Journal of Industrial Technology (산업기술연구)

Kangwon National University, Institute of Industrial Technology (강원대학교 산업기술연구소)
권호 표지
DOI QR코드

DOI QR Code

Cloning and expression of new laccase gene (soncotA) from Bacillus sonorensis KCTC13918 in E. coli

Bacillus sonorensis KCTC13918로부터 새로운 laccase유전자 (soncotA)의 클로닝과 대장균에서의 발현

  • Choi, Shin-Geon (Dept of Bioengineering and Technology, Kangwon National University) ;
  • Yoon, Hyeonjong (Dept of Bioengineering and Technology, Kangwon National University)
  • Received : 2017.04.13
  • Accepted : 2017.08.21
  • Published : 2017.08.31
Download PDF
⟨ Previous Next ⟩

Abstract

A new putative laccase gene (soncotA) which show 78% homology with that from Bacillus licheniformis (liccotA) was isolated from draft genome sequence of Bacillus sonorensis KCTC 13918. A 1,545 bp of PCR product corresponding 514 amino acids was cloned into NdeI-NotI site of pET21c and expressed as soluble form in E. coli. About 59 kDa size of recombinant laccase was purified into homogenity by Ni-NTA column and laccase activity was confirmed by zymography. The enzymatic properties of recombinant laccase were characterized. The specific activity of B. sonorensis laccase was 0.033 fold lower than that of Bacillus licheniformis laccase. The finding of new laccase gene broadened the enzymatic diversity of Bacillus species laccases.

Keywords

References

  1. Adimpong, D.B., Srensen, K.I., Nielsen, D.S., Thorsen, L., Rasmussen, T.B., Derkx, P.M.F., Jespersen, L., 2013, Draft whole-genome sequence of Bacillus sonorensis strain L12, a source of nonribosomal lipopeptides., Genome Announc. 1(2) e00097-13.
  2. Ausec, L., Zakrzewski, M., Goesmann, A., Schluter, A., Mandic-Mulec, I., 2011, Bioinformatic analysis reveals high diversity of bacterial genes for laccase-like enzymes., PLoS ONE 6(10) e25724. https://doi.org/10.1371/journal.pone.0025724
  3. Brander, S., Mikkelsen, J.D., Kepp, K.P., 2014, Characterization of an Alkali- and Halide-Resistant Laccase expressed in E. coli: CotA from Bacillus clausii., PLoS ONE 9(6) e99402. https://doi.org/10.1371/journal.pone.0099402
  4. Claus, H., 2004, Laccases: structure, reactions, distribution, Micron 35 93-96. https://doi.org/10.1016/j.micron.2003.10.029
  5. D'Souza-Ticlo, D.T., 2008, The lignin-degrading enzyme, laccase from marine fungi; biochemical and molecular approaches, Ph.D. Disseration, Goa University, India.
  6. Dwivedi, U.N., Singh, P., Pandey, V.P., Kumar, A., 2011, Structure-function relationship among bacterial, fungal and plant laccases., J Mol Catalysis B: Enzymatic 68 117-128. https://doi.org/10.1016/j.molcatb.2010.11.002
  7. Guan, Z.B., Zhang, N., Song, C,M,, Zhou, W., Zhou, L.X., Zhao, H., Xu, C.W., Cai, Y.J., Liao, X.R., 2014, Molecular cloning, characterization, and dye-decolorizing ability of a temperature- and pH-stable laccase from Bacillus subtilis X1., Appl Biochem Biotechnol 172 1147-1157. https://doi.org/10.1007/s12010-013-0614-3
  8. Imran M, Asad MJ, Hadri SH, Mehmood S., 2012, Production and industrial applications of laccase enzyme. J Cell Mol Biol. 10 1-11.
  9. Jeong,H., Sim,Y.M. and Kim,S.-K., Draft genome sequence of Bacillus sonorensis 13918T. (Unpublished data). Bacillus sonorensis NBRC 101234 = KCTC 13918 contig66, whole genome shotgun sequence NCBI Reference Sequence: NZ_AYTN01000063.1 (Unpublished data).
  10. Koschorreck, K., Richter, S.M., Ene, A.B., Roduner, E., Schmid, R.D., Urlacher, V.B., 2008, Cloning and characterization of a new laccase from Bacillus licheniformis catalyzing dimerization of phenolic acids. Appl Microbiol Biotechnol 79 217-224. https://doi.org/10.1007/s00253-008-1417-2
  11. Kudanga, T., Nyanhongo, G.S., Guebitz, G.M., Burton, S., 2011, Potential applications of laccase-mediated coupling and grafting reactions: A review. Enzyme Microbial Technol 48 195-208. https://doi.org/10.1016/j.enzmictec.2010.11.007
  12. Palmisano, M., Nakamura, L.K., Duncan, K.E., Istock, C.A., Cohan, F.M., 2001, Bacillus sonorensis sp. nov., a close relative of Bacillus licheniformis, isolated from soil in the Sonoran Desert, Arizona. Int. J. Sys Evol. Microbiol. 51 1671-1679. https://doi.org/10.1099/00207713-51-5-1671
  13. Piscitelli, A., Pezzella, C., Giardina, P., 2010, Heterologous laccase production and its role in industrial applications. Bioengineered Bugs 1 252-262.
  14. Reiss, R., Ihssen, J., Thony-Meyer, L., 2011, Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC Biotech 11 177-183.
  15. Riva, S., 2006, Laccases: blue enzymes for green chemistry Trends in Biotech. 24 219-226. https://doi.org/10.1016/j.tibtech.2006.03.006
  16. Rodrguez Couto, S., Toca Herrera, J.L., 2006, Industrial and biotechnological applications of laccases: A review. Biotechnol Adv. 24 500-513. https://doi.org/10.1016/j.biotechadv.2006.04.003
  17. Ruijssenaars, H.J., Hartmans, S., 2004, A cloned Bacillus halodurans multicopper oxidase exhibiting alkaline laccase activity Appl Microbiol Biotechnol 65 177-182.
  18. Yang, S.S., Liu, Z.W., Yi, X.P., Zhang, A.L., Zhang, T.Y., Luo, J.X., Zhang, Z.H., Shen, J.C., Yin, H.X., Chen, L.P., 2012, Isolation of laccase gene from Bacillus subtilis and analysis of its physicochemical properties. Gene 491 49-52. https://doi.org/10.1016/j.gene.2011.09.006
  19. Zhang, C,, Zhang, S., Diao, H., Zhao, H., Zhu, X., Lu, F., Lu, Z., 2013, Purification and characterization of a temperature- and pH-stable laccase from the spores of Bacillus vallismortis fmb-103 and its application in the degradation of Malachite Green. J. Appl. Food. Chem 61 5468-5473.