Biosynthetic Regulation of Invertase from Thermophilic and Alkalophilic Bacillus sp. TA-11

고온성이며 호알칼리성인 Bacillus sp. TA-11이 생성하는 Invertase의 생합성 조절

  • Kim, Jae-Ho (Dept. of Genetic Engineering, Paichai University) ;
  • Kim, Na-Mi (Division of Product Development, Korea Tabacco & Ginseng Company Central Institute) ;
  • Kim, Dong-Woo (Division of Food Science and Technology, Woosong Technical College)
  • Published : 2002.06.01

Abstract

Regulation of invertase biosynthesis was studied in thermophilic and alkalophilic Bacillus sp. TA-11. Biosynthesis of the invertase was effectively induced in the presence of 10 mM sucrose for 180 min. Glucose repressed the invertase induction by sucrose and as late as addition time of glucose, the invertase formation was increased, indicating that glucose repression was occurred by inducer exclusion. Catabolite repression was reduced a little by the addition of cAMP for 180 min of induction.

고온성이며 호알칼리성인 Bacillus sp. TA-11이 생성하는 Invertase의 생합성 조절 기작을 규명하고자 먼저 이들의 유도와 억제에 관하여 검토하였다. Invertase는 10mM sucrose을 함유한 생합성 조절배지에서 3시간에 효율적으로 유도되었고 glucose는 sucrose에 의한 invertase 유도를 inducer exclusion 방식으로 억제시켰다. CAMP의 첨가로 glucose에 의한 catabolic repression이 다소 줄어들었다.

Keywords

References

  1. Mybrack, K. : Invertase. The enzyme, P. D. Boyer. H. Lardy, and K. Mybrack (ed.), Academic Press. Inc., New York., Vol. 4, p. 379-396(1960)
  2. Straathof, A., Kieboom, A. P. G. and Bekkum, H. : Invertase catalyzed fructosyl transfer in concentrated solutions of sucrose, Carbohydr, Res., 146, 154-159(1986) https://doi.org/10.1016/0008-6215(86)85033-9
  3. Fitzgerald, R. J., Spinell, D. M. and Stoudt, T. H. : Enzymatic removal of artificial plague, Arch. Oral. Biol., 13, 125-128(1968) https://doi.org/10.1016/0003-9969(68)90042-3
  4. Obenland, D., Simmen, U., Boller, T. and Wiemken, A. : Purification and characterization of three soluble invertase from barley leaves, Plant Physiol., 101, 1331-1339(1993) https://doi.org/10.1104/pp.101.4.1331
  5. Pressey, R. : Separation and properties of potato invertase and invertase inhibitor, Arch. Biochem. Biophys., 113, 667-674(1966) https://doi.org/10.1016/0003-9861(66)90246-3
  6. Porntaveewat, W., Takayanagi, T. and Yokotsuka, K. : Purification and properties of invertase from Muscat Baliey A grapes, J. Ferment. Bioeng., 78, 288-292(1994) https://doi.org/10.1016/0922-338X(94)90359-X
  7. Nakagawa, H., Kawasaki, Y., Ogura, N. and Takehata, H. : Purification and properties two types of $\beta$-fructofuranosidase from tomato fruit, Agric. Biol. Chem., 36, 18-26(1971)
  8. Krishnan, H. B., Blanchette, J. T. and Okita, T.W. : Wheat invertase, Plant Physiol., 78, 241-245(1985) https://doi.org/10.1104/pp.78.2.241
  9. Unger, C., Hofsteenge, J. and Sturm, A, : Purification and characterization of a soluble $\beta$-fructofuranosidase from Daucus carota, Eur. J. Biochem., 204, 915-921(1992) https://doi.org/10.1111/j.1432-1033.1992.tb16712.x
  10. Kim, B. M. : Studies on invertase from Korean ginseng, Panax ginseng C. A. Meyer. Korean J. Food. Sci. Technol., 12, 1-5(1980)
  11. Park, J. B. and Choi, Y. J. : Purification and characterization of inulin fructotransferase from Arthrobacter sp. A-6, Korean J. Microbiol. Biotech., 6, 402-406(1996)
  12. Tanzer, J. M., Brown, A. T. and Mclnerney, M. F. : Identification, preliminary characterization, and evidence for regulation of invertase in Streptococcus mutans, J. Bacteriol., 116, 192-202(1973)
  13. Hirayama, M., Sumi, N. and Hidaka, H. : Purification and propeties of a fructooligosaccharides-producing $\beta$-fructofuranosidase from Aspergillus niger ATCC 20611, Agric. Biol. Chem., 53, 667-673(1989) https://doi.org/10.1271/bbb1961.53.667
  14. Yanase, H., Fukushi, H., Ueda, N., Maeda, Y., Toyoda, A. and Tonomura, K. : Cloning, sequencing and characterization of the intracellular invertase gene from Zymomonas mobilis, Agric. Biol. Chem., 55, 1383-1390(1991) https://doi.org/10.1271/bbb1961.55.1383
  15. Fujita, K., Hara, K., Hashimoto, H., and Kitahata, S. : Purification and some properties of $\beta$-fructofuranosidase I from Arhrobacter sp. K-1, Agric. Biol. Chem., 54, 913-919(1990) https://doi.org/10.1271/bbb1961.54.913
  16. Dodyk, F. and Rothstein, A. : Factors influencing the appearance of invertase in Saccharomyces cerevisiae, Arch. Biochem. Biophys., 104, 478-475(1964) https://doi.org/10.1016/0003-9861(64)90492-8
  17. Neumann, N. and Lampen, J. O. : Purification and properties of yeast invertase, Biochem, 6, 468-475(1967) https://doi.org/10.1021/bi00854a015
  18. Kidby, D. K. and Davies, R. : Inverase and disulphide bridge in the yeast wall, J. General Microbiol., 61, 327-333(1970) https://doi.org/10.1099/00221287-61-3-327
  19. Ottolenghi, P. : A comparison of five genetically distinct invertase from Saccharomyces, Eur. J. Biochem., 18, 554-552(1971)
  20. Amold, W. N. : Location of acid phosphatase and $\beta$-fructofuranosidase within yeast cell envelopes, J. Bacteriol., 112, 1346-1352(1972)
  21. Babczinski, P. : Partial purification, characterization and localization of the membrane-associated invertase of yeast, Biochim. Biophys. Acta., 614, 121-133(1980) https://doi.org/10.1016/0005-2744(80)90173-4
  22. Montenecourt, B. S., Kuo, S. C. and Lampen, J. O. : Saccharomyces mutans with invertase formation resistant to repression by hexoses, J. Bacteriol., 114, 233-238(1973)
  23. Abrams, B. B., Hckel, R., Mizunaga, T. and Lampen, J. O. : Relationship of large and small invertase in Saccharomyces mutant selectively deficient in small invertase, J. Bacteriol., 135, 809-817(1994)
  24. Choi, Y. J. and Lee, J. S. : Production of $\beta$-fructofuranosidase from alkalophilic, thermophilic Bacillus sp. TA-11, Korean J. Appl. Microbiol. Biotechnol., 23, 197-202(1995)
  25. Martin, I., Debarbouille, M., Ferrari, E., Klier, A. and Rapoport, G. : Characterization of the levanase gene of Bacillus subtilis which shows homology to yeast invertase, Mol. Gen Genet., 208(1-2), 177-184(1987) https://doi.org/10.1007/BF00330439
  26. Fouet, A., Klier, A. and Rapoport, G. : Nucleotide sequence of the sucrase gene of Bacillus subtilis, Gene., 45(2), 221-225(1986) https://doi.org/10.1016/0378-1119(86)90258-1