Biochemical characterisation of α- and β-glucosidases and α- and β-galactosidases from red palm weevil, Rhynchophorus ferrugineus (Olivier) (Col.: Curculionide)

Abstract

Riseh N.S., Ghadamyari M., Motamediniya B. (2012): Biochemical characterisation of α-and β-glucosidases and α-and β-galactosidases from red palm weevil, Rhynchophorus ferrugineus (Olivier) (Col.: Curculionide). Plant Protect. Sci., 48: 85-93.The red palm weevil, Rhynchophorus ferrugineus (Olivier), is one of the most destructive pests of palm trees in the southeast of Iran. Digestion in the alimentary canal of the red palm weevil is facilitated by some carbohydrases. Results of the in vitro studies indicated the presence of α-and β-glucosidases and α-and β-galactosidases in the digestive system and haemolymph of this pest. In the digestive system of females, the activities of α-glucosidase and β-galactosidase were higher than those of β-glucosidase and α-galactosidase. Also, the specific activity of α-and β-glucosidases and α-and β-galactosidases in the female digestive system was much higher than that in larvae. Results showed that the highest activities of α-and β-glucosidases were at pH 5 and of α-and β-galactosidases at pH 4. The R. ferrugineus α-and β-glucosidases and α-and β-galactosidases have an optimum temperature activity at 50, 50-60, 40-60, and 40°C, respectively. A zymogram pattern in the native gel revealed that R. ferrugineus α-and β-glucosidases and α-and β-galactosidases in the digestive system showed 2, 3, 1 and 1 major bands, respectively. The activity of α-glucosidase in the digestive system of larvae and female adults was higher than that of the other carbohydrases. Therefore, it is the most important subject for further study and design of a new approach to the control of this pest using carbohydrase inhibitors.

Enzymes of Earthworm as Indicators of Pesticide Pollution in Soil

“…To assess toxicity of any xenobiotics including the pesticides and the heavy metals as well as the diagnosis of cell, tissue and organ damage, LDH has been widely exploited in the vertebrates. However, in the invertebrate toxicity tests, the potential of this enzyme as indicator is rarely explored [65] [66] [67].…”

Biochemical characterization of α- and β-glucosidases in alimentary canal, salivary glands and haemolymph of the rice green caterpillar, Naranga aenescens M. (Lepidoptera: Noctuidae)

“…: Pyralidae) and midgut of Xanthogaleruca luteola Müll. (Col.: Chrysomelidae), Osphrantria coerulescens (Col.: Cerambycidae), Rhynchophorus ferrugineus Olivieri (Col.: Curculionidae) (Huber & Mathison 1976;Ghadamyari et al 2010;Sharifi et al 2011;Riseh et al 2012). Although α-glucosidases are found in four families of glycoside hydrolases (GHs): GH4, GH13, GH31, and GH97, based on CAZy (Carbohydrate-Active enZymes) (Cantarel et al 2009) classification system, insect α-glucosidases are found exclusively in family GH13 (Gabrisko & Janecek 2011).…”

“…In insects, hemicelluloses and cellulose can be hydrolyzed enzymatically by some specific enzymes to diand oligo-β-saccharides which digestive β-glucosidases Biochemical characterization of α-and β-glucosidases in Naranga aenescens 1187 are important for their hydrolysis (Terra & Ferreira 1994). Due to involvement of β-glucosidases in interactions between insect and host plant, β-digestive glucosidases have been studied in many insect species from different orders (Ferreira & Terra 1983;Santos & Terra 1985;Sharifi et al 2011;Riseh et al 2012). β-Glucosidases are reported in midgut and salivary glands of lepidopteran insect, such as G. pyloalis , Thaumetopoea pityocampa Schiffermuller (Lep.…”

“…Zymogram analyses were carried out using non-denaturing polyacrylamide gel electrophoresis (PAGE) based on the method of Davis (1964) modified by Riseh et al (2012). The enzyme samples were mixed with non-denaturing sample buffer (without mercaptoethanol) and applied onto 10% (w/v) polyacrylamide gel.…”

“…• C (Huber & Mathison 1976;Ghadamyari et al 2010;Riseh et al 2012). Franzl et al (1989) reported a temperature optimum for Z. trifolii β-glucosidase at 40…”