α-galactosidase activity in ingested seeds and in the midgut ofDysdercus peruvianus (Hemiptera: Pyrrhocoridae)

Silva, Carlos P.; Terra, Walter R.

doi:10.1002/(sici)1520-6327(1997)34:4<443::aid-arch4>3.0.co;2-t

Cited by 19 publications

(12 citation statements)

References 41 publications

(59 reference statements)

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“…This enzyme can be found in the alimentary canal, salivary secretions of insects and hypopharyngeal glands of some insects, such as Apis mellifera (Baker & Lehner 1972;Terra et al 1996). So far, αglus have been isolated and characterized from many insects including Dysdercus peruvianus Guerin-meneville (Hemiptera: Pyrrhocoridae), Sitophilus zeamais Motschulsky (Coleoptera: Curculionidae), A. mellifera L. (Hymenoptera: Apidae), Drosophila melanogaster Meigen (Diptera: Drosophilidae), Glyphodes pyloalis Guenée (Lepidoptera: Pyralidae), Eurygaster integriceps Putton (Hemiptera: Scutelleridae) and Rhopalosiphum padi L. (Homoptera: Aphididae) (Huber & Mathison 1976;Tanimura et al 1979;Baker 1991;Silva & Terra 1997;Ghadamyari et al 2010;Seddigh et al 2012). In the digestive system of Xanthogaleruca luteola, the optimum activity of αglu was reported at pH 5 and temperature 60 • C (Sharifi et al 2011).…”

Section: Introductionmentioning

confidence: 99%

Structural and phylogenetic analysis of α-glucosidase protein in insects

Seddigh

Darabi

2015

Biologia

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α-Glucosidases (αglus) (EC 3.2.1.20) have been detected in a wide range of plants, animals and microorganisms and are described by their ability to catalyze the hydrolysis of 1,4-α-glucosidic linkages, releasing α-glucose. In this study, 96 αglu protein sequences from 33 organisms species including different insects species, plants (including thale cress and rice), mammals (including human and mouse) and Mycobacterium tuberculosis as a bacterium were aligned. Sequences were analyzed by computational tools to predict the protein properties, such as molecular mass, isoelectric point, signal peptide, conserved motifs, transmembrane domain and secondary structure. Drosophila melanogaster (GenBank Accession No.: NP 610382) was chosen as one of the representatives of insects for further analyses. The tertiary structure of representative samples were acquired using the tertiary structure of oligo-1,6-glucosidase from Bacillus cereus (Protein Data Bank code: 1UOK) as a template by Phyre2 server. Protein structure analysis revealed there is a high identity among insects and other organisms. There were some similar functional domains between D. melanogaster and M. tuberculosis. The modeled αglu has a typical spatial structure in insects and exhibits a high similarity with other organisms, especially Arabidopsis thaliana. Phylogenetic analysis indicated that D. melanogaster αglu has a close relationship with other αglus from different insect families. According to these results, αglu in insects should be evolved from a common ancestor.

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Section: Introductionmentioning

confidence: 99%

Structural and phylogenetic analysis of α-glucosidase protein in insects

Seddigh

Darabi

2015

Biologia

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“…and ), suggests that these enzymes are involved in the digestion of substrates other than galactosyl‐oligosaccharides. As suggested for the heteropteran D. peruvianus , glycoproteins, and glycolipids may be the most likely natural substrates for these enzymes (Silva and Terra, ). As observed in other insect species, in L. zonatus the activity of α‐galactosidases is lower than the activity of α‐glucosidases, but higher than the activity of β‐glucosidases (Table ), suggesting that starch and galactosyl oligosaccharides may be more important as nutrients than cellulose or hemicellulose.…”

Section: Discussionmentioning

confidence: 89%

DIGESTION IN ADULT FEMALES OF THE LEAF‐FOOTED BUG Leptoglossus zonatus (HEMIPTERA: COREIDAE) WITH EMPHASIS ON THE GLYCOSIDE HYDROLASES α‐AMYLASE, α‐GALACTOSIDASE, AND α‐GLUCOSIDASE

Rocha

Pinto

Samuels

et al. 2014

Arch Insect Biochem Physiol

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The leaffooted bug, Leptoglossus zonatus (Hemiptera: Coreidae) is an emerging pest of several crops around the World and up to now very little is known of its digestive system. In this article, glycoside hydrolase (carbohydrase) activities in the adult midgut cells and in the luminal contents of L. zonatus adult females were studied. The results showed the distribution of digestive carbohydrases in adults of this heteropteran species in the different intestinal compartments. Determination of the spatial distribution of α-glucosidase activity in L. zonatus midgut showed only one major molecular form, which was not equally distributed between soluble and membrane-bound isoforms, being more abundant as a membrane-bound enzyme. The majority of digestive carbohydrases were found in the soluble fractions. Activities against starch, maltose and the synthetic substrate NPαGlu were found to show the highest levels of activity, followed by enzymes active against galactosyl oligosaccharides. Based on ion-exchange chromatography elution profiles and banding patterns in mildly denaturing electrophoresis, both midgut α-amylases and α-galactosidases showed at least two isoforms. The data suggested that the majority of carbohydrases involved in initial digestion were present in the midgut lumen, whereas final digestion of starch and of galactosyl oligosaccharides takes place partially within the lumen and partially at the cell surface. The complex of carbohydrases here described was qualitatively appropriate for the digestion of free oligosaccharides and oligomaltodextrins released by α-amylases acting on maize seed starch granules.

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“…So far, α-glucosidases have been isolated and characterised from many insects including Dysdercus peruvianus (Hemiptera: Pyrrhocoridase), Pyrhocoridae zeamais (Coleoptera: Curculionidae), Apis mellifera (Hymenoptera: Apidae), Drosophila melanogaster (Diptera: Drosophilidae), and Glyphodes pyloalis (Lep. : Pyralidae) (Huber & Mathison 1976;Tanimura et al 1979;Baker 1991;Silva & Terra 1997;Ghadamyari et al 2010). β-Glucosidase hydrolyses β 1-4 linkages between two glucoses or glucose-substituted molecules (such as cellobiose) (Terra et al 1996).…”

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confidence: 74%

“…The ratio of β-glucosidase/β-galactosidase was reported as 88.5 in Rhynchosciara americana Wiedemann (Diptera: Sciaridae) (Terra et al 1979), 105 in Stomoxys calcitrans (Deloach & Spotes 1984), 58 in the midgut tissue of Rhodnius prolixus (Terra et al 1988), and 2.5 in C. maculates (Gatehouse et al 1985). Also, in D. peruvianus, the β-glucosidase/β-galactosidase ratio in the midgut tissue was 28.7, but in the whole midgut (epithelium plus luminal contents) the ratio was 3.0, suggesting a major contribution of β-galactosidase activity by the seed meal present in the gut lumen (Silva & Terra 1997). The ratios of α-glucosidase/α-galactosidase found in adults and the last larval instar of X. luteola were 7.5 and 3.5, respectively (unpublished data).…”

Section: Discussionmentioning

confidence: 99%

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

Riseh¹,

Ghadamyari²,

Motamediniya³

2012

Plant Prot. Sci.

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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.

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α-galactosidase activity in ingested seeds and in the midgut ofDysdercus peruvianus (Hemiptera: Pyrrhocoridae)

Cited by 19 publications

References 41 publications

Structural and phylogenetic analysis of α-glucosidase protein in insects

Structural and phylogenetic analysis of α-glucosidase protein in insects

DIGESTION IN ADULT FEMALES OF THE LEAF‐FOOTED BUG Leptoglossus zonatus (HEMIPTERA: COREIDAE) WITH EMPHASIS ON THE GLYCOSIDE HYDROLASES α‐AMYLASE, α‐GALACTOSIDASE, AND α‐GLUCOSIDASE

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

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