A Trypsin Inhibitor from Sapindus saponaria L. Seeds: Purification, Characterization, and Activity Towards Pest Insect Digestive Enzyme
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2011-01-01
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Macedo, Maria Ligia R.
Diz Filho, Eduardo B. S.
Freire, Mariadas Gracas M.
Oliva, Maria Luiza V. [UNIFESP]
Sumikawa, Joana T. [UNIFESP]
Toyama, Marcos H.
Marangoni, Sergio
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The present paper describes the purification, characterization and determination of the partial primary structure of the first trypsin inhibitor isolated from the family Sapindaceae. A highly stable, potent trypsin inhibitor (SSTI) was purified to homogeneity. SDS-PAGE analysis revealed that the protein consists of a two-polypeptide chain with molecular masses of approximately 15 and 3 kDa. the purified inhibitor inhibited bovine trypsin at a 1:1 M ratio. Kinetic analysis revealed that the protein is a competitive inhibitor with an equilibrium dissociation constant of 10(-9) M for trypsin. the partial NH(2)- terminal sequence of 36 amino acids in SSTI indicates homology with other members of the trypsin-inhibitor family from different sources. This inhibitor is highly stable in the presence of denaturing agents. SSTI showed significant inhibitory activity against trypsin-like proteases present in the larval midgut on Anagasta kuehniella, Corcyra cephalonica, Diatreae saccharalis and Anticarsia gemmatalis.
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Protein Journal. New York: Springer, v. 30, n. 1, p. 9-19, 2011.