Bacterial Xylanase in Pseudomonas boreopolis LUQ1 is Highly Induced by Xylose

Authors Affiliation(s)

  • 1Institute of Insect Science, Department of Plant Protection, Zhejiang University, Hangzhou 310058, CHINA
  • 2Department of Biology, Lakehead University, Thunder Bay, P7B5E1, Ontario, CANADA
  • 3College of Biological and Environmental Engineering, Zhejiang University of Technology, Hangzhou 310014, CHINA

Can J Biotech, Volume 1Issue 3,  Pages 73-79,  DOI: https://doi.org/10.24870/cjb.2017-000112

Received: Sep 10, 2017; Revised: Oct 25, 2017; Accepted: Oct 26, 2017

Abstract

A xylanase producing bacterium was isolated from paper mill sludge in Thunder Bay, Canada. The newly isolated bacterium was identified as Pseudomonas boreopolis according to its 16S rRNA gene sequence and designated as LUQ1. The zymogram analysis indicated that there was one band of protein with xylanase activity, and the molecular weight of the enzyme was about 20 kDa. This xylanase works best at pH 6.0 and 65°C. The xylanase can be induced to express by xylose. The expression was enhanced on increasing the concentration of xylose, which reached its highest activity at 12 mM of xylose in fermentation. Wheat bran was the best carbon source in submerged fermentation. The highest xylanase activity of 25.61 U/ml was obtained at 96 h using wheat bran feedstock. When barley straw and wheat bran were used as feedstocks, the addition of 10 mM of xylose increased xylanase activity by ~50% and ~15%, respectively. The results showed that the strain LUQ1 has a great potential to produce xylanase for industrial applications.

References

  1. Biely, P. (1985) Microbial xylanolytic systems.  Trends Biotechnol 3: 286-290. Crossref
  2. Beg, Q.K., Kapoor, M., Mahajan, L. and Hoondal, G.S. (2001) Microbial xylanases and their industrial applications: a review.  Appl Microbiol Biotechnol 56: 326-338. Crossref
  3. Li, T. and He, J. (2016) Simultaneous saccharification and fermentation of hemicellulose to butanol by a non-sporulating clostridium species.  Bioresour Technol 219: 430-438. Crossref
  4. Bajpai, P. (1999) Application of enzymes in the pulp and paper industry.  Biotechnol Prog 15: 147-157. Crossref
  5. Battan, B., Sharma, J., Dhiman, S.S. and Kuhad, R.C. (2007) Enhanced production of cellulase-free thermostable xylanase by Bacillus pumilus ASH and its potential application in paper industry.  Enzyme Microb Technol 41: 733-739. Crossref
  6. Kulkarni,  N.,  Shendye,  A.  and  Rao,  M.  (1999) Molecular and biotechnological aspects of xylanases.  FEMS Microbiol Rev 23: 411-456. Crossref
  7. Nagar, S., Mittal, A., Kumar, D. and Gupta V.K. (2012) Production of alkali tolerant cellulase free xylanase in high levels by Bacillus pumilus SV-205.  Int J Biol Macromol 50: 414-420. Crossref
  8. Chapla, D., Patel, H., Singh, A., Madamwar, D. and Shah, A. (2012) Production, purification and properties of a cellulase-free thermostable endoxylanase from newly isolated Paenibacillus sp. ASCD2. Ann Microbiol 62:  825-834. Crossref
  9. Sá-Pereira, P., Mesquita, A., Duarte, J.C., Barros, M.R.A. and Costa-Ferreira, M. (2002) Rapid production of thermostable cellulase-free xylanase by a strain of Bacillus subtilis and its properties.  Enzyme Microb Technol 30: 924-933.Crossref
  10. Sharma, A., Adhikari, S. and Satyanarayana, T. (2007) Alkali-thermostable and cellulase-free xylanase production by an extreme thermophile Geobacillus thermoleovorans. World J Microb Biotechnol 23: 483-490.  Crossref
  11. Nagar, S., Mittal, A., Kumar, D., Kumar, L., Kuhad, R.C. and Gupta, V.K. (2011) Hyper production of alkali stable xylanase in lesser duration by Bacillus pumilus SV-85S using wheat bran under solid state fermentation.  N Biotechnol 28: 581-587. Crossref
  12. Bailey, M.J., Biely, P. and Poutanen, K. (1992) Interlaboratory testing of methods for assay of xylanase activity.  J Biotechnol 23: 257-270. Crossref
  13. Miller, G.L. (1959) Use of DNS reagent for the measurement of reducing sugar.  Anal Chem 31: 426-428. Crossref
  14. Ghose, T.K. (1987) Measurement of cellulase activities.  Pure appl Chem 59: 257-268.Crossref
  15. Mach-Aigner, A.R., Pucher, M.E. and Mach, R.L. (2010) D-Xylose as a repressor or inducer of xylanase expression in Hypocrea jecorina (Trichoderma reesei). Appl Environ Microb 76: 1770-1776. Crossref
  16. Prathumpai, W., McIntyre, M. and Nielsen, J. (2004) The effect of CreA in glucose and xylose catabolism in Aspergillus nidulans . Appl Microbiol Biotechnol 63:748-753. Crossref
  17. Merali, Z., Collins, S. R.A., Elliston, A., Wilson, D. R., Käsper, A. and Waldron, K. W. (2015) Characterization of cell wall components of wheat bran following hydrothermal pretreatment and fractionation.  Biotechnol Biofuels 8: 23. Crossref
  18. Ko, C.H., Lin, Z.P., Tu, J., Tsai, C.H., Liu, C.C., Chen, H.T. and Wang, T.P. (2010) Xylanase production by Paenibacillus campinasensis BL11 and its pretreatment of hardwood kraft pulp bleaching.  Int Biodeterior Biodegradation 64:13-19.Crossref
  19. Mamo, G., Hatti-Kaul, R. and Mattiasson, B. (2006) A thermostable alkaline active endo-β-1-4-xylanase from Bacillus halodurans S7: Purification and characterization.  Enzyme Microb Technol 39:1492-1498. Crossref
  20. Wu, Y.R. and He, J. (2015) Characterization of a xylanase-producing Cellvibrio mixtus strain J3-8 and its genome analysis.  Sci Rep 5: 10521. Crossref
  21. Chauhan, S., Choudhury, B., Singh, S.N. and Ghosh, P. (2006) Application of xylanase enzyme of Bacillus coagulans as a prebleaching agent on non-woody pulps. Process Biochem 41:226-231. Crossref