Determination of K, Ca, Fe and Ni in Leptinotarsa decemlineata (Say) by EDXRF spectroscopy

2006 ◽  
Vol 97 (1) ◽  
pp. 75-80 ◽  
Author(s):  
İrfan Aslan ◽  
Gökhan Budak ◽  
Abdulhalik Karabulut ◽  
Engin Tıraşogˇlu
Keyword(s):  
Leptinotarsa Decemlineata ◽  
Leptinotarsa Decemlineata Say

Involvement of methoprene-tolerant (Met) in the determination of the final body size in Leptinotarsa decemlineata (Say) larvae

2018 ◽  
Vol 97 ◽  
pp. 1-9 ◽  
Author(s):  
Qing-Wei Meng ◽  
Qing-Yu Xu ◽  
Pan Deng ◽  
Kai-Yun Fu ◽  
Wen-Chao Guo ◽  
...  
Keyword(s):  
Body Size ◽  
Leptinotarsa Decemlineata ◽  
Leptinotarsa Decemlineata Say

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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