Purification and biochemical characterization of a specific alpha-glucosidase from the digestive fluid of larvae of the palm weevil, Rhynchophorus palmarum L.

Paper Details

Research Paper 01/07/2015
Views (307) Download (11)
current_issue_feature_image
publication_file

Purification and biochemical characterization of a specific alpha-glucosidase from the digestive fluid of larvae of the palm weevil, Rhynchophorus palmarum L.

Yapi Assoi Yapi désiré Patrice, Konan Kouassi Hubert*, Binaté Siaka, Kouadio Eugène Jean Parfait, Kouamé Lucien Patrice
Int. J. Biosci.7( 1), 74-85, July 2015.
Certificate: IJB 2015 [Generate Certificate]

Abstract

A alpha-glucosidase was purified from the digestive fluid of the palm weevil Rhynchophorus palmarum L. (Coleoptera: Curculionidae) by chromatography on anion-exchange, gel filtration, and hydrophobic interaction columns. The preparation was shown to be homogeneous on polyacrylamide gels. alpha-glucosidase is a monomeric protein with a molecular weight of 60.60 kDa based on its mobility in SDS-PAGE and 61.05 kDa based on gel filtration. Maximal alpha-glucosidase activity occurred at 45°C and pH 5.6. The purified alpha-glucosidase was stable at 37°C and its pH stability was in the range of 4.0–5.6. The enzyme readily hydrolysed p-nitrophenyl-α-D-glucoside, maltose, maltodextrins and required strictly alpha-gluco configuration for activity. It cleaved glucose-glucose alpha-(1–2) linkages better than alpha-(1–4), alpha-(1–1), alpha-(1–3) and β-(1–6) linkages. The catalytic efficiency (Vmax/KM) values for p-nitrophenyl-α-D-glucoside, maltose, maltotriose, maltotetraose, maltopentose, maltohexose, Saccharose and Kojibiose were respectively 474.00, 36.81, 45.79, 45.85, 31.15, 6.63, 184.61 and 109.17. Alpha-glucosidase was capable of catalysing transglucosylation reactions. The yields in transglucosylation reactions at 37 °C were very high and could attain 62% with2-phenylethanol as glucosyl acceptors. This alpha-glucosidasehydrolyzed the products formed. It seems that the products formed were the phenylethyl-α-D-glucoside. These results suggest that alpha-glucosidase from the digestive fluid of the palm weevil Rhynchophorus palmarum is an exoglucosidase which catalyse the splitting of the α-glucosyl residue from the non reducing terminal of the substrate to liberate α-glucose.

VIEWS 4

Akinloye OA, Balogun EA, Kareem SO, Mosaku OS. 2012. Partial purification and some properties of α–glucosidase from Trichoderma longibrachiatum. Biokemistri 24(1), 31-37.

Asadi A, Ghadamyari M, Sajedi RH, Jalali J,Tabari M. 2012. Biochemical Characterization of α- and β-glucosidases in Alimentary Canal, Salivary Glands and Haemolymph of the Rice Green Caterpillar, Narangaae nescens M. (Lepidoptera: Noctuidae). Biologia 67(6), 1186-1194.

Ashford DA, Smith WA, Douglas AE. 2000. Living on a High Sugar Diet: the Fate of Sucrose Ingested by a Phloemfeeding Insect, the Pea Aphid Acyrthosiphon pisum. Journal of Insect Physiology 46, 335-341.

Baker RJ, Lehner Y. 1972. A Look at Honey Bee Gut Functions. Bee Journal 112, 336-338.

Baker JE. 1991. Properties of Glycosidases from the Maize Weevil, Sitophilus zeamais. Insect Biochemistry 21(6), 615-621.

Bernfeld P. 1955. Amylases, α and β. Methods in Enzymology 1, 149-158.

Blum H, Beier H, Gross B. 1987. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.

Carneiro CN, Isejima EM, Samuels RI,Silva CP. 2004. Sucrose hydrolases from the midgut of the sugarcane stalk borer Diatraea saccharalis. Journal of Insect Physiology 50(11), 1093-1110.

Chanchao CH, Pilalam S,Sangvanich P. 2008. Purification and Characterization of alpha-glucosidase in Apis cerana indica. Insect Science 15, 217-224.

Chiba S. 1988. Alpha-Glucosidases. In: “Handbook of Amylases and Related Enzymes”. The Amylase Research Society of Japan, Pergamon Press, Oxford, United Kingdom, 104–105.

Fonseca FV, Silva JR, Samuels RI, DaMatta RA, Terra WR, Silva CP. 2010. Purification and partial characterization of a midgut membrane-bound α-glucosidase from Quesada gigas (Hemiptera:Cicadidae). Comparative Biochemistry and Physiology Part B 155, 20–25.

Frandsen TP, Svensson B. 1998. Plant alpha-glucosidases of the Glycoside Hydrolase Family 31 Molecular Properties, Substrate Specificity, Reaction Mechanism and Comparison with Family Members of Different Origin. Journal of Insect Physiology 37, 1– 13.

Ghadamyari M, Hosseininaveh V, Sharifi M. 2010. Partial Biochemical Characterization of alpha and beta-glucosidases of Lesser Mulberry Pyralid, Glyphodes pyloalis Walker (Lep.:Pyralidae). Comptes Rendus Biologies 333, 197–204.

Huber RE, Mathison RD. 1976. Physical, Chemical and Enzymatic Studies on the Major Sucrose on Honey Bees (Apis melifera). Canadian Journal of Biochemistry 54, 153–164.

Johnson JW, Gretes M, Goodfellow VJ, Marrone L, Heynen ML, Strynadka NCJ, Dmitrienko G. 2010. Cyclobutanone Analogues of Beta-lactams Revisited: Insights into Conformational Requirements for Inhibition of Serine- and Metallo-beta-lactamases. Journal of the American Chemical Society 132(8), 2558- 2560. Kato N, Suyama S, Shirokane M, Kato M. 2002. Novel alpha-Glucosidase from Aspergillus nidulans with Strong Transglycosylation Activity Applied and Environmental Microbiology 68(3), 1250–1256.

Kouamé LP, Niamké S, Diopoh J, Colas B. 2001. Transglycosylation reactions by exoglycosidases from the termite Macrotermes subhyalinus. Biotechnology Letters 23, 1575-1581.

Kouamé LP, Due EA, Niamké SL, Kouamé FA, Kamenan A. 2005. Synthèses enzymatiques de neoglucoconjugués catalysées par l’α-glucosidase purifiée de la blatte Periplaneta americana (Linnaeus). Biotechnology, Agronomy, Society and Environment 9(1), 35–42.

Kunst A, Draeger B, Ziegenhorn J. 1984. Colorimetric methods with glucose oxydase and peroxydase. In: Bergmeyer HU, editor. Methods of enzymatic analysis 6, 178-185. Verlagchemie, weinheim.

Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.

Lagadic L, Chararas C. 1988. Etude des Activités Osidasiques Digestives D’Adultes de Bruchus afinis en Tours D’Hivernation en Clevage Artificial et en Conditions Semi-naturelles. Entomologia experimentalis et applicata 48, 247-255.

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951. Protein measurement with the Folin phenol reagent. Journal of Biology and Chemistry 193, 265-275.

Oyekanmi N, Sukhoon K, Se-Yong L, Dae-Sil L. 2001. Novel α-Glucosidase from Extreme Thermophile Thermus caldophilus GK24. Journal of Biochemistry and Molecular Biology 34(4), 347-354.

Memarizadeh N, Zamani P, Sajedi RH, Ghadamyari M. 2014. Purification and Characterization of Midgut alpha-Glucosidase from Larvae of the Rice Green Caterpillar, Naranga aenescens Moore, Journal of Agricultural Science and Technology 16, 1229-1240.

Nishimoto M, Kubota M, Tsuji M, Mori H, Kimura A, Matsui H, Chiba S. 2001. Purification and Substrate Specificity of Honeybee, Apis mellifera L., alpha-glucosidase. Bioscience, Biotechnology, and Biochemistry 65(7), 1610-1616.

Ramzi S, Hosseininaveh V. 2010. Biochemical Characterization of Digestive alpha-amylase, alpha-glucosidase and beta-glucosidase in Pistachio Green Stink Bug, Brachynema germari Kolenati (Hemiptera: Pentatomidae). Journal of Asia-Pacific Entomology 13, 215-219.

Saberi RN, Ghadamyari M, Motamediniya B. 2012. Biochemical Characterization of alpha- and beta-glucosidases and alpa- and beta-galactosidases from Red Palm Weevil, Rhynchophorus ferrugineus (Olivier) (Col.: Curculionidae). Plant Protection Science 48(2), 85-93.

Saki SJ, Sea TB, Koffi KM, Soro YR, Kra KA, Diopoh KJ. 2014. Purification and physicochemical characterization of the α-glucosidase of the digestive juice of the snail limicolria flammea. International Journal of Plant, Animal and Environmental Sciences 4(1), 376-388.

Silva CP, Terra WR. 1995. An a-glucosidase from perimicrovillar membranes of Dysdercus peruvianus (Hemiptera: Pyrrhocoridae) midgut cells. Purification and properties. Insect Biochemistry and Molecular Biology 25, 487–494.

Tanimura T, Kitamura K, Fukuda T, Kikuchi T. 1979. Purification and Partial Characterization of Three Forms of Alpha-glucosidase from the Fruit Fly Drosophila melanogaster. Biochemical Journal 85(1), 123-130.

Terra RW, Ferreira C. 1994. Insect digestive enzymes: properties, compartmentalization and function. Comparative Biochemistry and Physiology 109B, 1–62.

Terra WR, Ferreira C, Jordao BP, Dillon RJ. 1996. Digestive Enzymes. In: “Biology of the Insect Midgut”, (Eds.), Lehane, M. J. and Billingsley, P. F., Chapman and Hall, London, PP. 153-193.

Wigglesworth VB. 1972. The Principles of Insect Physiology, 7th edn. Methuen, London.

Wongchawalit J, Yamamoto T, Nakai H, Kim YM, Sato N, Nishimoto M, Okuyama M, Mori H, Saji O, Chanchao CH, Wongsiri S, Surarit R, Svasti J, Chiba S, Kimura A. 2006. Purification and Characterization of alpha-glucosidase from Japanese Honeybee (Apis ceana japonica) and Molecular Cloning of Its cDNA. Bioscience, Biotechnology, and Biochemistry 70(12), 2889-2898.

Yang C, Liu WH. 2004. Purification and properties of a maltotriose-producing alpha- amylase from Thermobifida fusca. Enzyme and Microbial Technology 35, 254-260.