Purification of a 6.5 kDa Protease Inhibitor from Amazon Inga umbratica Seeds Effective Against Serine Proteases of the Boll Weevil Anthonomus grandis

Author(s): L. A. Calderon, R. C.L. Teles, J. R.S.A. Leite, O. L. Franco, M. F. Grossi-de-Sa, F. J. Medrano, C. Bloch Jr., S. M. Freitas.

Journal Name: Protein & Peptide Letters

Volume 12 , Issue 6 , 2005

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A 6.5 kDa serine protease inhibitor was purified by anion-exchange chromatography from the crude extract of the Inga umbratica seeds, containing inhibitor isoforms ranging from 6.3 to 6.7 kDa and protease inhibitors of ∼19 kDa. The purified protein was characterized as a potent inhibitor against trypsin and chymotrypsin and it was named I. umbratica trypsin and chymotrypsin inhibitor (IUTCI). MALDI-TOF spectra of the IUTCI, in the presence of DTT, showed six disulfide bonds content, suggesting that this inhibitor belongs to Bowman-Birk family. The circular dichroism spectroscopy indicates that IUTCI is predominantly formed by unordered and β-sheet secondary structure. It was also characterized, by fluorescence spectroscopy, as a stable protein at range of pH from 5.0 to 7.0. Moreover, this inhibitor at concentration of 75 μM presented a remarkable inhibitory activity (60%) against digestive serine proteases from boll weevil Anthonomus grandis, an important economical cotton pest.

Keywords: protease inhibitor, chymotrypsin inhibitor, trypsin inhibitor, amazon forest, bowman-birk inhibitor, Inga umbratica, insect control, anthonomus grandis

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Article Details

Year: 2005
Page: [583 - 587]
Pages: 5
DOI: 10.2174/0929866054395888
Price: $65

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