Hostname: page-component-8448b6f56d-xtgtn Total loading time: 0 Render date: 2024-04-24T01:46:21.832Z Has data issue: false hasContentIssue false
  • English
  • Français

Digestive α-amylases from Tecia solanivora larvae (Lepidoptera: Gelechiidae): response to pH, temperature and plant amylase inhibitors

Published online by Cambridge University Press:  01 July 2008

A. Valencia-Jiménez ,
J.W. Arboleda V ,
A. López Ávila  and
M.F. Grossi-de-Sá
A. Valencia-Jiménez*
Affiliation:
Embrapa Recursos Genéticos e Biotecnologia, PqEB, W5 Norte Final, Brasília – DF, 70770-900, Brasil Departamento de Biologia Celular, Universidade de Brasília, Asa Norte, Brasília – DF, 70910-900, Brasil Facultad de Ciencias Agropecuarias, Departamento de Fitotecnia, Universidad de Caldas, Calle 65#26-10, Manizales, Colombia
J.W. Arboleda V
Affiliation:
Embrapa Recursos Genéticos e Biotecnologia, PqEB, W5 Norte Final, Brasília – DF, 70770-900, Brasil Departamento de Biologia Celular, Universidade de Brasília, Asa Norte, Brasília – DF, 70910-900, Brasil
A. López Ávila
Affiliation:
Corpoica, Tibaitatá, Bogotá, Colombia
M.F. Grossi-de-Sá
Affiliation:
Embrapa Recursos Genéticos e Biotecnologia, PqEB, W5 Norte Final, Brasília – DF, 70770-900, Brasil
*
*Author for correspondence Fax: +57-68-781545 E-mail: avalbioquimica@yahoo.com
Get access Rights & Permissions [Opens in a new window]

Abstract

The biochemical properties of the digestive alpha-amylase from Tecia solanivora larvae, an important and invasive insect pest of potato (Solanum tuberosum), were studied. This insect has three major digestive α-amylases with isoelectric points 5.30, 5.70 and 5.98, respectively, which were separated using native and isoelectric focusing gels. The alpha-amylase activity has an optimum pH between 7.0 and 10.0 with a peak at pH 9.0. The enzymes are stable when heated to 50°C and were inhibited by proteinaceous inhibitors from Phaseolus coccineus (70% inhibition) and P. vulgaris cv. Radical (87% inhibition) at pH 6.0. The inhibitors present in an amaranth hybrid inhibited 80% of the activity at pH 9.0. The results show that the alpha-amylase inhibitor from amaranth seeds may be a better candidate to make genetically-modified potatoes resistant to this insect than inhibitors from common bean seeds.

Keywords

α-AmylaseTecia solanivoraamylase inhibitorspotato
Type
Research Paper
Information
Bulletin of Entomological Research , Volume 98 , Issue 6 , December 2008 , pp. 575 - 579
Copyright
Copyright © 2008 Cambridge University Press

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abraham, E.G., Nagaraju, J. & Datta, R.A. (1992) Biochemical studies of amylases in the silkworm, Bombix mori L.: comparative analysis in diapausing and non-diapausing strains. Insect Biochemistry and Molecular Biology 22, 867–873.CrossRefGoogle Scholar
Applebaum, S.W. & Konijn, A.M. (1965) The utilization of starch by larvae of the flour beetle, Tribolium castaneum. Journal of Nutrition 85, 275–282.CrossRefGoogle ScholarPubMed
Baker, J.E. (1983) Properties of amylases from midguts of larvae of Sitophilus zeamais and Sitophilus granarius. Insect Biochemistry 13(4), 421–428.CrossRefGoogle Scholar
Baker, J.E. (1987) Purification of isoamylases from the rice weevil, Sitophilus orizae (Coleoptera: Curculionidae), by high-perfomance liquid chromatography and their interaction with partially-purified amylase inhibitors from wheat. Insect Biochemistry 17, 37–44.CrossRefGoogle Scholar
Biggs, D.R. & McGregor, P.G. (1996) Gut pH and amylase and protease activity in larvae of the New Zealand grass grub (Costelyra zealandica; Coleoptera: Scarabaeidae) as a basis for selecting inhibitors. Insect Biochemistry and Molecular Biology 26, 69–75.CrossRefGoogle Scholar
Botero, E.M.E., Londoño, Z.M.E., Trillos, G.O., Arias, R.J.A. & Jaramillo Pelaez, J.A. (1995) Detection of the Potato Moth Tecia solanivora in the Department of Antioquia (Colombia). 19 pp. Medellin, Colombia, ICA-CORPOICA.Google Scholar
Campos, F.A.P., Xavier-Filho, J., Silva, C.P. & Ary, M.B. (1989) Resolution and partial characterization of proteinases and alpha-amylases from midguts of larvae of the bruchid beetle Callosobruchus maculatus (F). Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 92, 51–57.CrossRefGoogle Scholar
Chagolla-Lopez, A., Blanco-Labra, A., Patthy, A., Sanchez, R. & Pongor, S. (1994) A novel alpha amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds. Journal of Biological Chemistry 269, 23675–23680.CrossRefGoogle ScholarPubMed
Doane, W.W. (1969) Amylase variants in Drosophila melanogaster: linkage studies and characterization of enzyme extracts. Journal of Experimental Zoology 171, 321–342.CrossRefGoogle ScholarPubMed
Gatehouse, A.M.R., Fenton, K.A., Jepson, I. & Pavey, D.J. (1986) The effects of α-amylase inhibitors on insect storage pests: inhibition of α-amylase in vitro and effects on development in vivo. Journal of the Science of Food and Agriculture 37, 727–734.CrossRefGoogle Scholar
Grant, G., Edwards, E.J. & Pusztai, A. (1995) Alpha amylase inhibitors levels in seeds generally available in Europe. Journal of the Science of Food and Agriculture 67, 235–238.CrossRefGoogle Scholar
Hilje, L. (1994) Characterization of the damage by the potato moths Tecia solanivora and Phthorimaea operculella (Lepidoptera: Gelechiidae) in Cartago, Costa Rica. Manejo Integrado de Plagas 31, 43–46 (in Spanish).Google Scholar
Lajolo, F.M. & Finardi-Filho, F. (1985) Partial characterization of the amylase inhibitor of black beans (Phaseolus vulgaris), variety Rico 23. Journal of Agricultural and Food Chemistry 33, 132–138.CrossRefGoogle Scholar
Lemos, F.J.A., Campos, F.A.P., Silva, C.P. & Xavier-Filho, I. (1990) Proteinases and amylases of larval midgut of Zabrotes subfasciatus (Boh) (Coleoptera: Bruchiidae) reared in Cowpea (Vigna ungiculata L.) seeds. Entomologia Experimentalis et Applicata 56, 219–227.CrossRefGoogle Scholar
Markwick, N.P., Laing, W.A., Christeller, J.T., Reid, S.T. & Newton, M.R. (1996) α-Amylase activities in larval midgut extracts from four species of Lepidoptera (Tortricidae and Gelechiidae): Response to pH and to inhibitors from wheat, Barley, Kidney bean, and Streptomyces. Journal of Economic Entomology 89(1), 39–45.CrossRefGoogle Scholar
Mendiola-Olaya, E., Valencia-Jiménez, A., Valdés-Rodríguez, S., Délano-Frier, J. & Blanco-Labra, A. (2000) Digestive amylase from the larger grain borer, Prostephanus truncatus Horn. Comparative Biochemistry and Physiology Part B 126, 425–433.CrossRefGoogle ScholarPubMed
Podoler, H. & Applebaum, S.W. (1971) The α-amylase of the beetle Callosobruchus chinensis: Properties. Biochemistry Journal 121, 321–325.CrossRefGoogle Scholar
Powers, J.R. & Whitaker, J.R. (1977) Effect of several experimental parameters on combination of red kidney bean (Phaseolus vulgaris) α-amylase inhibitor with porcine pancreatic α-amylase. Journal of Food Biochemistry 1, 217–238.CrossRefGoogle Scholar
Shade, R.E., Schroeder, H.E., Pueyo, J.J., Tabe, L.M., Murdock, L.L. & Chrispeels, M.J. (1994) Transgenic pea seeds expressing the α-amylase inhibitor of the common bean are resistant to bruchid beetles. Bio/Technology 12, 793–796.Google Scholar
Valencia-Jiménez, A., Bustillo, A.E., Ossa, G.A. & Chrispeels, M.J. (2000) α-Amylases of the coffee berry borer (Hypothenemus hampei) and their inhibition by two plant amylase inhibitors. Insect Biochemistry and Molecular Biology 30, 207–213.CrossRefGoogle Scholar
Weselake, J.R., MacGregor, W.A., Hill, D.R. & Duckworth, W.H. (1983) Purification and characteristics of an endogenous amylase inhibitor from barley kernels. Plant Physiology 73, 1008–1012.CrossRefGoogle ScholarPubMed
Yetter, M.A., Saunders, R.M. & Boles, H.P. (1979) α-Amylase inhibitors from wheat kernels as factor in resistance to postharvest insects. Cereal Chemistry 56, 243–244.Google Scholar