TITLE:
Purification and Biochemical Characterization of a Protease Inhibitor II Family from Jalapeño Pepper (Capsicum annuum L.)
AUTHORS:
Juan Pablo Carrillo-Montes, Roberto Arreguín-Espinosa, José Luis Muñoz-Sánchez, Manuel Soriano-García
KEYWORDS:
Protease Inhibitory Activity, Protease Inhibitor, Protein Purification, Jalapeño Pepper, Capsicum annuum L.
JOURNAL NAME:
Advances in Bioscience and Biotechnology,
Vol.5 No.7,
June
27,
2014
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.