全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Taxonomy and Polyphasic Characterization of Alkaline Amylase Producing Marine Actinomycete Streptomyces rochei BTSS 1001

DOI: 10.1155/2013/276921

Full-Text   Cite this paper   Add to My Lib

Abstract:

Actinomycetes isolated from marine sediments along the southeast coast of Bay of Bengal were investigated for amylolytic activity. Marine actinomycete BTSS 1001 producing an alkaline amylase was identified from marine sediment of Diviseema coast, Bay of Bengal. The isolate produced alkaline amylase with maximum amylolytic activity at pH 9.5 at 50°C. The organism produced white to pale grey substrate mycelium and grayish aerial mycelium with pinkish brown pigmentation. A comprehensive study of morphological, physiological parameters, cultural characteristics, and biochemical studies was performed. The presence of iso-C15?:?0, anteiso-C15?:?0, iso-C16?:?0, and anteiso-C17?:?0 as the major cellular fatty acids, LL-diaminopimelic acid as the characteristic cell wall component, and menaquinones MK-9H(6) and MK-9H(8) as the major isoprenoid quinones is attributed to the strain BTSS 1001 belonging to the genus Streptomyces. Comparison of 16S rRNA gene sequences showed that strain BTSS 1001 exhibited the highest similarities to the type strains of Streptomyces rochei (99%), Streptomyces plicatus (99%), and Streptomyces enissocaesilis (99%). Using the polyphasic taxonomical approach and phenotypic characteristic studies, the isolate BTSS 1001 was characterized as marine actinomycete Streptomyces rochei. 1. Introduction Actinomycetes have long been reported as important source of biotechnologically important compounds. The recent focus is on marine Actinomycetes as a source of bioactive compounds and industrial enzymes. This is due to the fact that terrestrial actinomycetes have been exhaustively analyzed for bioactive compounds and enzymes but they still fall short of industrial application. Thus, the need of the hour is to identify newer sources capable of withstanding the conditions of industrial and commercial applications. Studies by several researchers [1–4] on marine actinomycetes have reported diversity and presence of unique marine taxa in ocean sediments. Their survival in extreme conditions in the ocean sediments demonstrates their ability for adaptation and production of different types of bioactive compounds as compared to their terrestrial counterparts [5]. Marine actinomycetes have been established as a rich source of several secondary metabolites such as novel bioactive molecules like antibiotics, antifungal, and anticancer compounds, plant growth hormones, industrially important enzymes, enzyme inhibitors, and pigments [6, 7]. Culturally independent methods and polyphasic approaches have also demonstrated that marine sediments contain wide range

References

[1]  T. J. Mincer, P. R. Jensen, C. A. Kauffman, and W. Fenical, “Widespread and persistent populations of a major new marine actinomycete taxon in ocean sediments,” Applied and Environmental Microbiology, vol. 68, no. 10, pp. 5005–5011, 2002.
[2]  J. E. M. Stach, L. A. Maldonado, D. G. Masson, A. C. Ward, M. Goodfellow, and A. T. Bull, “Statistical approaches for estimating actinobacterial diversity in marine sediments,” Applied and Environmental Microbiology, vol. 69, no. 10, pp. 6189–6200, 2003.
[3]  P. R. Jensen and W. Fenical, “New natural-product diversity from marine actinomycetes,” in Natural Products: Drug Discovery and Therapeutics Medicines, L. Zhang and A. Demain, Eds., vol. 5, pp. 315–328, Humana Press, 2005.
[4]  L. Zhang, R. An, J. Wang et al., “Exploring novel bioactive compounds from marine microbes,” Current Opinion in Microbiology, vol. 8, no. 3, pp. 276–281, 2005.
[5]  K. S. Lam, “Discovery of novel metabolites from marine actinomycetes,” Current Opinion in Microbiology, vol. 9, no. 3, pp. 245–251, 2006.
[6]  S. Dharmaraj, “Marine Streptomyces as a novel source of bioactive substances,” World Journal of Microbiology and Biotechnology, vol. 26, no. 12, pp. 2123–2139, 2010.
[7]  T. W. Hodges, M. Slattery, and J. B. Olson, “Unique actinomycetes from marine caves and coral reef sediments provide novel PKS and NRPS biosynthetic gene clusters,” Marine Biotechnology, vol. 14, no. 3, pp. 270–280, 2012.
[8]  A. T. Bull, A. C. Ward, and M. Goodfellow, “Search and discovery strategies for biotechnology: the paradigm shift,” Microbiology and Molecular Biology Reviews, vol. 64, no. 3, pp. 573–606, 2000.
[9]  N. A. Magarvey, J. M. Keller, V. Bernan, M. Dworkin, and D. H. Sherman, “Isolation and characterization of novel marine-derived actinomycete taxa rich in bioactive metabolites,” Applied and Environmental Microbiology, vol. 70, no. 12, pp. 7520–7529, 2004.
[10]  A. S. Anderson and E. M. H. Wellington, “The taxonomy of Streptomyces and related genera,” International Journal of Systematic and Evolutionary Microbiology, vol. 51, no. 3, pp. 797–814, 2001.
[11]  A. Pandey, P. Nigam, C. R. Soccol, V. T. Soccol, D. Singh, and R. Mohan, “Advances in microbial amylases,” Biotechnology and Applied Biochemistry, vol. 31, no. 2, pp. 135–152, 2000.
[12]  M. J. van der Maarel, B. van der Veen, J. Uitdehaag, H. Leemhuis, and L. Dijkhuizen, “Properties and applications of starch-converting enzymes of the α-amylase family,” Journal of Biotechnology, vol. 94, no. 2, pp. 137–155, 2002.
[13]  H. W. G. Kuilderd, “Applied technology-simultaneous desizing and scouring with enzymes-simultaneous fabric desizing and scouring, using alkaline alpha-amylase and an alkaline scouring enzyme, reduces water,” American Association of Textile Chemists and Colorists, vol. 8, pp. 33–36, 2008.
[14]  M. Antoinette Mc Tigue, C. T. Kelly, E. M. Doyle, and W. M. Fogarty, “The alkaline amylase of the alkalophilic Bacillus sp. IMD 370,” Enzyme and Microbial Technology, vol. 17, no. 6, pp. 570–573, 1995.
[15]  H. Yang, L. Liu, J. Li, G. Du, and J. Chen, “Heterologous expression, biochemical characterization, and overproduction of alkaline alpha-amylase from Bacillus alcalophilus in Bacillus subtilis,” Microbial Cell Factories, vol. 10, article 77, 2011.
[16]  A. Burhan, U. Nisa, C. G?khan, C. ?mer, A. Ashabil, and G. Osman, “Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6,” Process Biochemistry, vol. 38, no. 10, pp. 1397–1403, 2003.
[17]  S. O. Hashim, O. D. Delgado, M. A. Martínez, R.-H. Kaul, F. J. Mulaa, and B. Mattiasson, “Alkaline active maltohexaose-forming α-amylase from Bacillus halodurans LBK 34,” Enzyme and Microbial Technology, vol. 36, no. 1, pp. 139–146, 2005.
[18]  N. Hmidet, A. Bayoudh, J. G. Berrin, S. Kanoun, N. Juge, and M. Nasri, “Purification and biochemical characterization of a novel α-amylase from Bacillus licheniformis NH1. Cloning, nucleotide sequence and expression of amyN gene in Escherichia coli,” Process Biochemistry, vol. 43, no. 5, pp. 499–510, 2008.
[19]  B. Arikan, “Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from a thermophilic Bacillus sp. isolate A3-15,” Bioresource Technology, vol. 99, no. 8, pp. 3071–3076, 2008.
[20]  B. H. Joshi, “A novel thermostable alkaline α-amylase from bacillus circulans PN5: biochemical characterization and production,” Asian Journal of Biotechnology, vol. 3, pp. 58–67, 2007.
[21]  D. G. Syed, D. Agasar, and A. Pandey, “Production and partial purification of α-amylase from a novel isolate Streptomyces gulbargensis,” Journal of Industrial Microbiology and Biotechnology, vol. 36, no. 2, pp. 189–194, 2009.
[22]  R. K. Saxena, K. Dutt, L. Agarwal, and P. Nayyar, “A highly thermostable and alkaline amylase from a Bacillus sp. PN5,” Bioresource Technology, vol. 98, no. 2, pp. 260–265, 2007.
[23]  R. Nakai, T. Sato, and K. Okamoto, “Manufacture of alkaline amylase with Streptomyces,” Japanese Kokai Tokkyo Koho, vol. 86, no. 209, 588, 1986.
[24]  S. Chakraborty, R. G. A. Khopade, K. Mahadik, and C. Kokare, “Study on calcium ion independent α -amylase from haloalkaliphilic marine Streptomyces strain A3,” Indian Journal of Biotechnology, vol. 11, JP2000060546A2, pp. 427–437, 2012.
[25]  S. Chakraborty, A. Khopade, C. Kokare, K. Mahadik, and B. Chopade, “Isolation and characterization of novel α-amylase from marine Streptomyces sp. D1,” Journal of Molecular Catalysis B, vol. 58, no. 1–4, pp. 17–23, 2009.
[26]  S. Chakraborty, R. G. A. Khopade, K. Mahadik, and C. Kokare, “Study on calcium ion independent α -amylase from haloalkaliphilic marine Streptomyces strain A3,” Indian Journal of Biotechnology, vol. 11, pp. 427–437, 2012.
[27]  S. Ramesh and N. Mathivanan, “Screening of marine actinomycetes isolated from the Bay of Bengal, India for antimicrobial activity and industrial enzymes,” World Journal of Microbiology and Biotechnology, vol. 25, no. 12, pp. 2103–2111, 2009.
[28]  J. Berger, L. M. Jampolsky, and M. W. Goldberg, “A guide to the classification of the actinomycetes and their antibiotics,” in A Guide to the Classification of the Actinomycetes and their Antibiotics, S. A. W. Lechevalier and H. A. Baltimore, Eds., pp. 1–246, The Williams & Wilkins, 1953.
[29]  G. L. Miller, “Use of dinitrosalicylic acid reagent for determination of reducing sugar,” Analytical Chemistry, vol. 31, no. 3, pp. 426–428, 1959.
[30]  O. H. Lowry, N. J. Rosenbrough, A. L. Fan, and R. J. Randall, “Protein estimation with the Folinphenol reagent,” Indian Journal of Biotechnology, vol. 193, pp. 265–275, 1951.
[31]  E. B. Shirling and D. Gottlieb, “Methods for characterization of Streptomyces species,” International Journal of Systematic and Evolutionary Microbiology, vol. 16, pp. 313–340, 1966.
[32]  M. Goodfellow, “Numerical taxonomy of some nocardioform bacteria,” Journal of General Microbiology, vol. 69, no. 1, pp. 33–80, 1971.
[33]  R. E. Gordon, D. A. Barnett, J. E. Handerhan, and C. Hor Nay Pang, “Nocardia coeliaca, Nocardia autotrophica, and the Nocardin strain,” International Journal of Systematic Bacteriology, vol. 24, no. 1, pp. 54–63, 1974.
[34]  S. T. Williams, S. Lanning, and E. M. H. Wellington, “Ecology of actinomycetes,” in The Biology of the Actinomycetes, M. Goodfellow, M. Mordarski, and S. T. Williams, Eds., pp. 481–528, Academic Press, London, U.K, 1984.
[35]  T. Hasegawa, M. Takizawa, and S. Tanida, “A rapid analysis for chemical grouping of aerobic actinomycetes,” Journal of General and Applied Microbiology, vol. 29, no. 4, pp. 319–322, 1983.
[36]  J. L. Staneck and G. D. Roberts, “Simplified approach to identification of aerobic actinomycetes by thin layer chromatography,” Journal of Applied Microbiology, vol. 28, no. 2, pp. 226–231, 1974.
[37]  D. E. Minnikin, I. G. Hutchinson, A. B. Caldicott, and M. Goodfellow, “Thin-layer chromatography of methanolysates of mycolic acid-containing bacteria,” Journal of Chromatography A, vol. 188, no. 1, pp. 221–233, 1980.
[38]  M. D. Collins, “Isoprenoid quinone analyses in bacterial classification and identification,” in Bacterial Systematics, M. Goodfellow and D. E. Minnikin, Eds., pp. 267–287, Academic Press, London, UK, 1985.
[39]  M. Sasser, Technical Note 101: Identification of Bacteria by Gas Chromatography of Cellular Fatty Acids, MIDI, North Newark, Del, USA, 1991.
[40]  R. M. Kroppenstedt, “Fatty acid and menaquinone analysis of actinomycetes and related organisms,” in Chemical Methods in Bacterial Systematics, M. Goodfellow and D. E. Minnikin, Eds., pp. 173–199, Elsevier Science & Technology Books, London, UK, 1985.
[41]  W.-J. Li, P. Xu, P. Schumann et al., “Georgenia ruanii sp. nov., a novel actinobacterium isolated from forest soil in Yunnan (China), and emended description of the genus Georgenia,” International Journal of Systematic and Evolutionary Microbiology, vol. 57, no. 7, pp. 1424–1428, 2007.
[42]  A. Morgulis, G. Coulouris, Y. Raytselis, T. L. Madden, R. Agarwala, and A. A. Sch?ffer, “Database indexing for production MegaBLAST searches,” Bioinformatics, vol. 24, no. 16, pp. 1757–1764, 2008.
[43]  J. D. Thompson, T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins, “The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools,” Nucleic Acids Research, vol. 25, no. 24, pp. 4876–4882, 1997.
[44]  J. Felsenstein, “Evolutionary trees from DNA sequences: a maximum likelihood approach,” Journal of Molecular Evolution, vol. 17, no. 6, pp. 368–376, 1981.
[45]  J. Felsenstein, “PHYLIP (Phylogeny Inference Package) version 3.6.,” Tech. Rep., Department of Genome Sciences, University of Washington, Seattle, Wash, USA, 2005.
[46]  R. Page, “TreeView: an application to display phylogenetic trees on personal computers,” Computer Applications in the Biosciences, vol. 12, no. 4, pp. 357–358, 1996.
[47]  J. Felsenstein, “Confidence limits on phylogenies: an approach using the bootstrap,” Evolution, vol. 39, pp. 783–791, 1985.
[48]  V. S. Bernan, M. Greenstein, and W. M. Maiese, “Marine microorganisms as a source of new natural products,” Advances in Applied Microbiology, vol. 43, pp. 57–90, 1997.
[49]  S. Thippeswamy, K. Girigowda, and V. H. Mulimani, “Isolation and identification of α-amylase producing Bacillus sp. from dhal industry waste,” Indian Journal of Biochemistry and Biophysics, vol. 43, no. 5, pp. 295–298, 2006.

Full-Text

comments powered by Disqus

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133