Purification and characterization of a trypsin inhibitor from Phaseolus vulgaris L. cultivar IAC carioca seeds
DOI:
https://doi.org/10.22481/exon.v8i1.20438Keywords:
PvTI, Bowman-Birk, FusariumAbstract
Proteinase inhibitors are proteins or peptides capable of specifically and reversibly interact with proteolytic enzymes and are widely distributed in the plant kingdom. This study aimed the purification and characterization of a trypsin inhibitor from Phaseolus vulgaris L. cultivar IAC carioca seeds by ion exchange chromatography on DEAE- Sepharose and high performance liquid chromatography (HPLC). The inhibitor, named PvTI, exhibited an apparent molecular mass of 14 kDa in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and was capable to inhibit bovine trypsin, but not chymotrypsin. The value of the inhibition constant (Ki) against bovine trypsin was 3.7 x 10-8 M. The N-terminal sequence of PvTI, GDDVKSA-CCDTCLCTKSEPPTCRCVDV, showed high homology with other Bowman-Birk type inhibitors. PvTI exerted fungistatic effect on Fusarium moniliforme at concentration of 500 µg/mL.
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