Examination of midgut luminal proteinase activities in six economically important insects

Expression profile of water-soluble proteinases during ontogenesis of Megachile rotundata: an electrophoretic investigation

“…This hypothesis is in agreement with data concerning the presence of several proteolytic activities with a digestive role at alkaline pH detectable in the midgut of several insects (Purcell et al, 1992;Walker et al, 1998;Jimenez and Gilliam, 1989). These data have been emphasized on the basis of observations concerning the digestion physiology in the bee S. bipunctata that involve aminopeptidase and trypsin enzyme (Schumaker et al, 1993).…”

“…As a consequence, a wide range of investigations have been focused on the characterisation and identification of different target proteinases in a variety of insect orders: Lepidoptera, such as Agrotis (Purcell et al, 1992), Cydia (Christeller et al, 1992), Spodoptera (Lee and Anstee, 1995), Lymantria (Valaitis, 1995), Heliothis (Johnston et al, 1995), Ostrinia (Bernardi et al, 1996), Bombyx (Nobuyasu and Yamashita, 1997), Sesamia (Novillo et al, 1999), Pieris (Broadway, 1995); in Coleoptera, such as Adalia (Murdock et al, 1987;Walker et al, 1998), Tenebrio (Dadd, 1956;Jang et al, 1998) and Tribolium (BlancoLabra et al, 1996); in Diptera, such as Aedes (Fisk, 1950) and Aenopheles (Berner et al, 1983;Vizioli et al, 2001); in Hemiptera, such as Dysdercus (Khan and Ford, 1962); and in Orthoptera, such as Locusta (Khan, 1963). The potential damage of protein-inhibitors on the digestive proteinases of beneficial insects has received less attention.…”

Purification and characterization of trypsin inhibitor from Cicer arietinum L. and its efficacy against Helicoverpa armigera

“…Compared to other varieties, P-256 exhibited maximum inhibition (66%) of HGP ( Table 1). The inhibition of HGP by trypsin inhibitor is in agreement with the earlier report that primary digestive enzymes of H. armigera larvae are predominantly serine proteinases of trypsin and chymotrypsin type, which are extra cellular and active at alkaline pH (Johnston et al, 1991;Purcell et al, 1992). Patankar et al (1999) showed a significant variation in the trypsin inhibitor (TI) and the Helicoverpa armigera gut proteinase inhibitor (HGPI) content in the seeds of eight chickpea cultivars.…”

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

“…Among them, the Kunitz trypsin inhibitor super family [23] has gained particular attention for its specific activity against trypsin-like serine proteinases, with no inhibition of other proteinase classes [24]. Furthermore, Kunitz trypsin inhibitors were capable of inhibiting the proteolytic activity of several lepidopterans, such as the black cutworm (Agrotis ipsilon), corn earworm (H. zea), tobacco budworm (Heliothis virescens), Western spruce budworm (Choristoneura occidentalis) [25] and coleopterans such as the cotton boll weevil (A. grandis) [10]. Several plants have been screened in order to isolate and characterize such proteinase inhibitors, among them the species Crotalaria pallida, which belongs to the Fabaceae family (Sub-family Faboideae), the members of which are herbs, shrubs and trees found in both temperate and tropical areas.…”