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Purification and Biochemical Characterization of a Protease Inhibitor II Family from Jalapeño Pepper (Capsicum annuum L.)

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DOI: 10.4236/abb.2014.57078    4,034 Downloads   5,349 Views Citations

ABSTRACT

Capsicum annuum L. was initially domesticated in Mexico and northern Central America, and represented an ancient Neotropical plant food complex. The purpose of this paper is to report the isolation and purification of a novo-member of a protease inhibitor from jalapeño pepper (Capsicum annuum L.) (PIJP). The molecular weight of PIJP inhibitor is 5.95 kDa with 56 amino acids and 6 Cys residues with high inhibitory activity to trypsin with a Ki value of 95 nM. This inhibitor according to the alignment with homologous from NCBI and Pfam databases is a member of proteinase inhibitors II. It is worthwhile to mention a major compositional difference between the proteinase inhibitor II families which have 8 Cys residues. PIJP is the first purified proteinase inhibitor, member of this family with only 6 Cys residues.

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Carrillo-Montes, J. , Arreguín-Espinosa, R. , Muñoz-Sánchez, J. and Soriano-García, M. (2014) Purification and Biochemical Characterization of a Protease Inhibitor II Family from Jalapeño Pepper (Capsicum annuum L.). Advances in Bioscience and Biotechnology, 5, 661-668. doi: 10.4236/abb.2014.57078.

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