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Cellulase Activity and Kinetics in Rice Grasshopper Hieroglyphus banian (Orthoptera: acrididae)
Grasshopper (Hieroglyphus banian), an orthopteran species is considered to be a serious pest of rice plant in India. To study the activity and kinetics of cellulase in grasshopper this experiment is undertaken and accordingly foregut and midgut homogenates were prepared. The cellulase enzyme activity and kinetics was measured by DNSA method of Miller,(1959) by taking different concentrations of crystalline cellulose substrate in spectrophotometer at 540nm. Cellulase activity in foregut and midgut were found to be 0.482 u/mg of tissue and 0.687u/mg of tissue respectively. Km values were determined separately both in foregut and midgut and were found to be 3 mg/dl and 2 mg/dl respectively. Experimental data indicates the presence of high cellulolytic activity in the midgut which may suggest that cellulases of endogenous origin are present in this organism. It can be expected that in future, detailed study of these efficient lignocellulolytic systems will help in identification of novel enzymes possessing features that optimize biotechnological applications for the biofuel industry. Moreover, identification of crucial insect cellulases may help in the development of insecticidal technologies aimed at inhibiting their vital digestive role. Considering that this grasshopper species is a pest of paddy and grass, characterization of insect cellulolytic systems may aid in reducing the grasshopper pest attack in Indian subcontinent.
Keywords
Cellulase, Kinetics, Hieroglyphus banian, Foregut, Midgut
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- Barbehenn R V, Karowe D N, Chen Z (2004) Performance of a generalist grasshopper on a C3 and a C4 grass: compensation for the effects of elevated CO2 on plant nutritional quality. Oecologia 140, 96–103.
- Clarke A J (1997) Biodegradation of Cellulose: Enzymology and Biotechnology. Technomic Pub. Co., Lancaster, PA. pp. 3–68.
- Clissold F J , Sanson G D , Read J (2004) Indigestibility of plant cell wall by Australian plague locust, Chortoicetes terminifera. Entomol. Exp. Appl. 112, 159–168.
- Cazemier A E , Op den Camp H J, Hackstein J H and Vogels G D (1997) Fibre digestion in arthropods. Comparative Biochemistry and Physiology, 118A, 101–109.
- Davis G R F (1963) Carbohydrase activity of alimentary canal homogenates of five grasshopper species (Orthoptera: Acrididae). Arch. Int. Physiol. Biochim. 71,166–174.
- Evans W A L, Payne D W (1964) Carbohydrases of the alimentary tract of the desert locust. Schistocerca gregaria. J. Insect Physiol. 10, 657–674.
- Fielding D J, Defoliart L S (2007) Growth, development, and nutritional physiology of grasshoppers from subarctic and temperate regions. Physiol. Biochem. Zool. 80,607–618.
- Girard C, Jouanin L (1999) Molecular cloning of cDNAs encoding a range of digestive enzymes from a phytophagous beetle, Phaedon cochleariae.Insect Biochem. Mol. Biol. 29, 1129–1142
- Gruno M , Valjamae P, Pettersson G and Johansson G (2004) Inhibition of the Trichoderma reesei cellulases by cellobiose is strongly dependent on the nature of the substrate.Biotechnology and Bioengineering, 86, 503–511.
- Holtzapple M, Cognata M, Shu Y and Hendrickson C (1990) Inhibition of Trichoderma reesei cellulase by sugars and solvents. Biotechnology and Bioengineering, 36, 375– 287.
- Ishaaya I, Plaut H N (1974) Digestive enzymes in Eurytoma amygdali and their relation to food digestion and to the boring process of the emergence holes in almond fruits.Comp. Biochem. Physiol. 48, 37–44.
- Kim N , Choo Y M, Lee K S, Hong S J, Seol K Y, Je Y H, Sohn H D, Jin B R (2008) Molecular cloning and characterization of a glycosyl hydrolase family cellulase distributed throughout the digestive tract of the cricket Teleogryllus emma. Comp. Biochem. Physiol. B 150, 368–376.
- Kumarasinghe N C (2003) Insect fauna associated with sugarcane plantations in Sri Lanka. J. Environ. Biol. 24, 359–368
- Lee S J, Lee K S, Kim S R,Gui Z Z, Kim Y S,Yoon H J,Kim I, Kang PD, Sohn H D, Jin B R (2005) A novel cellulase gene from the mulberry longicorn beetle, Apriona germari: gene structure, expression, and enzymatic activity. Comp. Biochem. Physiol. B 140, 551–560.
- Lee S, Kim S R, Yoon HJ, Kim I, Lee K S, Je Y H, Lee S M, Seo S J, Sohn H D, Jin B R (2004) cDNA cloning, expression, and enzymatic activity of a cellulase from the mulberry longicorn beetle, Apriona germari. Comp. Biochem. Physiol. B139, 107–116.
- Lo N , Watanabe H, Sugimura M (2003) Evidence for the presence of a cellulase gene in the last common ancestor of bilaterian animals. Proc. Biol. Sci. 270 (Suppl 1), S69–S72.
- Lynd L R, Laser M S, Bransby D, Dale B E, Davison B, Hamilton R, Himmel M, Keller M, McMillan J D,Sheehan J and Wyman C E (2008) How biotech can transform biofuels. Nature Biotechnology, 26, 169–172.
- Lynd L R, Cushman J H, Nichols R J, Wyman C E (1991) Fuel ethanol from cellulosic biomass. Science 251, 1318–1323.
- Martin M M (1983) Cellulose digestion in insects. Comp. Biochem. Physiol. 75, 313–324.
- Matsui T, Tokuda G and Shinzato N (2009) Termites as functional gene resources. Recent Patents on Biotechnology,3, 10–18.
- McLaughlin SB, De la Torre Ugarte D G, Garten C T, Lynd L R, Sanderson M A, Tolbert V R and Wolf D D (2002) High-value renewable energy from prairie grasses. EnvironmentalScience and Technology, 36, 2122–2129.
- Miller G L (1959) Use of dinitrosalicylic acid reagent for determinationof reducing sugar. Analytical Chemistry, 31, 426–428.
- Morgan M R J (1976) Gut carbohydrases in locusts and grasshoppers. Acrida 5, 45–58.
- Morgan M R J (1975) Relationship between gut cellobiose,lactase, aryl β-glucoside, and aryl β-galactoside activities of Locusta migratoria. Insect Biochemistry, 5, 609–617.
- Morrison M , Pope P B, Denman S E and McSweeney CS (2009) Plant biomass degradation by gut microbiomes: more of the same or something new? Current Opinion in Biotechnology,20, 358–363.
- Oppert C, Klingeman W E,Willis J D, Oppert B, Jurat-Fuentes JL ( 2010) Prospecting for cellulolytic activity in insect digestive fluids. Comp. Biochem. Physiol. 155B, 145–154.
- Parrish D J, Fike J H (2009) Selecting, establishing, and managing switchgrass (Panicum virgatum) for biofuels. Methods Mol. BIol. 581, 27–40.
- Pitman A J, Jones E B, Jones M A, Oevering P ( 2003) An overview of the biology of the wharf borer beetle (Nacerdes melanura L., Oedemeridae) a pest of wood in marine structures. Biofouling 19, 239–248 Suppl.
- Schmer M R, Vogel K P, Mitchell R B and Perrin R K (2008) Net energy of cellulosic ethanol from switchgrass. Proceedings of the National Academy of Sciences of the United States of America, 105, 464–469.
- Schoenberg S A, Maccubin A E, Hodson R E (1984) Cellulose digestion by freshwater microcrustacea. Limnol. Oceanogr. 29, 1132–1136.
- Schultz M W, Slaytor M, Hogan M E, O’Brien R W (1986) Components of cellulase from the higher termite, Nasutitermes walkeri. Insect Biochem. 16, 929–932.
- Scrivener A M, Slaytor M, Rose H A (1989) Symbiont-independent digestion of cellulose and starch in Panesthia cribrata Saussure, an Australian wood-eating cockroach. J. Insect Physiol. 35, 935–941
- Sinsabaugh R L, Linkins A E, Benfield E F (1985) Cellulose digestion and assimilation by three leaf-shredding aquatic insects. Ecology 66, 1464–1471
- Smalley A E (1960) Energy flow of a salt marsh grasshopper population. Ecology 41, 672–677.
- Sun Y and Cheng J (2002) Hydrolysis of lignocellulosic materialsfor ethanol production: a review. Bioresource Technology,83, 1–11.
- Tokuda G, Watanabe H, Matsumoto T, Noda H (1997) Cellulose digestion in the wood-eating higher termite, Nasutitermes takasagoensis (Shiraki): distribution of cellulases and properties of endo-beta-1, 4-glucanase. Zool. Sci. 14, 83–93.
- Watanabe H, Tokuda G (2010) Cellulolytic systems in insects. Ann. Rev. Entomol. 55,609–632.
- Watanabe H, Noda H, Tokuda G, Lo N (1998) A cellulase gene of termite origin. Nature 394, 330–331.
- Watanabe H, Tokuda G (2001) Animal cellulases. Cell. Mol. Life Sci. 58, 1167–1178.
- Watanabe H, Nakamura M, Tokuda G, Yamaoka I, Scrivener A M,Noda H (1997) Site of secretion and properties of endogenous endo-beta-1, 4-glucanase components from Reticulitermes speratus (Kolbe), a Japanese subterranean termite. Insect Biochem. Mol. Biol. 27, 305–3013.
- Wharton D R, Wharton M L (1965) The cellulase content of various species of cockroaches. J. Insect Physiol. 11, 1401–1405.
- Wei Y D, Lee K S, Gui Z Z, Yoon H J, Kim I , Zhang G Z ,Guo X, Sohn H D, Jin BR (2006) Molecular cloning, expression, and enzymatic activity of a novel endogenous cellulase from the mulberry longicorn beetle. Apriona germari. Comp. Biochem. Physiol. B 145, 220–229.
- Willis J D, Oppert C, Jurat-Fuentes J L (2010) Methods for discovery and characterization of cellulolytic enzymes from insects. Insect Sci. 17, 184–198.
- Wyman C E (2007) What is (and is not) vital to advancing cellulosic ethanol. Trends in Biotechnology, 25, 153–157.
- Wyman C E (1999) Biomass ethanol: technical progress, opportunities, and commercial challenges. Annu. Rev. Energy Environ. 24, 189–226.
- Yang Y , Joern A (1994) Influence of diet, developmental stage and temperature on food residence time in Melanoplus sanguinipes. Physiol. Zool. 67, 598–616
- Yokoe Y, Yasumasu I (1964) Distribution of cellulose in invertebrates. Comp. Biochem. Physiol. 13, 323–338.
- Zhang D H, Lax A R, Bland J M, Yu J J, Fedorova N, Nierman W C (2010) Hydrolysis of filter-paper cellulose to glucose by two recombinant endogenous glycosyl hydrolases of Coptotermes formosanus. Insect Sci. 17, 245–252.
- Zhang D, Lax A R, Raina A K, Bland J M (2009) Differential cellulolytic activity of native-form and C-terminal tagged-form cellulase derived from Coptotermes formosanus and expressed in E. coli. Insect Biochem. Mol. Biol. 39, 516–522.
- Zhou X, Wheeler M M, Oi F M and Scharf M E (2008) RNA interference in the termite Reticulitermes flavipes through ingestion of double-stranded RNA. Insect Biochemistry and Molecular Biology, 38, 805–815.
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