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고호염성 Haloarcular sp. EH-1으로 부터 amylase 생산

Amylase Production from Haloarcular sp. EH-1

  • 정명주 (경성대학교 교양과정부)
  • 발행 : 2002.10.01

초록

천일염에서 분리된 고호염성균인 Hainrcular sp. EH-1 으로부터 amylase 생성을 위한 배양조건을 검토하여 최적조건을 설정하였다. 그 결과는 다음과 같다. 아밀라아제 생산을 위한 배양 조건은 4$0^{\circ}C$, pH 7.5이었으며, 최적 생육배지를 soluble starch 1.5%, yeast extract 1.0%, MgSO$_4$7$H_2O$ 2.0%, KCI 0.1%, NaCl 25%로 조성하여 500 $m\ell$ 삼각 플라스크에 100 $m\ell$ 씩 분주하여 110 rpm/min으로 진탕 배양시켰다. 생육과 효소활성은 9일 배양 후 최대치를 나타내어서, 균의 생육정도와 효소생산 사이에서 증식연관형을 나타내었다.

The extremely halophilic archaebacterium Haloarcular sp. EH-1 was isolated from solar salts. Amylae production from Halonrcular sp. EH-1 have been studied. The results obtained were as follows. The optimal medium composition for the production of amylase from Haloarcular sp. EH-1 were soluble starch 1.5%, yeast extract 1.0%, MgSO$_4$ 7h$_2$O 2.0%, KCI 0.1%, NaCl 25% (pH 7.5). The incubation temperature, aeration rate and agitation speed were 4$0^{\circ}C$, 100 $m\ell$ medium / 500 $m\ell$ shaking flask, and 110 rpm. The cell growth and enzymatic activity was highest at 9 days of incubation. So amylase production appeared to be a growth-related phenomenon.

키워드

참고문헌

  1. Appl. Microbiol. v.2 The reddening of salted hides and fish Anderson, H.
  2. Can. J. Microbiol. v.1 The effect of magnesium, potassium and iron on the growth and morphology of red halophilic bacteria Brown, H.J.;N.E. Gibbons https://doi.org/10.1139/m55-062
  3. Food Technol. v.45 Enzymes: Catalyst for food process Dziezak, J.D.
  4. Practical methods in electro microscopy v.3 Glauert, A.M.
  5. J. Microbiol. v.104 Properties of the amylase from Halobacterium halobium Good, W.A.;P.A. Hartman
  6. Bergey's manual of systematic bacteriology v.3 Extremely halophilic archaebacteria. Order Halobacteriales ord. nov. Grant, W.D.;H. Larsen;N. Pfennig (ed.)
  7. Letters Appl. Microbiol. v.9 Archaebacteria: ancient organisms with commercial potential Hough, D.W.;M.J. Danson https://doi.org/10.1111/j.1472-765X.1989.tb00285.x
  8. FEMS Microbiol. Reviews. v.39 Production and function of enzymes of eubacterial halophiles Kamekura, M. https://doi.org/10.1111/j.1574-6968.1986.tb01855.x
  9. Letters Appl. Microbiol. v.19 Production of moderately halophilic amylase by newly isolated Micrococcus sp. 4 from a salt-pan Khire, J.M. https://doi.org/10.1111/j.1472-765X.1994.tb00945.x
  10. World J. Microbiol. v.8 Thermostable, salttolerant amylase from Bacillus sp. 64 Khire, J.M.;A. Pant https://doi.org/10.1007/BF01195840
  11. Handbook of amylases and related enzymes Application of amylases and related enzymes to industry Komaki, T.;The amylase research society of Japan (ed.)
  12. The bacteria v.8 The Halobacteriaceae Kushner, D.J.;Woese, C.R.(ed.);R.S. Wolf(ed.)
  13. Advances in microbial physiology v.1 Biochemical aspects of extreme halophilism Larsen, H.
  14. Can. J. Res. v.10 Bacteriological studies on the red discoloration of salted hides Lochhead, A.G. https://doi.org/10.1139/cjr34-026
  15. J. Biol. Chem. v.193 Protein measurement with the folin phenol reagent Lowry, O.H.;N.J. Rosebrough;F.A. Lewis;R.J.Randall
  16. J. Gen. Microbiol. v.55 Proteolytic enzymes from extremely halophilic bacteria Norberg, P.;B.V. Hofsten https://doi.org/10.1099/00221287-55-2-251
  17. J. Bacteriol. v.109 Halophilic amylase from a moderately halophilic micrococcus Onishi, H.
  18. Kor. J. Microbiol. Biotechnol. v.24 Isolation and Identification of an Extremely Halophilic Bacterium from Solar Salts Park, H.S.;M.J. Jeong
  19. World J. Microbiol. Biotechnol. v.9 Production of α-amylase from Halobacterium halobium Patel, S.;N. Jain;D. Madamwar https://doi.org/10.1007/BF00656510
  20. Aspects of Microbiology v.9 Extracellular enzymes Priest, F.G.;Cole, J.A.(ed.);C.J. Knowles(ed.);D. Schlessinger(ed.)
  21. Can. J. Microbiol. v.6 Effect of some metal ions growth of Halobaterium cutirubrum Sehgal, S.N.;N.E. Gibbons https://doi.org/10.1139/m60-018
  22. Can. J. Microbiol. v.18 Studies on acid production during carbohydrate metabolism by extremely halophilic bacteria Tomlinson, G.A.;L.I. Hochstein https://doi.org/10.1139/m72-308