Preliminary Gene Characterization of α-Amylase from Bacillus amyloliquefaciens UMAS 1002

  • Muhammad Suhaib Mat Hussin
  • Mohd Hasnain Hussain
  • Awang Ahmad Sallehin Awang Husaini
  • Koplo Bujang
  • Dayang Salwani Awg Adeni
  • Mohd Azib Salleh
Keywords: Bacillus amyliquefaciens, starch degrading, amylase, in silico, sago waste

Abstract

Characterization of α-amylase gene sequence produced by Bacillus amyloliquefaciens UMAS 1002, a
cellulolytic and amylolytic bacilli isolated from sago pith waste is described here. The amyE gene encoding the
α-amylase was isolated by polymerase chain reaction. The 1,980 bp of amyE gene corresponding to 660 amino
acids showed 99% homology to the α-amylase sequence from Bacillus subtilis X-23 (GenBank: BAA31528).
The α-amylase sequence of B. amyloliquefaciens UMAS 1002 (GenBank: KC800929) differs from that of B.
subtilis X-23 by 5 amino acids. In silico analysis of α-amylase from B. amyloliquefaciens UMAS 1002 showed
similar characteristics compared to α-amylase from B. subtilis X-23.

References

Apun, K., Jong, B.C., & Salleh, M.A. (2000). Screening and isolation of a cellulolytic and amylolytic Bacillus from sago pit waste. Journal of General and Applied Microbiology, 46: 263-267.

https://doi.org/10.2323/jgam.46.263

Chen, X.H., Koumoutsi, A., Scholz, R., Schneider, K., Vater, J., Süssmuth, R., Piel, J., & Borriss, R. (2009). Genome analysis of Bacillus amyloliquefaciens FZB42 reveals its potential for biocontrol of plant pathogens. Journal of Biotechnology, 140: 27-37.

https://doi.org/10.1016/j.jbiotec.2008.10.011

Demirkan, E.S., Mikami, B., Adachi, M., Higasa, T., & Utsumi, S. (2005). α-Amylase from B. amyloliquefaciens: purification, characterization, raw starch degradation and expression in E. coli. Process Biochemistry, 40(8): 2629-2636.

https://doi.org/10.1016/j.procbio.2004.08.015

Gangadharan, D., Nampoothiri, K.M., Sivaramakrishnan, S., & Pandey, A. (2009). Biochemical characterization of raw-starchdigesting alpha amylase purified from Bacillus amyloliquefaciens. Applied Biochemistry and Biotechnology, 158(3): 653-662.

https://doi.org/10.1007/s12010-008-8347-4

Matsuzaki, H., Yamane, K., Yamaguchi, K., Nagata, Y., & Maruo, B. (1974). Hybrid α-amylases produced by transformants of Bacillus subtilis. I. Purification and characterization of extracellular α-amylases produced by the parental strains and transformants. Biochimica et Biophysica Acta (BBA) - Protein Structure, 365: 235-247.

https://doi.org/10.1016/0005-2795(74)90268-2

Ohdan, K., Kuriki, T., Kaneko, H., Shimada, J., Takada, T., Fujimoto, Z., Mizuno, H., & Okada, S. (1999). Characteristics of two forms of alpha-amylases and structural implication. Applied and Environmental Microbiology, 65: 4652-4658.

https://doi.org/10.1128/AEM.65.10.4652-4658.1999

Panda, S. & Chandra, G. (2012). Physicochemical characterization and functional analysis of some snake venom toxin proteins and related non-toxin proteins of other chordates. Bioinformation, 8(18): 891.

https://doi.org/10.6026/97320630008891

Pandey, A., Nigam, P., Soccol, C.R., Soccol, V.T., Singh, D., & Mohan, R. (2000). Advances in microbial amylases. Biotechnology and Applied Biochemistry, 31: 135-152.

https://doi.org/10.1042/BA19990073

Priest, F.G. (1977). Extracellular enzyme synthesis in the genus Bacillus. Bacteriological Reviews, 41: 711-753.

https://doi.org/10.1128/MMBR.41.3.711-753.1977

Sambrook, J., Fritsch, E.F., & Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. 3rd Edition. J. Argentine (Ed). New York: Cold Spring Harbor Press.

Singh, S., Moholkar, V.S., & Goyal, A. (2013). Isolation, identification, and characterization of a cellulolytic Bacillus amyloliquefaciens strain SS35 from rhinoceros dung. ISRN Microbiology, 2013: Article ID 728134.

https://doi.org/10.1155/2013/728134

Svensson, B. & Søgaard, M. (1992). Protein engineering of amylases. Biochemical Society Transactions, 20(1): 34-42.

https://doi.org/10.1042/bst0200034

van der Maarel, M.J.E.C., Van-der-Veen, B., Uitdehaag, J.C.M., Leemhuis, H., & Dijkhuizen, L. (2002). Properties and application of starch converting enzymes of the α-amylases family. Journal of Biotechnology, 94: 137-155.

https://doi.org/10.1016/S0168-1656(01)00407-2

Welker, N.E. & Campbell, L.L. (1967). Unrelatedness of Bacillus amyloliquefaciens and Bacillus subtilis. Journal of Bacteriology, 94: 1124-1130.

https://doi.org/10.1128/jb.94.4.1124-1130.1967

How to Cite
Mat Hussin, M. S., Hussain, M. H., Sallehin Awang Husaini, A. A., Bujang, K., Awg Adeni, D. S., & Salleh, M. A. (1). Preliminary Gene Characterization of α-Amylase from Bacillus amyloliquefaciens UMAS 1002. Borneo Journal of Resource Science and Technology, 3(2), 36-39. https://doi.org/10.33736/bjrst.248.2013
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General