Effects of cotton condensed tannin on feeding and digestion in the cotton pest, Heliothis zea

Klocke, James A.; Chan, Bock G.

doi:10.1016/0022-1910(82)90106-8

Cited by 80 publications

(50 citation statements)

References 19 publications

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“…For long-term tests, consumption, growth, and digestive efficiency can all be measured separately (chapter 6, this volume). Performing both short-and long-term tests provides the most information (Klocke and Chan, 1982;Lewis, 1984;Lewis and Bernays, 1985) as data on changes in behavior through lengthy exposure to a chemical may be useful.…”

Section: Short-and Long-term Testsmentioning

confidence: 99%

“…A dome of agar is covered by a wax coating; test and control chemicals can be added to both agar and wax. Diet, in cups or discs, has been used to test chemicals against gypsy moth (Trial and Dimond, 1979;Doskotch et al, 1980), cotton bollworm (Klocke and Chan, 1982), armyworm (Meisner et al, 1982), and other lepidopteran larvae (Kaethler et al, 1982). Freedman et al (1979) found that larvae penetrating into the diet received insufficient exposure to the test chemical applied to the surface only, and suggest mixing chemical throughout.…”

Section: Artificial Substratesmentioning

confidence: 99%

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Assays for Insect Feeding

Lewis¹,

Emden

1986

Springer Series in Experimental Entomology

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Section: Short-and Long-term Testsmentioning

confidence: 99%

Section: Artificial Substratesmentioning

confidence: 99%

Assays for Insect Feeding

Lewis¹,

Emden

1986

Springer Series in Experimental Entomology

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“…With the substrate BApNA, it was found that the optimal pH for the purified protease activity from third instar larvae of N. aenescens is alkaline (pH 10). An optimal alkaline pH for protease activity has been demonstrated for lepidopteran digestive enzymes in other insects, such as Spodoptera littoralis Fabricius (Lepidoptera: Noctuidae), pH 11.0 (Ishaaya et al, 1971), S. litura Fabricius (Lepidoptera: Noctuidae), pH 9.0, 10.5, and 11.0 (Ahmad et al, 1976(Ahmad et al, , 1980, Heloithis zea Fabricius (Lepidoptera: Noctuidae), pH 11.0 (Kloke and Chan, 1982), G. mellonella L. (Lepidoptera: Pyralidae), pH 10.5 and 11.2 (Hamed and Attias, 1987), Helicoverpa armigera Hubner (Lepidoptera: Noctuidae), pH 9.5 and 10.0 (Johnston et al, 1991), Phtorimaea opercula Hubner (Lepidoptera: Noctuidae), pH49.0 (Christeller et al, 1992), Manduca sexta L. (Lepidoptera: Noctuidae), pH 8.5 (Samuels et al, 1993), Heliothis virescens Fabricius (Lepidoptera: Noctuidae), pH 10.0-11.0 (Johnston et al, 1995), Spilosoma obliqua (Lepidoptera: Arctiidae) (Anwar and Saleemudin, 2002), and Mamestra brassicae (Lepidoptera: Noctuidae) has a continuous increase in activity from 7 to 11.5 with a peak at 11.5 (Chougule et al, 2008). Our results correspond with these studies and suggest an alkaline pH value in the midgut that regulates serine proteolytic activity of N. aenescens.…”

Section: Discussionmentioning

confidence: 98%

A trypsin‐like protease in rice green semi‐looper, Naranga aenescens moore (lepidoptera: Noctuidae): purification and characterization

Zibaee

Bandani

Fazeli‐Dinan

et al. 2011

Arch Insect Biochem Physiol

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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 instar larvae of N. aenescens was achieved by gel filtration and anion exchange chromatography. After the final purification step, the enzyme was purified 9.62-fold with a recovery of 16.1% and a specific activity of 4.12 U/mg protein and a molecular mass of approximately 88.5 kDa. Biochemical characterization indicated that the purified protease had highest activity at pH 10 and 30°C and was stable for up to 6 h under those conditions. Divalent cations, especially Ca2+, Mg2+, and Cu2+, increased the enzyme activity and synthetic inhibitors that target trypsin-like activity caused a significant reduction in caseinolytic activity. These data may be used to develop inhibitors that decrease the damage of N. aenescens to rice cultivars in the field.

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“…It has been reported previously that a large number of proteases present in insect guts have alkaline pH optima. These include those from S. littoralis, pH 11 (Ishaaya et al 1971), S. litura, pH 9, 10.5 and 11.0 (Ahmad et al 1976(Ahmad et al , 1980, Heloithis zea, pH 11 (Kloke & Chan 1982), G. mellonella, pH 10.5 and 11.2 (Hamed & Attias 1987), P. rapae, pH 8 (Broadway 1989), Helicoverpa armigera, pH 9.5 and 10 (Johnston et al 1991), Phtorimaea operculla, pH > 9.0 (Christeller et al 1992), Manduca sexta, pH 8.5 (Samuels et al 1993), Helothis virescens, pH 10.0-11.0 (Johnston et al 1995), Lacanobia oleracea pH < 11 (Gatehouse et al 1999) and Mamestra brassicae, pH 11 (Chougule et al 2008). The results of optimal pH in the current study confirmed Terra and Ferreira (1994) on attribution of the high pH of the lepidopteran gut to an adaptation of leaf-eating lepidopteran ancestors for extracting hemicellulose from plant cell walls.…”

Section: Discussionmentioning

confidence: 99%

Digestive enzymes of large cabbage white butterfly,Pieris brassicaeL. (Lepidoptera: Pieridae) from developmental and site of activity perspectives

Zibaee

2012

Italian Journal of Zoology

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Investigation of digestive enzymes in the alimentary tract of insects is very important for knowledge on physiology of nutrition. The overall results of this study showed the presence of the majority of digestive enzymes including α-amylase, α-and β-glucosidase and galactosidase, lipases and proteases in the midgut of Pieris brassicae. It was found that the fourth and fifth instar larvae had the highest enzymatic activity, but the obvious differences were found in the cases of sites of enzyme activity known as soluble and membrane-bound fractions. The highest enzymatic activities in the soluble fractions were found in cases of α-amylase, lipases and proteinases such as trypsin-like, chymotrypsin-like and elastase. In contrast, glycosidases and exopeptidases (amino and carboxypeptidases) demonstrated the highest enzymatic activity in the membrane-bound fractions. However, no enzymatic activity was observed on cysteine protease as a type of proteinases. By using line regression, parameter β (slope) showed larval dependency on enzymes along with developmental and feeding processes. It was found that α-glucosidase had the highest slope and the membrane-bound fraction of general proteases had the lowest, showing high and low dependencies of larvae to α-glucosidase and exopeptidases, respectively, in addition to second priority on β-glucosidase and α-amylase. Optimal pHs of soluble and membrane-bound α-amylase were found at 9 while all assayed glycosidases had the highest activity at pH 8 for both fractions. Soluble fraction of lipase had the highest enzymatic activity at pH 8 in comparison with membrane-bound fraction at pH 10. The soluble fraction showed the highest proteolytic activity at pH 9, while the highest proteolytic activity was observed at pH 8 in the case of the membrane-bound one.

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Effects of cotton condensed tannin on feeding and digestion in the cotton pest, Heliothis zea

Cited by 80 publications

References 19 publications

Assays for Insect Feeding

Assays for Insect Feeding

A trypsin‐like protease in rice green semi‐looper, Naranga aenescens moore (lepidoptera: Noctuidae): purification and characterization

Digestive enzymes of large cabbage white butterfly,Pieris brassicaeL. (Lepidoptera: Pieridae) from developmental and site of activity perspectives

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