Korean Journal of Microbiology (미생물학회지)

The Microbiological Society of Korea (한국미생물학회)
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Isolation and Characterization of $\alpha$-Amylase Producing Bacillus sp. AIV 1940 and Properties of Starch Synthetic Wastewater Degradation

$\alpha$-Amylase 생성균주 Bacillus sp. AIV 1940의 분리, 특성 및 합성폐수분해능

  • 박형수 (삼성엔지니어링 기술연구소) ;
  • 김무훈 (삼성엔지니어링 기술연구소) ;
  • 양선영 (삼성엔지니어링 기술연구소) ;
  • 조미영 (삼성엔지니어링 기술연구소) ;
  • 고범준 (삼성엔지니어링 기술연구소) ;
  • 박용근 (고려대학교 생명공학원)
  • Published : 2002.03.01
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Abstract

$\alpha$-Amylase producing bacteria were isolated from activated sludge of corn processing wastewater plant and paddy field soil samples and selected by the direct iodine reaction. The isolate was identified as Bacillus sp. after morphology, API system and fatty acid analyses. To enchance $\alpha$-amylase productivity, a successive mutation of Bacillus sp. AIV 19 was performed using the treatment of nitrosoguanidine(NTG).The mutant, Bacillus sp. AIV 1940, showed about 1.8-fold level of amylase activity compared with parental strain. The isolate was Gram-positive and rod (2.8-3.0 $\mu$m long, 0.5-0.6 $\mu$m wide) type. The strain increased the bacterial mass at 3000 mg/l starch concentration. Organic substance removal rate was 40.2, 72.3% respectively after 1 and 3 day reaction using starch synthetic wastewater (intial CODcr was 4,455 mg/l).

전분가공폐수처리장 활성슬러지와 논, 밭 토양에서 전분성분을 분해하는 $\alpha$-amylase를 생성하는 균주들을 분리 선별하였다. 이중 효소활성이 우수한 AIV 19를 형태학적 분석 및 API system 과 지방산분석(MIDI) 방법을 이용한 결과 Bacillus 속으로동정되었다. $\alpha$-amylase 생성능을 향상시키기 위해 nitrosoguanidine (NTG)처리를 한 균주 중 선별된 AIV 1940균주의 효소활성능이 원 균주에 비해 1.8배 향상되었다. 분리균주는 그람양성가균으로 길이가 2.3-5 $\mu$ m폭이 0.8-1$\mu$m이었고, Bioscreen C 시스템을 이용한 균주성장능 평가에서는 전분이 3 g/ι농도에서 성장능이 증가되었다. 전분합성폐수를 이용한 유기물제거실험에서는 초기 CODcr가 4,455 mg/ι인 고농도 합성폐수를 1일 3일 반응 후 각각 40.2% 72.3%의 유기물 제거율을 나타내었다.

Keywords

References

  1. J. Bacteriol. v.85 Classification of microorganism by analysis of chemical composition. 1. Feasibility of utilizing gas chromatography Abel, K.;H. de Schmertzing;J.I. Peterson
  2. Appl. Environ. Microbiol. v.57 Isolation and characterization of Clostridium acetobutylicum mutants with enhanced amylolytic activity Annous, B.;H. Blaschek
  3. Amylase, α and β, Method in Enzymology v.1 Bernfeld, P. https://doi.org/10.1016/0076-6879(55)01021-5
  4. Mannual of methods for general Bacteriology Gerhardt, P.;RG.E. Murrary;R.N. Costilow;W.A. Wood;N.R. Krieg;E.W. Nester;G.B. Philips
  5. Kor. J. Appl. Microbiol. Biotechnol. v.19 Isolation of thermostable α-amylase hyperproducing Bacillus sp. No. 32H417 and some properties of the enzyme Kim, M.S.;P.S. O.
  6. Appl. Microbiol. Biotechnol. v.51 Reversal of the inhibitory effect of surfactants upon germination and growth of a consortium of two strains of Bacillus Ledent, P.;H. Michels;G. Blackman;H. Naveau;S.N. Agathos https://doi.org/10.1007/s002530051404
  7. Experiments in molecular genetics Miller, J.M.
  8. Hewlett-Pacard Application. Note 228-248 Bacteria identification by gas chromatography of whole cell fatty acid Miller, L.;T. Berger
  9. Biochem. J. v.230 Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulricum Melasniemi, H.
  10. Bergey's Manual of Systematic Bacteriology(2nd ed.) Peter, H.;A. Sneath
  11. Bacteriol. Rev. v.41 Extracellular enzyme synthesis in the Bacillus genus Priest, F.G.
  12. Arch. Biochem. Biophy. v.155 Structure and function of amylase. Ⅱ. Multiple forms of Bacillus subtilis α-amylase Robyt, J.F.;R.J. Ackerman https://doi.org/10.1016/0003-9861(73)90135-5
  13. J. Appl. Bacteriol. v.73 Another explanation for the toxicity of fermentation acids at low pH; anion accumulation vs uncoupling Russel, J.B. https://doi.org/10.1111/j.1365-2672.1992.tb04990.x
  14. Agric. Biol. Chem. v.40 Purification and enzymatic properties of β-amylase and pullulanse from Bacillus cereus Takasaki, Y. https://doi.org/10.1271/bbb1961.40.1523
  15. Crit. Rev. Biochem. Mol. Biol. v.24 Microbial amylolytic enzymes Vihinen, M.;P. Mantsala https://doi.org/10.3109/10409238909082556
  16. J. Bacteriol. v.156 α-Amylase genes amyR2 and amyE from and α-amylase hyperproducing Bacillus subtilis strain: Molecular cloning and nucleotide sequence Yamazaki, H.;K. Ohmura;A. Nakayama
  17. Biotech. Bioeng. v.31 Fed-Batch Fermentation for the Production of α-Amylase by Bacillus Amyloliquefaciens Yoo, Y.H. https://doi.org/10.1002/bit.260310506