S. and Ranjekar P. K. (1998). Chickpea defensive proteinase inhibitors can be inactivated by pod borer gut proteinases. Plant Physiol. 116: 393-401.
  6. Hilder V. A., Boulter D., Gatehouse K., Powell S., Brough C., Hamilton W D O,. Newell C, Merryweather A., and Gatehouse J. A. (1993). Approaches to insect resistance using transgenic plants. Philos. Trans. Royal Soc. London. B 342: 279-286.
  7. Jongsme M. A. and Bolter C. J. (1996). The adaptation of insects to plant protease inhibitors. J Insect Physiol; 43: 885-895.
  8. Koiwa H., Bressan R. A., and Hasegawa P. M., (1998). Regulation of protease inhibitors and plant defense. Trends Plant Sci 2: 379-384.
  9. Michaud, D., Rnguenot, R., and Brunelle, F., (2005). U.S. Patent No. 20050055746.
  10. Ogata. F., H. Imamura, K. Hirayama and S. Makisumi. 1986. Purification and characterization of four trypsin inhibitors from seeds of okra, Abelmoschus esculentus L. Agric. Biol. Chem.50 (9) : 2325-2333.
  11. Patankar A.G., Giri A.P., Harsulkar A.H., Sainani M.N., Deshpande V.V., Ranjekar P.K. and Gupta V.S. (2000). Complexity in specificities and expression of Helicoverpa armigera gut proteinases explain polyphagous nature of the insect pest. Insect Biochem. and Mol. Bio. 31(4): 453-464.
  12. Ryan C.A. (1990). Proteinase inhibitors in plants: Genes for improving defenses against insect and pathogens. Annu Rev Phytopathol; 28: 425-449.
  13. Wu Y., Llewellyn D., Mathews A. and Dennis E.S., (1997). Adaptation of Helicoverpa armigera (Lepidopter: Noctuidae) to proteinase inhibitor expressed in transgenic tobacco. Mol. Breed. 3: 371-380.
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