2011
DOI: 10.1002/arch.20435
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A trypsin‐like protease in rice green semi‐looper, Naranga aenescens moore (lepidoptera: Noctuidae): purification and characterization

Abstract: The rice green semi looper, Naranga aenescens Moore (Lepidoptera: Noctuidae) causes severe damage to rice fields in Eastern Asia and Middle East. We demonstrate that two types of serine proteases are active in the midgut of the third instar larvae of N. aenescens, but trypsin-like proteases are considerably more active than chymotrypsin-like proteases. To develop better control strategies, purification and biochemical characterization of a major trypsin-like digestive protease from the midgut of the third inst… Show more

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Cited by 18 publications
(20 citation statements)
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“…(2008) found pH 8.0–10.5 as optimal pH for proteolytic activity in the larval midgut of Achaea janata L. (Lepidoptera: Noctuidae). Zibaee et al . (2011) demonstrated pH 10.0 for trypsin‐like and pH 9.0–10.0 for chymotrypsin‐like proteinases of Naranga aenescens Moore (Lepidoptera: Noctuidae).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…(2008) found pH 8.0–10.5 as optimal pH for proteolytic activity in the larval midgut of Achaea janata L. (Lepidoptera: Noctuidae). Zibaee et al . (2011) demonstrated pH 10.0 for trypsin‐like and pH 9.0–10.0 for chymotrypsin‐like proteinases of Naranga aenescens Moore (Lepidoptera: Noctuidae).…”
Section: Resultsmentioning
confidence: 99%
“…Homogenates were separately transferred to 1.5‐mL centrifuge tubes and centrifuged at 20 000 g for 20 min at 4°C. The supernatants were pooled and stored at −20°C for subsequent analyses (Zibaee et al . 2011).…”
Section: Methodsmentioning
confidence: 99%
“…For example, Mg 2ϩ increases trypsin-like protease activity in the midgut of the rice green semilooper, Naranga aenescens Moore (Zibaee et al 2011). Additionally, the population size of the root weevil, Diaprepes abbreviatus (L), is positively related to the Mg concentration in the soil (Li et al 2007).…”
Section: Discussionmentioning
confidence: 96%
“…For example, the salivary gland proteinases involved in extraoral digestion in Heteroptera exhibit a low temperature optimum (Oliveira et al., ; Zibaee et al., ). Similarly, among‐ and within‐species differences in the efficiency of substrate cleavage and sensitivity to TLCK (Novillo et al., ; Lam et al., ; Oliveira et al., ; Zibaee et al., ) might reflect adaptation to a specific food. For instance, trypsins in some hematophagous insects do not hydrolize B‐R‐pNA and require longer peptide chains (Dametto et al., ; Lu et al., ).…”
Section: Structural Diversity Of Insect Digestive Trypsinsmentioning
confidence: 99%