Table of Contents Author Guidelines Submit a Manuscript
International Journal of Microbiology
Volume 2017, Article ID 4018398, 12 pages
https://doi.org/10.1155/2017/4018398
Research Article

Gene Expression and Molecular Characterization of a Xylanase from Chicken Cecum Metagenome

1Department of Microbiology, Faculty of Science, Mahidol University, Ratchathewi, Bangkok 10400, Thailand
2Chemical and Petrochemical Research Center, Commission for Research and Industrial Development, Ministry of Industry and Minerals, 10068 Baghdad, Iraq

Correspondence should be addressed to Suthep Wiyakrutta; ht.ca.lodiham@yiw.pehtus

Received 21 March 2017; Revised 15 May 2017; Accepted 23 May 2017; Published 2 July 2017

Academic Editor: Hugh W. Morgan

Copyright © 2017 Hind AL-Darkazali 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. J. L. Adrio and A. L. Demain, “Microbial enzymes: tools for biotechnological processes,” Biomolecules, vol. 4, no. 1, pp. 117–139, 2014. View at Publisher · View at Google Scholar · View at Scopus
  2. A. Bhardwaj, P. Mahanta, S. Ramakumar, A. Ghosh, S. Leelavathi, and V. S. Reddy, “Emerging role of N- and C-terminal interactions in stabilizing (β/a)8 fold with special emphasis on Family 10 xylanases,” Computational and Structural Biotechnology Journal, vol. 2, no. 3, article e201209014, 2012. View at Publisher · View at Google Scholar · View at Scopus
  3. O. Adeola and A. J. Cowieson, “Board-invited review: opportunities and challenges in using exogenous enzymes to improve nonruminant animal production,” Journal of Animal Science, vol. 89, no. 10, pp. 3189–3218, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. D. Verma and T. Satyanarayana, “Molecular approaches for ameliorating microbial xylanases,” Bioresource Technology, vol. 117, pp. 360–367, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. D. Driss, F. Bhiri, M. Siela, R. Ghorbel, and S. E. Chaabouni, “Purification and properties of a thermostable xylanase GH 11 from Penicillium occitanis Pol6,” Applied Biochemistry and Biotechnology, vol. 168, no. 4, pp. 851–863, 2012. View at Publisher · View at Google Scholar · View at Scopus
  6. A. Gasparic, J. Martin, A. S. Daniel, and H. J. Flint, “A xylan hydrolase gene cluster in prevotella ruminicola B14: sequence relationships, synergistic interactions, and oxygen sensitivity of a novel enzyme with exoxylanase and β-(1,4)-xylosidase activities,” Applied and Environmental Microbiology, vol. 61, no. 8, pp. 2958–2964, 1995. View at Google Scholar · View at Scopus
  7. Y. Gu, Y. Ding, C. Ren et al., “Reconstruction of xylose utilization pathway and regulons in firmicutes,” BMC Genomics, vol. 11, no. 1, article 255, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. E. Fierens, S. Rombouts, K. Gebruers et al., “TLXI, a novel type of xylanase inhibitor from wheat (Triticum aestivum) belonging to the thaumatin family,” Biochemical Journal, vol. 403, no. 3, pp. 583–591, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Shi, Y. Zhang, X. Li et al., “A novel highly thermostable xylanase stimulated by Ca2+ from thermotoga thermarum: cloning, expression and characterization,” Biotechnology for Biofuels, vol. 6, pp. 1–9, 2013. View at Publisher · View at Google Scholar · View at Scopus
  10. G. C. Mead, “Microbes of the avian cecum: types present and substrates utilized,” Journal of Experimental Zoology, vol. 252, pp. 48–54, 1989. View at Publisher · View at Google Scholar · View at Scopus
  11. S. Zhao, J. Wang, D. Bu et al., “Novel glycoside hydrolases identified by screening a chinese holstein dairy cow rumen-derived metagenome library,” Applied and Environmental Microbiology, vol. 76, no. 19, pp. 6701–6705, 2010. View at Publisher · View at Google Scholar · View at Scopus
  12. M. J. Sergeant, C. Constantinidou, T. A. Cogan, M. R. Bedford, C. W. Penn, and M. J. Pallen, “Extensive microbial and functional diversity within the chicken cecal microbiome,” PLoS ONE, vol. 9, no. 3, Article ID e91941, 2014. View at Publisher · View at Google Scholar · View at Scopus
  13. Z. Tu, G. He, K. X. Li et al., “An improved system for competent cell preparation and high efficiency plasmid transformation using different Escherichia coli strains,” Electronic Journal of Biotechnology, vol. 8, no. 1, pp. 113–120, 2005. View at Publisher · View at Google Scholar
  14. J. Vikramathithan, G. Nirmal Kumar, P. Muthuraman, and K. Srikumar, “Purification and characterization of thermophilic xylanase isolated from the xerophytic-Cereus pterogonus SP,” The Protein Journal, vol. 29, no. 7, pp. 481–486, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. H.-C. Zheng, M.-Z. Sun, L.-C. Meng et al., “Purification and characterization of a thermostable xylanase from Paenibacillus sp. NF1 and its application in xylooligosaccharides production,” Journal of Microbiology and Biotechnology, vol. 24, no. 4, pp. 489–496, 2014. View at Publisher · View at Google Scholar · View at Scopus
  16. G. L. Miller, “Use of dinitrosalicylic acid reagent for determination of reducing sugar,” Analytical Chemistry, vol. 31, no. 3, pp. 426–428, 1959. View at Publisher · View at Google Scholar · View at Scopus
  17. O. Gallardo, P. Diaz, and F. I. J. Pastor, “Characterization of a Paenibacillus cell-associated xylanase with high activity on aryl-xylosides: a new subclass of family 10 xylanases,” Applied Microbiology and Biotechnology, vol. 61, no. 3, pp. 226–233, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. Y. S. Jeong, H. B. Na, S. K. Kim et al., “Characterization of Xyn10J, a novel family 10 xylanase from a compost metagenomic library,” Applied Biochemistry and Biotechnology, vol. 166, no. 5, pp. 1328–1339, 2012. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Khandeparker, P. Verma, and D. Deobagkar, “A novel halotolerant xylanase from marine isolate Bacillus subtilis cho40: Gene cloning and sequencing,” New Biotechnology, vol. 28, no. 6, pp. 814–821, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. N. C. D. A. Guimaraes, M. Sorgatto, S. D. C. Peixoto-Nogueira et al., “Bioprocess and biotechnology: effect of xylanase from Aspergillus niger and Aspergillus flavus on pulp biobleaching and enzyme production using agroindustrial residues as substract,” SpringerPlus, vol. 2, no. 1, article 380, pp. 1–7, 2013. View at Publisher · View at Google Scholar · View at Scopus
  21. L. da Silva, C. R. F. Terrasan, and E. C. Carmona, “Purification and characterization of xylanases from Trichoderma inhamatum,” Electronic Journal of Biotechnology, vol. 18, no. 4, pp. 307–313, 2015. View at Publisher · View at Google Scholar · View at Scopus
  22. G. C. Pradeep, Y. H. Choi, Y. S. Choi et al., “A novel thermostable cellulase free xylanase stable in broad range of pH from Streptomyces sp. CS428,” Process Biochemistry, vol. 48, no. 8, pp. 1188–1196, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. Z. Gao, L. Ruan, X. Chen, Y. Zhang, and X. Xu, “A novel salt-tolerant endo-β-1,4-glucanase Cel5A in Vibrio sp. G21 isolated from mangrove soil,” Applied Microbiology and Biotechnology, vol. 87, no. 4, pp. 1373–1382, 2010. View at Publisher · View at Google Scholar · View at Scopus
  24. B. Henrissat, I. Callebaut, S. Fabrega, P. Lehn, J.-P. Mornon, and G. Davies, “Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 15, pp. 7090–7094, 1995. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Roberge, C. Dupont, R. Morosoli, F. Shareck, and D. Kluepfel, “Asparagine-127 of xylanase A from Streptomyces lividans, a key residue in glycosyl hydrolases of superfamily 4/7: kinetic evidence for its involvement in stabilization of the catalytic intermediate,” Protein Engineering, vol. 10, no. 4, pp. 399–403, 1997. View at Publisher · View at Google Scholar · View at Scopus
  26. B. Xu, L. Dai, J. Li et al., “Molecular and biochemical characterization of a novel xylanase from Massilia sp. RBM26 isolated from the feces of Rhinopithecus bieti,” Journal of Microbiology and Biotechnology, vol. 26, no. 1, pp. 9–19, 2015. View at Publisher · View at Google Scholar · View at Scopus
  27. M. Biasini, S. Bienert, A. Waterhouse et al., “SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information,” Nucleic Acids Research, vol. 42, no. 1, pp. W252–W258, 2014. View at Publisher · View at Google Scholar · View at Scopus
  28. X. Gong, R. J. Gruniniger, R. J. Forster, R. M. Teather, and T. A. McAllister, “Biochemical analysis of a highly specific, pH stable xylanase gene identified from a bovine rumen-derived metagenomic library,” Applied Microbiology and Biotechnology, vol. 97, no. 6, pp. 2423–2431, 2013. View at Publisher · View at Google Scholar · View at Scopus
  29. T. M. Alvarez, R. Goldbeck, C. R. D. Santos et al., “Development and biotechnological application of a novel endoxylanase family GH10 identified from sugarcane soil metagenome,” PLoS ONE, vol. 8, no. 7, article e70014, 2013. View at Publisher · View at Google Scholar · View at Scopus
  30. P. W. J. J. Van Der Wielen, S. Biesterveld, S. Notermans, H. Hofstra, B. A. P. Urlings, and F. Van Knapen, “Role of volatile fatty acids in development of the cecal microflora in broiler chickens during growth,” Applied and Environmental Microbiology, vol. 66, no. 6, pp. 2536–2540, 2000. View at Publisher · View at Google Scholar · View at Scopus
  31. Y. Takahashi, H. Kawabata, and S. Murakami, “Analysis of functional xylanases in xylan degradation by Aspergillus niger E-1 and characterization of the GH family 10 xylanase XynVII,” SpringerPlus, vol. 2, article 447, 2013. View at Publisher · View at Google Scholar · View at Scopus
  32. M. L. T. M. Polizeli, A. C. S. Rizzatti, R. Monti, H. F. Terenzi, J. A. Jorge, and D. S. Amorim, “Xylanases from fungi: properties and industrial applications,” Applied Microbiology and Biotechnology, vol. 67, no. 5, pp. 577–591, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. C. S. Rupert, “Photoenzymatic repair of ultraviolet damage in DNA. II. formation of an enzyme-substrate complex,” The Journal of general physiology, vol. 45, pp. 725–741, 1962. View at Publisher · View at Google Scholar · View at Scopus
  34. A. Varga, F. Beáta, É. Gráczer, S. Osváth, A. N. Szilágyi, and M. Vas, “Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase,” FEBS Journal, vol. 272, no. 8, pp. 1867–1885, 2005. View at Publisher · View at Google Scholar · View at Scopus
  35. B. Guo, X.-L. Chen, C.-Y. Sun, B.-C. Zhou, and Y.-Z. Zhang, “Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241,” Applied Microbiology and Biotechnology, vol. 84, no. 6, pp. 1107–1115, 2009. View at Publisher · View at Google Scholar · View at Scopus
  36. S. Heo, J. Kwak, H.-W. Oh et al., “Characterization of an extracellular xylanase in paenibacillus sp. HY-8 isolated from an herbivorous longicorn beetle,” Journal of Microbiology and Biotechnology, vol. 16, no. 11, pp. 1753–1759, 2006. View at Google Scholar · View at Scopus
  37. A. Margolles and C. G. De los Reyes-Gavilán, “Purification and functional characterization of a novel α-L-arabinofuranosidase from Bifidobacterium longum B667,” Applied and Environmental Microbiology, vol. 69, no. 9, pp. 5096–5103, 2003. View at Publisher · View at Google Scholar · View at Scopus
  38. M. B. Fialho and E. C. Carmona, “Purification and characterization of xylanases from Aspergillus giganteus,” Folia Microbiologica, vol. 49, no. 1, pp. 13–18, 2004. View at Publisher · View at Google Scholar · View at Scopus
  39. S. Mohana, A. Shah, J. Divecha, and D. Madamwar, “Xylanase production by Burkholderia sp. DMAX strain under solid state fermentation using distillery spent wash,” Bioresource Technology, vol. 99, no. 16, pp. 7553–7564, 2008. View at Publisher · View at Google Scholar · View at Scopus
  40. D. Verma, Y. Kawarabayasi, K. Miyazaki, and T. Satyanarayana, “Cloning, expression and characteristics of a novel alkalistable and thermostablexylanase encoding gene ( Mxyl ) retrieved from compost-soil metagenome,” PLoS ONE, vol. 8, no. 1, article e52459, 2013. View at Publisher · View at Google Scholar · View at Scopus
  41. M. A. Rahman, Y. H. Choi, G. C. Pradeep et al., “An alkaline and metallo-protein type endo xylanase from Streptomyces sp. CSWu-1,” Biotechnology and Bioprocess Engineering, vol. 19, no. 2, pp. 311–319, 2014. View at Publisher · View at Google Scholar · View at Scopus
  42. W. Bai, Y. Xue, C. Zhou, and Y. Ma, “Cloning, expression and characterization of a novel salt-tolerant xylanase from Bacillus sp. SN5,” Biotechnology Letters, vol. 34, no. 11, pp. 2093–2099, 2012. View at Publisher · View at Google Scholar · View at Scopus
  43. X. Li, Y. She, B. Sun et al., “Purification and characterization of a cellulase-free, thermostable xylanase from Streptomyces rameus L2001 and its biobleaching effect on wheat straw pulp,” Biochemical Engineering Journal, vol. 52, no. 1, pp. 71–78, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. D. Morrison, J. S. van Dyk, and B. I. Pletschke, “The effect of alcohols, lignin and phenolic compounds on the enzyme activity of Clostridium cellulovorans XynA,” Bioresources, vol. 6, pp. 3132–3141, 2011. View at Google Scholar · View at Scopus
  45. J. L. S. Lemos, E. P. S. Bon, M. D. F. E. Santana, and N. Pereira Jr., “Thermal stability of xylanases produced by Aspergillus awamori,” Brazilian Journal of Microbiology, vol. 31, pp. 206–211, 2000. View at Google Scholar · View at Scopus
  46. K. S. Bae, C. K. Sung, Y. H. Rhee et al., “Novel alkali-tolerant GH10 endo-ß-1, 4-xylanase with broad substrate specificity from Microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpaorientalis,” Journal of Microbiology and Biotechnology, vol. 24, no. 7, pp. 943–953, 2014. View at Google Scholar
  47. P. Dheeran, N. Nandhagopal, S. Kumar, Y. K. Jaiswal, and D. K. Adhikari, “A novel thermostable xylanase of Paenibacillus macerans IIPSP3 isolated from the termite gut,” Journal of Industrial Microbiology and Biotechnology, vol. 39, no. 6, pp. 851–860, 2012. View at Publisher · View at Google Scholar · View at Scopus
  48. J. Zhou, H. Huang, K. Meng et al., “Molecular and biochemical characterization of a novel xylanase from the symbiotic Sphingobacterium sp. TN19,” Applied Microbiology and Biotechnology, vol. 85, no. 2, pp. 323–333, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. D. Y. Kim, M. K. Han, J. S. Lee et al., “Isolation and characterization of a cellulase-free endo-β-1,4-xylanase produced by an invertebrate-symbiotic bacterium, Cellulosimicrobium sp. HY-13,” Process Biochemistry, vol. 44, no. 9, pp. 1055–1059, 2009. View at Publisher · View at Google Scholar · View at Scopus
  50. J. An, Y. Xie, Y. Zhang et al., “Characterization of a thermostable, specific GH10 xylanase from Caldicellulosiruptor bescii with high catalytic activity,” Journal of Molecular Catalysis B: Enzymatic, vol. 117, pp. 13–20, 2015. View at Publisher · View at Google Scholar · View at Scopus
  51. C. Mirande, P. Mosoni, C. Béra-Maillet, A. Bernalier-Donadille, and E. Forano, “Characterization of Xyn10A, a highly active xylanase from the human gut bacterium Bacteroides xylanisolvens XB1A,” Applied Microbiology and Biotechnology, vol. 87, no. 6, pp. 2097–2105, 2010. View at Publisher · View at Google Scholar · View at Scopus
  52. M. S. Butt, M. Tahir-Nadeem, Z. Ahmad, and M. T. Sultan, “Xylanases and their applications in baking industry,” Food Technology and Biotechnology, vol. 46, no. 1, pp. 22–31, 2008. View at Google Scholar · View at Scopus
  53. Z. Lei, Y. Shao, X. Yin, D. Yin, Y. Guo, and J. Yuan, “Combination of xylanase and debranching enzymes specific to wheat arabinoxylan improve the growth performance and gut health of broilers,” Journal of Agricultural and Food Chemistry, vol. 64, no. 24, pp. 4932–4942, 2016. View at Publisher · View at Google Scholar · View at Scopus