Alkaline protease in the larvae of the army worm, Spodoptera litura

Ahmad, Zubair; Saleemuddin, M.; Siddiqi, Majid

doi:10.1016/0020-1790(76)90075-5

Cited by 27 publications

(9 citation statements)

References 10 publications

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“…However, the fifth instar larvae were selected for further study because of the availability for larger amounts of enzyme despite the somewhat lower specific activity. Such age‐dependent alterations of the proteolytic enzymes have been found in the larvae of Lygus disponsi (H ORI , 1973),and in Spodoptera litura (A HMAD et al., 1976). Evidently other digestive enzymes also exhibited similar alterations as has been shown in some recent studies (C HRISTOPHER and M ATHAVAN , 1985) with amylase and invertase in the larvae of Catopsila crocale .…”

Section: Resultsmentioning

confidence: 82%

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Regulation of digestive proteolytic activity in the larvae of Spilosoma obliqua (Lep., Arctiidae)

Anwar

Saleemuddin

2001

J Applied Entomology

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Proteolytic activity from the guts of the lepidopteran larvae Spilosoma obliqua was studied in relation to the developmental stages. The activity was found to increase with the advancement in the age of larvae and decreased with the onset of pupation. Starvation of fifth instar larvae, which exhibited maximum proteolytic activity, led to an increase at 8 h and declined further. There seems to be a possible relationship between the availability of the food and secretion of the enzymatic activity. The optimum pH and temperature for the gut protease was 11.0 and 50°C, respectively. Incubation of the gut protease for 24 h at 37°C led to a decrease in 52% of the activity, whereas there was a decrease of 17% in the activity at 4°C. No evidence could be found for the existence of the protease as an inactive precursor. The alkaline properties of the digestive protease seem to have all the potential to be exploited commercially as a additive in various biological formulations.

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Section: Resultsmentioning

confidence: 82%

“…A lack of significant increase in the enzymatic activity was taken as the indication of lack of zymogen form of the enzyme. However other workers have also failed to demonstrate the existence of the zymogen form of proteases among lepidopterans (A HMAD et al., 1976).…”

Section: Resultsmentioning

confidence: 99%

Regulation of digestive proteolytic activity in the larvae of Spilosoma obliqua (Lep., Arctiidae)

Anwar

Saleemuddin

2001

J Applied Entomology

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“…This was followed by a rapid decrease in activity at pH 12.0. Like most of the proteases from other lepidopterans (Ahmad et al, 1976Christeller et al, 1992), the alkaline protease from S. obliqua appears to have a pH optimum of 11.0. In a separate study, Peterson et al (1995) suggested that the presence of the large number of arginine residues in Manduca chymotrypsin sequence may be responsible for the stabilization of the enzymes at highly alkaline pH.…”

Section: Enzymatic Propertiesmentioning

confidence: 95%

Purification and characterization of a digestive alkaline protease from the larvae of Spilosoma obliqua

Anwar¹,

Saleemuddin²

2002

Arch Insect Biochem Physiol

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A digestive protease from Spilosoma obliqua (Lepidoptera: Arctiidae) fifth instar larval guts was purified and characterized. The protease was purified using ammonium sulfate fractionation, ion-exchange chromatography, and hemoglobin-sepharose affinity chromatography. The purification procedure resulted in a 37-fold increase in the specific activity of the protease. Protease thus obtained was found to be electrophoretically pure under native and denaturing conditions. The purified protease had a molecular mass of 90 kDa as determined by gel filtration, and a pH optimum of 11.0. The purified protease optimally hydrolyzed casein at 50 degrees C. A Km of 2 x10(-6) M was obtained using BApNA as a substrate for the purified alkaline protease. The ability of S. obliqua protease and bovine trypsin to hydrolyze various synthetic substrates (BApNA, BAEE, and BAME), and the inhibition patterns of S. obliqua and bovine trypsin with "classical" trypsin inhibitors are also reported.

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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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Alkaline protease in the larvae of the army worm, Spodoptera litura

Cited by 27 publications

References 10 publications

Regulation of digestive proteolytic activity in the larvae of Spilosoma obliqua (Lep., Arctiidae)

Regulation of digestive proteolytic activity in the larvae of Spilosoma obliqua (Lep., Arctiidae)

Purification and characterization of a digestive alkaline protease from the larvae of Spilosoma obliqua

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

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