Screening and Purification of a Novel Trypsin Inhibitor from Prosopis juliflora Seeds with Activity Toward Pest Digestive Enzymes

Abstract

Several pests are capable of decreasing crop production causing severe economical and social losses. Aiming to find novel molecules that could impede the digestion process of different pests, a screening of alpha-amylase and trypsin-like proteinase inhibitors was carried out in Prosopis juliflora, showing the presence of both in dry seeds. Furthermore, a novel trypsin inhibitor, with molecular mass of 13,292 Da, was purified showing remarkable in vitro activity against T. castaneum and C. maculatus.

Purification, characterization and evaluation of insecticidal activity of trypsin inhibitor from Albizia lebbeck seeds

“…Till date trypsin inhibitors have been purified and characterized from a variety of plant sources (Macedo et al2000;Oliviera et al 2007;Kansal et al 2008;Rai et al 2008). The purified inhibitor protein was found to consist of a single polypeptide chain of 12,303 daltons as revealed by Native-PAGE and SDS-PAGE, which is consistent with the molecular masses of other trypsin inhibitors (Mizuta and Ventura 1976;Fook et al 2005;Sivakumar et al 2005). On the contrary trypsin inhibitor purified from A. kalkora seeds showed the presence of two disulfide linked polypeptide chains and a high molecular mass (Zhou et al 2008).…”

Negative Effects of a Nonhost Proteinase Inhibitor of ~19.8 kDa fromMadhuca indicaSeeds on Developmental Physiology ofHelicoverpa armigera(Hübner)

“…Inhibition of more than 80% of H. armigera proteinase activity has also been reported with nonhost PIs from bitter gourd [34]. Similarly inhibitors isolated from the seeds of Prosophis juliflora exhibited 83% inhibition against H. armigera midgut trypsin-like activity [35]. The IC 50 of MiTI for trypsin like midgut proteinases was 1.75  μ g/mL, which was less effective than standard SBTI (0.13  μ g/mL) [31, 32].…”