Purification and characterization of three β-glycosidases from midgut of the sugar cane borer, Diatraea saccharalis

Insect Biochemistry and Molecular Biology

Volumn 33, Issue 1, 2003, Pages 81-92

  Azevedo, Tamara R ^a   Terra, Walter R ^a   Ferreira, Clélia ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Glycosidase; Diatraea saccharalis; Hydrolyse prunasin

Indexed keywords

GLYCOSIDASE; ISOENZYME;

ANIMAL; ARTICLE; BINDING SITE; ENZYMOLOGY; GEL CHROMATOGRAPHY; ISOELECTRIC FOCUSING; ISOLATION AND PURIFICATION; KINETICS; LEPIDOPTERA; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ANIMALS; BINDING SITES; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSIDE HYDROLASES; ISOELECTRIC FOCUSING; ISOENZYMES; KINETICS; LEPIDOPTERA;

ARUNDINARIA; COLEOPTERA; DIATRAEA; DIATRAEA SACCHARALIS; LEPIDOPTERA; PYRALIDAE; SACCHARUM; TENEBRIO MOLITOR;

EID: 0037211714     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(02)00179-0     Document Type: Article

References (27)

1. Baker, J.E., Woo, S.M., 1992. β-Glucosidases in the rice weevil, Sitophilus oryzae: Purification, properties, and activity levels in wheat-and legume-feeding strains. Insect Biochem. Mol. Biol 22, 495-504.
2. Blum, H., Beier, H., Gross, H.J., 1987. Improved silver staining of plant proteins: RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
3. Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem 72, 248-254.
4. Dahlqvist, A., 1968. Assay of intestinal disaccharides. Anal. Biochem 22, 99-107.
5. Davies, G.J., Wilson, K.S., Henrisat, B., 1997. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J 321, 557-559.
6. Desroches, P., Mandon, N., Beaehr, J.C., Huignard, J., 1997. Mediation of host-plant use by a glucoside in Callosobruchus maculatus F. (Coleoptera: Bruchidae). J. Insect Physiol. 43, 439-446.
7. Ferreira, C., Terra, W.R., 1983. Physical and kinetic properties of a plasma membrane bound b-D-glucosidase (cellobiase) from midgut cells of an insect (Rhynchosciara americana larva). Biochem. J 213, 43-51.
8. Ferreira, C., Capella, C.N., Sitnik, R., Terra, W.R., 1994. Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae. Comp. Biochem. Physiol.A 107, 631-640.
9. Ferreira, C., Parra, J.R.P., Terra, W.R., 1997. The effect of dietary plant glycosides in larval midgut β-glycosidases from Spodoptera frugiperda and Diatraea saccharalis. Insect Biochem. Mol. Biol. 27, 55-59.
10. Ferreira, C., Torres, B.B., Terra, W.R., 1998. Substrate specificities of midgut β-glycosidases from insects of different orders. Comp. Biochem. Physiol. 119B, 219-225.
11. Ferreira, A.H.P., Marana, S., Terra, W.R., Ferreira, C., 2001. Purification, sequencing, and properties of a β-glycosidase purified from midgut lumen of Tenebrio molitor (Coleoptera) larvae. Insect Biochem. Mol. Biol. 31, 1065-1076.
12. Ferreira, A.H.P., Terra, W.R., Ferreira, C., Characterization of a β-Glycosidase Highly Active on Disaccharides and of a β-Galactosidase from Tenebrio Molitor Midgut Lumen, 2002, submitted for publication.
13. Manchenko, G.P., 1994. Handbook of Detection of Enzymes on Electrophoretic Gels, CRC Press, Boca Raton, FL, p. 226.
14. Marana, S.R., Terra, W.R., Ferreira, C., 1995. Midgut β-D-glucosidases from Abracris flavolineata (Orthoptera: Acrididae): Physical properties, substrate specificities, and function. Insect Biochem. Mol. Biol. 25, 835-843.
15. Marana, S.R., Terra, W.R., Ferreira, C., 2000. Purification and properties of a β-glycosidase purified from midgut cells of Spodoptera frugiperda (Lepidoptera) larvae. Insect Biochem. Mol. Biol. 30, 1139-1146.
16. Marana, S.R., Jacobs-Lorena, M., Terra, W.R., Ferreira, C.F., 2001. Amino acid residues involved in substrate binding and catalysis in an insect digestive β-glycosidase. Biochem. Biophys. Acta 1545, 41-52.
17. Martin, R.G., Ames, B.N., 1961. A method for determining the sedimentation behavior of enzymes: Application to protein mixtures. J. Biol. Chem. 236, 1372-1379.
18. Nakano, M., Sacktor, B., 1984. Renal trehalase: Two subsites at the substrate-binding site. Biochim. Biophys. Acta. 791, 45-49.
19. Parra, J.R.P., Mishfeldt, L.J., 1992. Comparison of artificial diets for rearing the sugarcane borer, In: Anderson, T.E., Leppla, N.C., (Eds.), Advances in Insect Rearing for Research and Pest Management, Westview Press, Boulder, CO.
20. Santos, C.D., Terra, W.R., 1985. Physical properties, substrate specificities and a probable mechanism for a b-D-glicosidase (cellobiase) from midgut cells of the cassava hornworm (Erinnyis ello). Biochim. Biophys. Acta 831, 179-185.
21. Segel, I.H., 1975. Enzyme Kinetics. Wiley, New York.
22. Sierks, M.R., Bock, K., Refn, S., Svensson, B., 1992. Active site similarities of glucose dehydrogenase, glucose oxidase, and glucoamylase probed by deoxygenated substrates. Biochemistry 31, 8972-8977.
23. Terra, W.R., Ferreira, C., de Bianchi, A.G., 1979. Distribution of digestive enzymes among the endo- and ectoperitrophic spaces and midgut cells of Rhynchosciara americana and its physiological significance. J. Insect Physiol. 25, 487-494.
24. Terra, W.R., Valentin, A., Santos, C.D., 1987. Utilization of sugars, hemicellulose, starch, protein, fat and minerals by Erinnyis ello larvae and the digestive role of their midgut hydrolases. Insect Biochem. 17, 1143-1147.
25. Van Beers, E.H., Büller, A., Grand, R.J., Einerhand, A.W.C., Decker, J., 1995. Intestinal brush border glycohydrolases: Structure, function, and development. Critical Rev. Biochem. Molec. Biol. 30, 197-262.
26. White, A., Rose, D.R., 1997. Mechanism of catalysis by retaining β-glycosyl hydrolases. Curr. Opin. Struct. Biol. 7, 645-651.
27. Withers, S.G., Rupitz, K., 1990. Measurement of active-site homology between potato and rabbit muscle α-glucan phosphorylases through use of a free energy relationship. Biochemistry 29, 6405-6409.