About this Journal Submit a Manuscript Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 264020, 8 pages
http://dx.doi.org/10.1155/2013/264020
Review Article

Actinomycetes: A Repertory of Green Catalysts with a Potential Revenue Resource

1Dr. D. Y Patil Biotechnology & Bioinformatics Institute, Dr. D. Y. Patil Vidyapeeth, Pune 411 033, India
2System Biology Research Center, School of Life Sciences, University of Skövde, P.O. Box 408, 541 28 Skövde, Sweden
3Department of Microbiology, University of Pune, Pune 411 007, India

Received 25 December 2012; Revised 27 March 2013; Accepted 28 March 2013

Academic Editor: Bertrand Aigle

Copyright © 2013 Divya Prakash et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. Leisola, J. Jokela, O. Pastinen, O. Turunen, and H. E. Schoemaker, “Industrial use of enzymes,” in In Encyclopedia of Life Support Systems (EOLSS), vol. 2, UNESCO, Eolss Publishers, Oxford, UK, 2004.
  2. http://naturebiochem.com/downloads/Enzymes_Pharma_applications.
  3. http://ec.europa.eu/food/fs/sc/scan/out85_en.pdf.
  4. P. Monteiro de souza and P. de Oliveira, “Application of microbial a-amylase in industry: a review,” Brazilian Journal of Microbiology, vol. 41, 2010.
  5. Collection of information on enzymes, Final Report “Collection of Information on Enzymes”, 2002, http://ec.europa.eu/environment/archives/dansub/pdfs/enzymerepcomplete.pdf.
  6. B. E. Jones, A. H. Kleij Wilhelmus, P. Van Solingen, and W. Weyler, “Cellulase producing actinomycetes, cellulase produced there from and method of producing same,” EP 1408108 B1, 2004.
  7. F. Zhang, J. J. Chen, W. Z. Ren et al., “Cloning, expression and characterization of an alkaline thermostable GH9 endoglucanase from Thermobifida halotolerans YIM, 90462 T,” Bioresource Technology, vol. 102, no. 21, pp. 10143–10146, 2011.
  8. B. E. Jones, A. H. Kleij Wilhelmus, P. Van Solingen, and W. Weyler, “Cellulase producing actinomycetes, cellulase produced there from and method of producing same,” US Patent 6566112, 2003.
  9. S. P. George, A. Ahmad, and M. B. Rao, “Studies on carboxymethyl cellulase produced by an alkalothermophilic actinomycete,” Bioresource Technology, vol. 77, no. 2, pp. 171–175, 2001. View at Publisher · View at Google Scholar · View at Scopus
  10. N. A. El-Sersy, H. Abd-Elnaby, G. M. Abou-Elela, H. A. H. Ibrahim, and N. M. K. El-Toukhy, “Optimization, economization and characterization of cellulase produced by marine Streptomyces ruber,” African Journal of Biotechnology, vol. 9, no. 38, pp. 6355–6364, 2010. View at Scopus
  11. R. Brzezinski, C. V. Dery, and C. Beaulieu, “Thermostable xylanase DNA, protein and methods in use,” USA patent 5871730, 1999.
  12. J. Zhang, M. Siika-Aho, T. Puranen, M. Tang, M. Tenkanen, and L. Viikari, “Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw,” Biotechnology for Biofuels, vol. 4, article 12, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. R. Fagerstrom, T. Lahtinen, R. Lantto et al., “Production and secretion of actinomycete xylanases in a filamentous trichoderma fungus,” EP 0876494 B1, 2008.
  14. B. S. Priya, T. Stalin, and K. Selvam, “Efficient utilization of xylanase and lipase producing thermophilic marine actinomycetes (Streptomyces albus and Streptomyces hygroscopicus) in the production of ecofriendly alternative energy from waste,” African Journal of Biotechnology, vol. 11, no. 78, pp. 14320–14325, 2012.
  15. Y. B. Ammar, T. Matsubara, K. Ito et al., “New action pattern of a maltose-forming α-amylase from Streptomyces sp. and its possible application in bakery,” Journal of Biochemistry and Molecular Biology, vol. 35, no. 6, pp. 568–575, 2002. View at Scopus
  16. S. Kar and R. C. Ray, “Statistical optimization of α-amylase production by Streptomyces erumpens MTCC 7317 cells in calcium alginate beads using response surface methodology,” Polish Journal of Microbiology, vol. 57, no. 1, pp. 49–57, 2008. View at Scopus
  17. T. L. M. Stamford, N. P. Stamford, L. C. B. B. Coelho, and J. M. Araújo, “Production and characterization of a thermostable α-amylase from Nocardiopsis sp. endophyte of yam bean,” Bioresource Technology, vol. 76, no. 2, pp. 137–141, 2001. View at Publisher · View at Google Scholar · View at Scopus
  18. C.-H. Yang and W.-H. Liu, “Purification and properties of a maltotriose-producing alpha-amylase from Thermobifida fusca,” Enzyme and Microbial Technology, vol. 35, pp. 254–260, 2004.
  19. M. Kuddus, J. M. Roohi, J. M. Arif, and P. W. Ramteke, “An overview of cold-active microbial alpha-amylase: adaptation strategies and biotechnological potentials,” Biotechnology, vol. 10, pp. 246–258, 2011.
  20. N. Jacob, C. Asha Poorna, and P. Prema, “Purification and partial characterization of polygalacturonase from Streptomyces lydicus,” Bioresource Technology, vol. 99, no. 14, pp. 6697–6701, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. K. Horikoshi, “Alkaliphiles: some applications of their products for biotechnology,” Microbiology and Molecular Biology Reviews, vol. 63, no. 4, pp. 735–750, 1999. View at Scopus
  22. K. A. Moreira, B. F. Albuquerque, M. F. S. Teixeira, A. L. F. Porto, and J. L. Lima Filho, “Application of protease from Nocardiopsis sp. as a laundry detergent additive,” World Journal of Microbiology and Biotechnology, vol. 18, no. 4, pp. 307–312, 2002. View at Scopus
  23. P. Mitra and P. K. Chakrabartty, “An extracellular protease with depilation activity from Streptomyces nogalator,” Journal of Scientific and Industrial Research, vol. 64, no. 12, pp. 978–983, 2005. View at Scopus
  24. A. Brandelli, “Bacterial keratinases: useful enzymes for bioprocessing agroindustrial wastes and beyond,” Food and Bioprocess Technology, vol. 1, no. 2, pp. 105–116, 2008. View at Publisher · View at Google Scholar · View at Scopus
  25. B. Jaouadi, B. Abdelmalek, D. Fodil et al., “Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents,” Bioresource Technology, vol. 101, no. 21, pp. 8361–8369, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. D. Bhattacharya, A. Nagpure, and R. K. Gupta, “Bacterial chitinases: properties and potential,” Critical Reviews in Biotechnology, vol. 27, no. 1, pp. 21–28, 2007. View at Publisher · View at Google Scholar · View at Scopus
  27. N. N. Nawani, B. P. Kapadnis, A. D. Das, A. S. Rao, and S. K. Mahajan, “Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2,” Journal of Applied Microbiology, vol. 93, no. 6, pp. 965–975, 2002. View at Publisher · View at Google Scholar · View at Scopus
  28. 2011, http://www.reportlinker.com/p0747897-summary/World-Enzymes-Industry.html.
  29. The Freedonia group, “Industry Study with Forecasts for 2015 and 2020,” Study 2824, 2011.
  30. S. S. Dewan, “Global markets for enzymes in industrial applications (BIO030G),” BCC Research, 2011.
  31. S. S. Dewan, “Global Markets and Technologies for Biofuel Enzymes (EGY099A),” BCC Research, 2012.
  32. World Intellectual Property Organization, http://www.wipo.int.
  33. http://www.specialtyenzymes.com/seb-group-usa.
  34. 2010, http://www.newstatesman.com/healthcare-and-pharmaceuticals/2010/11/specialty-enzymes-global.
  35. 2012, http://forbesindia.com/article/breakpoint/novozyme-makes-enzymes-for-a-better-lifes/32760/1.
  36. M. Remya and R. Vijayakumar, “Isolation and characterization of marine antagonistic actinomycetes from west coast of India,” Medicine and Biology, vol. 15, no. 1, pp. 13–19, 2008.
  37. H. D. Jang and K. S. Chang, “Thermostable cellulases from Streptomyces sp.: scale-up production in a 50-l fermenter,” Biotechnology Letters, vol. 27, no. 4, pp. 239–242, 2005. View at Publisher · View at Google Scholar · View at Scopus
  38. R. K. Rathan and M. Ambili, “Cellulase Enzyme Production by Streptomyces Sp. Using Fruit Waste as Substrate,” Australian Journal of Basic and Applied Sciences, vol. 5, no. 12, pp. 1114–1118, 2011.
  39. H. M. Rifaat, Z. A. Nagieb, and Y. M. Ahmed, “Production of xylanases by Streptomyces species and their bleaching effect on rice straw pulp,” Applied Ecology and Environmental Research, vol. 4, no. 1, pp. 151–160, 2006. View at Scopus
  40. B. A. Kikani and S. P. Singh, “Single step purification and characterization of a thermostable and calcium independent α-amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam hot spring reservoir, Gujarat (India),” International Journal of Biological Macromolecules, vol. 48, no. 4, pp. 676–681, 2011. View at Publisher · View at Google Scholar · View at Scopus
  41. Y. J. Jeon, P. J. Park, and S. K. Kim, “Antimicrobial effect of chitooligosaccharides produced by bioreactor,” Carbohydrate Polymers, vol. 44, no. 1, pp. 71–76, 2001. View at Publisher · View at Google Scholar · View at Scopus
  42. S. L. Wang, W. H. Hsu, and T. W. Liang, “Conversion of squid pen by Pseudomonas aeruginosa K187 fermentation for the production of N-acetyl chitooligosaccharides and biofertilizers,” Carbohydrate Research, vol. 345, no. 7, pp. 880–885, 2010. View at Publisher · View at Google Scholar · View at Scopus
  43. S. Heumann, A. Eberl, H. Pobeheim et al., “New model substrates for enzymes hydrolysing polyethyleneterephthalate and polyamide fibres,” Journal of Biochemical and Biophysical Methods, vol. 69, no. 1-2, pp. 89–99, 2006. View at Publisher · View at Google Scholar · View at Scopus
  44. M. Jayaprakashvel, “Therapeutically active biomolecules from marine actinomycetes,” Journal of Modern Biotechnology, vol. 1, no. 1, pp. 1–7, 2012.
  45. J. M. Short and M. Keller, “High throughput screening for novel enzymes,” US Patent 6174673, 2001.
  46. M. Keller, M. W. Lafferty, and M. J. Short, “High throughput or capillary-based screening for a bioactivity or biomolecules,” EP1364052 A2, 2003.
  47. P. Lorenz, K. Liebeton, F. Niehaus, and J. Eck, “Screening for novel enzymes for biocatalytic processes: accessing the metagenome as a resource of novel functional sequence space,” Current Opinion in Biotechnology, vol. 13, no. 6, pp. 572–577, 2002.
  48. J. Kennedy, B. Flemer, S. A. Jackson et al., “Marine metagenomics: new tools for the study and exploitation of marine microbial metabolism,” Marine Drugs, vol. 8, pp. 608–628, 2010.
  49. M. Olsen, B. Iverson, and G. Georgiou, “High-throughput screening of enzyme libraries,” Current Opinion in Biotechnology, vol. 11, no. 4, pp. 331–337, 2000. View at Publisher · View at Google Scholar · View at Scopus
  50. D. P. Nannemann, W. R. Birmingham, R. A. Scism, and B. O. Bachmann, “Assessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis,” Future Medicinal Chemistry, vol. 3, no. 7, pp. 803–819, 2011. View at Publisher · View at Google Scholar · View at Scopus
  51. G. Yang and S. G. Withers, “Ultrahigh-throughput FACS-based screening for directed enzyme evolution,” ChemBioChem, vol. 10, no. 17, pp. 2704–2715, 2009. View at Publisher · View at Google Scholar · View at Scopus
  52. J. J. Agrestia, E. Antipov, A. R. Abatea et al., “Ultrahigh-throughput screening in drop-based microfluidics for directed evolution,” Proceedings of the National Academy of Sciences of the USA, vol. 107, pp. 4004–4009, 2010.
  53. C. Chang, J. Sustarich, R. Bharadwaj, A. Chandrasekaran, P. D. Adams, and A. K. Singh, “Droplet-based microfluidic platform for heterogeneous enzymatic assays,” Lab Chip 9, 2013.
  54. O. Paley, G. Agnello, J. Cantor, T. H. Yoo, and G. Georgiou E Stone, “GFP reporter screens for the engineering of amino acid degrading enzymes from libraries expressed in bacteria,” Methods in Molecular Biology, vol. 978, pp. 31–44, 2013.
  55. R. Ostafe, R. Prodanovic, U. Commandeur, and R. Fischer, “Flow cytometry-based ultra-high-throughput screening assay for cellulase activity,” Analytical Biochemsitry, vol. 435, no. 1, pp. 93–98, 2013.
  56. M. Akeroyd, M. Olsthoorn, J. Gerritsma et al., “Searching for microbiall protein over-expression in a complex matrix using automated high throughput MS-based proteomics tools,” Journal of Biotechnology, vol. 164, no. 1, pp. 112–120, 2013.
  57. C. Smith, X. Li, T. Mize et al., “Sensitive, high throughput detection of proteins in individual, surfactant stabilized picoliter droplets using NanoESI mass spectrometry,” Analytical Chemistry, 2013. View at Publisher · View at Google Scholar
  58. P. R. Murumkar, S. D. Gupta, V. P. Zambre, R. Giridhar, and M. R. Yadav, “Development of predictive 3D-QSAR CoMFA and CoMSIA models for β-aminohydroxamic acid-derived tumor necrosis factor-α converting enzyme inhibitors,” Chemical Biology and Drug Design, vol. 73, no. 1, pp. 97–107, 2009. View at Publisher · View at Google Scholar · View at Scopus