Effect of diets on digestive enzymes from worker termites of Odontotermes brunneus (Termitidae)

  • Muthusamy R. 
  • Gayathri R. 
  • Suresh K. 
  • Chethan Kumar T. 
Original Article
  • 7 Downloads

Abstract

The digestive system of termites may have several biotechnological applications. The enzyme activity of α-amylase, cellulase and protease in Odontotermes brunneus workers were tested against three different diets. Additionally, the effects of temperature (30–80 °C) and pH (2.0–10.0) on enzyme activities were evaluated. All enzymes investigated were detected in the gut extracts of worker termites. Odontotermes brunneus worker gut α-amylase and cellulase activity was high in wood diet 25 U and 1700 mU/mg and the protease activity was high in filter paper 130 U/mg. α-amylase in termites consisted of 15–25 U/mg protein when the pH was about 4.0–6.0. Cellulase in termites consisted of 1000 U/mg protein when the pH was about 4.0–6.0. Protease in termites consisted of 125 U/mg protein when the pH was about 6.0–8.0. Also the enzyme activity on temperature was influenced by different diet in O. brunneus. Over all study revealed that the diet of O. brunneus from different source may influence the enzyme production and its stability, which can be used as individual resources. The influence of mixed diet and the involvement of enzymes producing micro bacteria need to be further analyzed.

Keywords

Worker Enzymes Odontotermes brunneus Protease Amylase Cellulase 

Notes

Acknowledgments

The authors thank our department of PG and Research Centre in Biotechnology for providing infrastructure facility and we thank Dr. P. Balaji Head of the department for his support to carry out this work.

Compliance with ethical standards

Conflict of interest

The authors declared that we have no conflict of interest.

References

  1. Ackerman IL, Constantino R, Gauch HG, Lehmann J, Riha SJ, Erick CMF (2009) Termite (Insecta: Isoptera) species composition in a primary rain forest and agroforests in Central Amazonia. Asso Trop Biol Cons Biotrop 41(2):226–233.  https://doi.org/10.1111/j.1744-7429.2008.00479.x Google Scholar
  2. Ahmed S, Mustafa T, Riaz MA, Hussain A (2006) Efficacy of insecticides against subterranean termites in sugarcane. Int J Agric Biol 8:508–510Google Scholar
  3. Azeez A, Sane AP, Bhatnagar D, Nath P (2007) Enhanced expression of serine proteases during floral senescence in Gladiolus. Phytochemistry 68:1352–1357.  https://doi.org/10.1016/j.2007.02.027 CrossRefPubMedGoogle Scholar
  4. Bernfeld P (1955) Amylases, α and β. Methods Enzymol 1:149–158CrossRefGoogle Scholar
  5. Campbell NA, Reece JB, Urry LA, Cain ML, Wasserman SA, Minorsky PV, Jackson RB (2008) Biology, Eight edn. Pearson-Benjamin Cummings, LondonGoogle Scholar
  6. Chottani OB (1997) Fauna of India–isoptera (termites) Vol. II, pp. xx + 801 (Published Director.ZSI. Calcutta)Google Scholar
  7. Drapcho CM, Nhuan NP, Walker TH (2008) Biofuels engineering process technology. The McGraw-Hill companies and Industries, New YorkGoogle Scholar
  8. Fagbohunka BS, Edorh SE, Adeyanju MM, Ezima EN, Alabi MA, Ogunlabi OO (2015) Activites of a cellulase of the termite, Ametermes eveuncifer (Silverstri) soldier: clue to termites salt intolerance. J Nat Sci Res 5(11):117–121Google Scholar
  9. Franco OL, Ridgen DJ, Melo FR, Grossi-de-Sa MF (2002) Plant alpha-amylase inhibitors and their interaction with insect alpha-amylase structure, function and potential for crop protection. Eur J Biochem 269:397–412.  https://doi.org/10.1046/j.0014-2956.2001.02656.x CrossRefPubMedGoogle Scholar
  10. Fujita A, Abe T (2002) Amino acid concentration and distribution of lysozyme and protease activities in the guts of higher termites. Physiol Entomol 27:76–78.  https://doi.org/10.1046/j.1365-3032.2001.00265.x CrossRefGoogle Scholar
  11. Fujita A, Miura T, Matsumoto T (2008) Differences in cellulose digestive systems among castes in two termites lineages. Physiol Entomol 33:73–82.  https://doi.org/10.1111/j.1365-3032.2007.00606.x CrossRefGoogle Scholar
  12. Haddar A, Agrebi R, Bougatef A, Hmidet N, Sellami-Kamoun A, Nasri M (2009) Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: purification, characterization and potential application as a laundry detergent additive. Biores Technol 100:3366–3373.  https://doi.org/10.1016/j.biortech.2009.01.061 CrossRefGoogle Scholar
  13. Hahn-Hagerdal B, Galbe M, Gorwa Grauslund MF, Liden G, Zacchi G (2007) Bio-ethanol—the fuel of tomorrow from the residues of today. Trends Biotechnol 24:12.  https://doi.org/10.1016/2006.10.004 Google Scholar
  14. Hemachandra J, Edirisinghe P, Karunaratne WAIP, Gunatilleke CVS (2010) Distinctiveness of termite assemblages in two fragmented forest types in Hantane hills in the Kandy district of Sri Lanka. Ceylon J Sci (Biol Sci) 39(1):11–19.  https://doi.org/10.4038/cjsbs.v39i1.2349 CrossRefGoogle Scholar
  15. Hmidet N, Ali NE, Haddar A, Kanoun S, Alya S, Nasri MJ (2009) Alkaline proteases and thermo stable α-amylase co-produced by Bacillus licheniformis NH1: characterization and potential application as detergent additive. Biochem Eng 47:71–79.  https://doi.org/10.1016/j.bej.2009.07.005 CrossRefGoogle Scholar
  16. Jany KD, Haug H, Ishay J (1978) Trypsin-like endopeptidases from the midguts of the larvae from the hornets of Vespa orientalis and Vespa crabro. Insect Biochem 8:221–230.  https://doi.org/10.1016/0020-1790(78)90030-6 CrossRefGoogle Scholar
  17. Li X, Yang H, Roy B, Wang D, Yue W, Jiang L, Park EY, Miao Y (2009) The most stirring technology in future: cellulase enzyme and biomass utilization. Afr J Biotechnol 8(11):2418–2422Google Scholar
  18. Lima TA, Pontual EV, Dornelles LP, Amorim PK, Sa RA, Coelho LCBB, Napoleao TH, Paiva PMG (2014) Digestive enzymes from workers and soldiers of termite Nasutitermes corniger. Comp Biochem Physiol B: Biochem Mol Biol 176:1–8.  https://doi.org/10.1016/j.cbpb.2014.07.001 CrossRefGoogle Scholar
  19. Mendiola-Olaya E, Valencia-Jimenez A, Valdes-Rodriguez S, Delano-Frier J, Blanco-Labra A (2000a) Digestive amylase from the larger grain borer, Prostephanus truncates. Comp Biochem Physiol B Biochem Mol Biol 126:425–433.  https://doi.org/10.1016/j.cbpb.2014.07.001 CrossRefPubMedGoogle Scholar
  20. Mendiola-Olaya E, Valencia-Jimenez A, Valdes-Rodriguez S, Delano-Frier J, Blanco Labra A (2000b) Digestive amylase from the larger grain borer, Prostephanus truncates Horn. Comp Biochem Physiol B: Biochem Mol Biol 126:425–433.  https://doi.org/10.1016/S0305-0491(00)00219-4 CrossRefGoogle Scholar
  21. Ni J, Tokuda G (2013) Lignocellulose-degrading enzymes from termites and their symbiotic microbiota. Biotechnol Adv 31:838–850.  https://doi.org/10.1016/j.biotechadv.2013.04.005 CrossRefPubMedGoogle Scholar
  22. Noirot C (1992) From wood- to humus feeding: an important trend in termite evolution. Biol Evol Soc Insects, pp 107–119Google Scholar
  23. Ogino H, Otsubo T, Ishikawa H (2008) Screening, purification, and characterization of a leather-degrading protease. J Biochem Eng 38:234–240.  https://doi.org/10.1016/j.bej.2007.07.008 CrossRefGoogle Scholar
  24. Panwar NL, Kaushik SC, Kothari S (2011) Role of renewable energy sources in environmental protection: a review. Rene Sust Energy Reviews 15:1513–1524.  https://doi.org/10.1016/j.rser.2010.11.037 CrossRefGoogle Scholar
  25. Priya S, Kaur N, Gupta AK (2010) Purification, characterization and inhibition studies of α-amylase of R. dominica. Pestic Biochem Physiol 98:231–237.  https://doi.org/10.1016/j.pestbp.2010.06.012 CrossRefGoogle Scholar
  26. Souza PM, Magalhaes PO (2010) Application of microbial α-amylase in industry a review. Braz J Microbiol 41:850–861.  https://doi.org/10.1590/S1517-83822010000400004 CrossRefPubMedCentralPubMedGoogle Scholar
  27. Terra WR, Ferreira C (1994) Insect digestive enzymes: properties, compartmentalization and function. Comp Biochem Physiol B: Biochem Mol Biol 109:1–62CrossRefGoogle Scholar
  28. Tokuda G, Watanable H (2007) Hidden cellulases in termites: revision of an old hypothesis. Biol Lett 3:336–339.  https://doi.org/10.1098/rsbl.2007.0073 CrossRefPubMedCentralPubMedGoogle Scholar
  29. Tokuda G, Watanabe H, Hojo M, Fujita A, Makiya H, Miyagi M, Arakawa G, Arioka M (2012) Cellulolytic environment in the midgut of the wood-feeding higher termite Nasutitermes takasagoensis. J Insect Physiol 58:147–154.  https://doi.org/10.1016/j.jinsphys.2011.10.012 CrossRefPubMedGoogle Scholar
  30. Waller DA, La Fage JP (1986) Nutritional ecology of termites. In: Slansky F Jr, Rodriguez JG (eds) Nutritional ecology of insects, mites, spiders, and related invertebrates. Wiley, New York, pp 487–532Google Scholar
  31. Whistler RL, Chen CC (1991) Hemicelluloses. In: Lewin M, Goldstein IS (eds) Wood structure and composition. International fiber science and technology series, vol 11. Marcel Decker Inc, New York, pp 287–320Google Scholar
  32. Yezdani E, Sendi JJ, Zibaee A, Ghadamyari M (2010) Enzymatic properties of α-amylase in the midgut and the salivary glands of mulberry moth, Glyphodes pyloalis Walker (Lepidoptera: Pyralidae). C R Biol 333:17–22.  https://doi.org/10.1016/j.crvi.2009.11.004 CrossRefPubMedGoogle Scholar
  33. Zibaee A, Bandani AR, Kafil M, Ramzi S (2008) Characterization of α-amylase in the midgut and the salivary glands of rice striped stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae). J Asia Pac Entomol 11:201–205.  https://doi.org/10.1016/j.aspen.2008.09.003 CrossRefGoogle Scholar

Copyright information

© Indian Academy of Wood Science 2018

Authors and Affiliations

  • Muthusamy R. 
    • 1
  • Gayathri R. 
    • 1
  • Suresh K. 
    • 1
  • Chethan Kumar T. 
    • 1
  1. 1.PG and Research Centre in BiotechnologyMGR CollegeHosurIndia

Personalised recommendations