scholarly journals Inhibitory effects of barley and wheat seed protein on digestive α-amylase and general protease activity of Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae)

2015 ◽  
Vol 39 (4) ◽  
Author(s):  
Shabnam Ashouri ◽  
Reza Farshbaf Pourabad ◽  
Alireza Bandani ◽  
Mehdi Dastranj
Keyword(s):  
Leptinotarsa Decemlineata ◽  
Protease Activity ◽  
Seed Protein ◽  
Wheat Seed ◽  
Inhibitory Effects ◽  
Leptinotarsa Decemlineata Say

scholarly journals Effect of Plant Growth Regulators on Protease Activity in Forest Floor of Norway Spruce Stand

Forests ◽  
2021 ◽  
Vol 12 (6) ◽  
pp. 665
Author(s):  
Ladislav Holik ◽  
Jiří Volánek ◽  
Valerie Vranová
Keyword(s):  
Organic Matter ◽  
Proteolytic Activity ◽  
Protease Activity ◽  
Forest Floor ◽  
Soil Microbial Activity ◽  
Inhibitory Effects ◽  
Chlorocholine Chloride ◽  
Soil Microbial ◽  
Native Soil ◽  
Transformation Processes

Soil proteases are involved in organic matter transformation processes and, thus, influence ecosystem nutrient turnovers. Phytohormones, similarly to proteases, are synthesized and secreted into soil by fungi and microorganisms, and regulate plant rhizosphere activity. The aim of this study was to determine the effect of auxins, cytokinins, ethephon, and chlorocholine chloride on spruce forest floor protease activity. It was concluded that the presence of auxins stimulated native proteolytic activity, specifically synthetic auxin 2-naphthoxyacetic acid (16% increase at added quantity of 5 μg) and naturally occurring indole-3-acetic acid (18%, 5 μg). On the contrary, cytokinins, ethephon and chlorocholine chloride inhibited native soil protease activity, where ethephon (36% decrease at 50 μg) and chlorocholine chloride (34%, 100 μg) showed the highest inhibitory effects. It was concluded that negative phytohormonal effects on native proteolytic activity may slow down organic matter decomposition rates and hence complicate plant nutrition. The study enhances the understanding of rhizosphere exudate effects on soil microbial activity and soil nitrogen cycle.

scholarly journals Biochemical characterisation of α-glucosidase and β-glucosidase in the alimentary canal of larval Leptinotarsa decemlineata SAY, 1824 (Coleoptera: Chrysomelidae)

2014 ◽  
Vol 83 (4) ◽  
pp. 281-294 ◽  
Author(s):  
Majid Kazzazi ◽  
Fahimeh Dehghanikhah ◽  
Hossein Madadi ◽  
Vahid Hossseininaveh
Keyword(s):  
Incubation Time ◽  
Leptinotarsa Decemlineata ◽  
Digestive Enzymes ◽  
Specific Activity ◽  
Inhibitory Effect ◽  
Maximum Activity ◽  
Pest Population ◽  
Biochemical Characterisation ◽  
Leptinotarsa Decemlineata Say ◽  
Environmentally Safe

ABSTRACT Host plant resistance is an environmentally safe method used for reducing a pest population. Basically, when developing resistant cultivars one needs to study the biochemical characteristics of the digestive enzymes in the insect’s midgut. In this study, the activities of α- and β-glucosidase were determined from Leptinotarsa decemlineata midgut using p-nitrophenyl-α-Dglucopyranoside and p-nitrophenyl-β-D-glucopyranoside as substrates respectively. The results showed that the specific activity of α- and β-glucosidase from 4th instar larvae midguts of L. decemlineata were 5.14 and 5.48 Umg-1 protein respectively. The activity of α-glucosidase was optimal at pH 4, whereas the maximum activity of β-glucosidase in the midgut of L. decemlineata occurred at pH 4-5.5. Both enzymes were stable at pH 3-8 over an incubation time of 8 hours. The respective activities of α- and β-glucosidase were at their highest at 45 °C and 50 °C, but they were not stable at 50 °C during an incubation time of 8 days. Furthermore, our data showed that MgCl2, Tris and urea have a moderate but SDS a severe inhibitory effect on enzyme activity. Biochemical characterisation revealed one and three bands of α- and β-glucosidase activities in the midgut of L. decemlineata respectively.

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