PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2013 | 53 | 3 |

Tytuł artykułu

Inhibition of Digestive α-Amylases from Chilo Suppressalis Walker (Lepidoptera: Crambidae) by a Proteinaceous Extract of Citrullus Colocynthis L. (Cucurbitaceae)

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The striped rice-stem borer, Chilo suppressalis (Walker) is one of the most important pest of rice worldwide. In this study, a proteinaceous extract from Citrullus colocynthis L. shows various degrees of inhibition to digestive α-amylases of C. suppressalis. Digestive α-amylases of larvae were inhibited by different concentrations (approximately 50%) of C. colocynthis amylase inhibitor (CCAI). One of the isozymes totally disappeared and the sharpness of another decreased on native-PAGE electrophoresis. The pH dependency of inhibition revealed that the enzyme was inhibited in a wide range of pH from 7-10, and the optimal pH of the enzyme occurred in lepidopteran larvae. The highest inhibition of α-amylase by CCAI was observed at 25°C; the temperature near the optimal temperature of amylolytic activity. A time-course experiment demonstrated that enzymatic activity was the highest, 30 min after the onset of the experiment, when the highest inhibition occurred. The enzyme kinetic studies using Lineweaver-Burk analysis, revealed a mixed inhibition of CCAI on α-amylase activity. The current study is the first basic one using α-amylase inhibitor against C. suppressalis. This study opens the way for transgenic rice varieties containing inhibitors.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

53

Numer

3

Opis fizyczny

p.195-202,fig.,ref.

Twórcy

autor
  • University of Guilan, Department of Plant Protection, Faculty of Agricultural Science, Rash Iran, 41637-1314
autor
  • University of Guilan, Department of Plant Protection, Faculty of Agricultural Science, Rash Iran, 41637-1314
autor
  • University of Guilan, Department of Plant Protection, Faculty of Agricultural Science, Rash Iran, 41637-1314

Bibliografia

  • Alfonso J., Ortego F., Sanchez-Monge R., Garcia-Casado G., Pujol M., Castanera P., Salcedo G. 1997. Wheat and barley inhibitors active towards α-amylase and trypsin-like activities from Spodoptera frugiperda. J. Chem. Ecol. 23 (7): 1729-1741.
  • Barbosa A.E., Albuquerque E.V., Silva M.C., Souza D.S., Oliveira- Neto O.B., Valencia A., Rocha T.L., Grossi-de-Sa M.F. 2010. Alphα-amylase inhibitor-1 gene from Phaseolus vulgaris expressed in Coffea arabica plants inhibits alphα-amylases from the coffee berry borer pest. BMC Biotechnol. 17 (1): 10-44.
  • Baker J.E. 1987. Purification of isoamylases from the rice weevil, Sitophilus orizae L. by HPLC and their interaction with paratiallypurified amylase inhibitor from wheat. Insect. Biochem. 93 (2): 37-44.
  • Baker J.E. 1989. Interaction of partially-purified amylases from larval Anagasta kuehniella (Lepidoptera: Pyralidae) with amylase inhibitors from wheat. Comp. Biochem. Physiol. Part B. 93 (2): 239-245.
  • Bernfeld P. 1955. Amylases, α and β. Meth. Enzymol. 1 (1): 149-158.
  • Bonavides K.B., Pelegrini P.B., Laumann R.L., Grossi-de-Sá M.F., Bloch Jr. C., Melo J.A.T., Quirino B.F., Noronha E.F., Franco O.L. 2007. Molecular identification of four different α-amylase inhibitors from Baru (Dipteryx alata) seeds with activity toward insect enzymes. J. Biochem. Mol. Biol. 40 (4): 494-500.
  • Franco O.L., Ridgen D.J., Melo F.R., Bloch C. Jr., Silva C.P., Grossi- de-Sa M.F. 2002. Activity of wheat α-amylase inhibitors towards bruchid α-amylases and structural explanation of observed specificities. Eur. J. Biochem. 267 (8): 2166-2173.
  • Giri A.P., Kachole M. 1998. Amylase inhibitors of pigeonpea (Cajanus cajan) seeds. Phytochemistry 47 (2): 197-202.
  • Heidari R., Zareae S., Heidarizadeh M. 2005. Extraction, purification and inhibitory effect of alphα-amylase inhibitor from wheat (Triticum aestivum var. zarrin). Pakistan. J. Nutr. 4 (2): 101-105.
  • Khanjani M. 2006. Crop Pests of Iran. Boali Sina University Press, Hamadan, Iran, 717 pp.
  • Kotkar H.M., Sarate P.J., Tamhane V.A., Gupta V.S., Giri A.P. 2009. Responses of midgut amylases of Helicoverpa armigera to feeding on various host plants. J. Insect. Physiol. 55 (8): 663-670.
  • Kutty A.V.M., Pattabiraman T.N. 1986. Isolation and characterization of an amylase inhibitor from sorghum seeds, specific for human enzymes. J. Agric. Food Chem. 34 (3): 552-557.
  • Laemmli U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (5259): 680-685.
  • LeBerre-Anton V., Bompard-Gilles C., Payan F., Rouge P. 1997. Characterization and functional properties of the alphα- amylase inhibitor (alpha A-1) from kidney bean (Phaseolusvulgaris) seeds. Biochim. Biophys. Acta 1343 (1): 31-40.
  • Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1): 265-75.
  • Marshall J.J., Lauda C.M. 1975. Purification and properties of phaseolamin, an inhibitor of á-amylase, from the kidney bean Phaseolus vulgaris. J. Biol. Chem. 250 (20): 8030-8037.
  • Marzouk B., Haloui E., Akremi N., Aouni M., Marzouk Z., Fenina N. 2012. Antimicrobial and anticoagulant activities of Citrullus colocynthis Schrad. leaves from Tunisia (Medenine). Afr. J. Pharm. Pharmacol. 6 (26): 1982-1988.
  • McEwan R., Madivha R.P., Djarova T., Oyedeji O.A., Opoku A.R. 2010. Alphα-amylase inhibitor of amadumbe (Colocasiaesculenta): Isolation, purification and selectivity toward α-amylases from various sources. Afr. J. Biochem. Res. 4 (9): 220-224.
  • Mehrabadi M., Bandani A.R., Saadati F. 2010. Inhibition of Sunn pest, Eurygaster integriceps, α-amylases by α-amylase inhibitors (T-αAI) from Triticale. J. Insect. Sci. 10 (2): 179.
  • Melo F.R., Sales M.P., Silva L.S., Franco O.L., Bloch Jr C., Ary M.B. 1999. α-amylase inhibitors from cowpea seeds. Prot. Pept. Letter. 6 (3): 387-392.
  • Muralikrishna G., Nirmala M. 2005. Cereal α-amylases - an overview. Carbohydr. Polym. 60 (2): 163-173.
  • Khan N. 2011. In vitro effects of protienaceous alpha amylase inhibitors on red flour beetle, Tribolium castaneum. Sci. Res. Rep. 1 (2): 101-104.
  • Priya S., Kaur N., Gupta A.K. 2010. Purification, characterization and inhibition studies of α-amylase of Rhyzopertha dominica. Pest. Biochem. Physiol. 98 (2): 231-237.
  • Rekha M.R. Padmaja G., Easwari C.S., Sheela M.N. 1999. Genotype differences in the α-amylase inhibitor activity in sweet potato and yam tubers. J. Root. Crops 25 (1): 95-101.
  • Roy I., Gupta M.N. 2000. Purification of a double-headed inhibitor of alphα-amylase/Proteinase K from wheat germ by expanded bed chromatography. Bioseparation 9 (4): 239-245.
  • Seltzer R.D., Strumeyer D.H. 1990. Purification and characterization of esculentamin, a proteinaceous alphα-amylase inhibitor from the taro root, Colocasia esculenta. J. Food. Biochem. 14 (3): 199-217.
  • Silva C.P., Terra W.R., Xavier-Filho J., Grossi-de-Sa M.F., Lopes A.R., Pontes E.G. 1999. Digestion in larvae of Callosobruchusmaculatus and Zabrotes subfasciatus (Coleoptera: Bruchidae) with emphasis on α-amylases and oligosaccharidases. Insect. Biochem. Mol. Biol. 29 (4): 355-366.
  • Sivakumar S., Mohan M., Franco O.L., Thayumanavan B. 2006. Inhibition of insect pest α-amylases by little and finger millet inhibitors. Pest. Biochem. Physiol. 85 (3): 155-160.
  • Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Ruth F., Glockshuber R. 1998. A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with Ragi bifunctional inhibitor at 2.5 Å resolution. Structure 6 (7): 911-921.
  • Suzuki K., Ishimoto M., Kitamura K. 1994. cDNA sequence and deduced primary structure of an alphα-amylase inhibitor from a bruchid-resistant wild common bean. Biochim. Biophys. Acta 1206 (2): 289-291.
  • Tannin-Spitz T. Grossman S., Dovrat S., Gottlieb H.E., Bergman M. 2007. Growth inhibitory activity of cucurbitacin glucosides isolated from Citrullus colocynthis on human breast cancer cells. Biochem. Pharmacol. 73 (1): 56-67
  • Tavakkol-Afshari J., Rakhshandeh H., Zamani A., Mahdavi- Shahri N., Ghazi-Zadeh L., Vahedi F., Nourouze M. 2005. Cytotoxic effect of Citrullus colocynthis extract on cell line of Hep2 and L929. Res. J. Hakim. 8 (2): 47-54.
  • Valencia-Jimenez A., Arboleda J.W., Lopez Avila A., Grossi-de-Sa M.F. 2008. Digestive α-amylases from Tecia solanivora larvae (Lepidoptera: Gelechiidae): response to pH, temperature and plant amylase inhibitors. Bull. Entomol. Res. 98 (6): 575-579.
  • Zibaee A., Sendi J., Alinia F., Etebari K. 2009a. Diazinon resistance in different selected strains of Chilo suppressalis Walker (Lepidoptera: Pyralidae), rice striped stem borer, in the north of Iran. J. Econ. Entomol. 102 (3): 1189-1196.
  • Zibaee A. 2012. Proteolytic profile in the larval midgut of Chilosuppressalis Walker (Lepidoptera: Crambidae). Entomol. Res. 42 (3): 142-150.
  • Zibaee A., Bandani A. R., Kafil M., Ramzi S. 2008a. Characterization of α-amylase in midgut and salivary glands of Chilosuppressalis Walker (Lepidoptera: Pyralidae), rice striped stem borer. J. Asia-Pacific. Entomol. 11 (4): 201-205.
  • Zibaee A., Bandani A.R., Ramzi S. 2008b. Lipase and invertase activities in midgut and salivary glands of Chilo suppressalis (Walker) (Lepidoptera, Pyralidae), rice striped stem borer. Invert. Surv. J. 5 (2): 180-189.
  • Zibaee A., Bandani A.R., Ramzi S. 2009b. Characterization of α and β-glucosidases in midgut and salivary glands of Chilo suppressalis Walker (Lepidoptera: Pyralidae), rice striped stem borer. Comp. Rend. Biol. 332 (7): 633-641.

Uwagi

rekord w opracowaniu

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-6cb5b22d-d943-4aac-acc9-81be79b6a175
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.