꽃송이버섯(Sparassis crispa)의 세포외 효소활성

The Extracellular Enzyme Activities in Culture Broth of Sparassis crispa.

  • 김지영 (동국대학교 대학원 생물학과) ;
  • 임창수 (동국대학교 대학원 생물학과) ;
  • 김재용 (동국대학교 대학원 생물학과) ;
  • 한영환 (동국대학교 대학원 생물학과)
  • 발행 : 2004.09.01

초록

꽃송이버섯(Sparassis crispa DSMZ 5201)의 균사를 사용하여 균사외 효소활성을 측정하였다. Yeast-malt extract-glucose 배지를 사용하여 $24^{\circ}C$에서 15일간 배양 후 배양여액을 조효소원으로 사용하였을 때, $\alpha$-amylase효소의 활성은 44.27 unit/$mg{\cdot}protein$이었다. 배양여액 중의 Protease, CMCase, $\beta$-glucosidase, chitinase 및 exo-$\beta$-1,4-glucanase의 세포외 효소활성은 상대적으로 높았으나, xylanase 효소활성은 낮게 나타났다.

The mycelia of Sparassis crispa DSMZ 5201 were cultivated at $24^{\circ}C$ for 15 days in yeast-malt extract-glucose broth (pH 4.0) and the filtrate was used as crude enzyme solution to determined the extracellular enzyme activity. The specific activity of $\alpha$-amylase was 44.27 unit/protein. The specific activities of protease, CMCase, $\beta$-glucosidase, chitinase, exo-$\beta$-l,4-glucanase were relatively high. However, a very little activity of xylanase was found.

키워드

참고문헌

  1. Bradford, M.M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
  2. Brown, V. and G. Schmitz. 1980. Excretion of protease of Serratia marcescens. Arch. Microbiol. 124, 55-61
  3. Do, J.H. and S.D. Kim. 1985. Properties of amylase produced from higher fungi Ganoderma lucidum. Kor. J. Appl. Microbiol. Bioeng. 13, 173-178
  4. Hsu, S.C. and L. Lockwood. 1975. Powdered chitin agar as a selective medium for enumeration of actinomycetes on water soil. Appl. Microbiol. 29, 422-426
  5. Jeong E.U. and Y.H. Lee. 1995. Isolation of microorganism producing chitinase for chitooligosaccharides production, purification of chitinase, and its enzymatic characteristics. Kor. J. Appl. Microbiol. Biotechnol. 23, 187-196
  6. Kanda, T., K. Wakabayashi, and K. Nisizawa. 1976. Purification and properties of and endocellulase of avicelase type from Irpex lacteus (Polyporus tuliferae). J. Ferment. Technol. 60, 381-383
  7. Kim, D.J., H.J. Shin., B.H. Min, and K.H. Yoon. 1995. Isolation of a thermophilic Bacillus sp. producing the therm stable cellulasefree xylanase, and properties of the enzyme. Kor. J. Appl. Microbiol. Biotechnol. 23, 304-310
  8. Lee, C.Y., O.P. Hong, M.J. Jung, and Y.H. Han. 1998. The extracellular enzyme activities in culture broth of Tricholoma matsutake. Kor. J. Mycol. 26, 496-501
  9. Lee. J.H., C.S. Jung, and J.S. Cho. 2001. Purification and characterization of protease from Sarcodon aspratus (Berk.) S. Ito. Kor. J. Food Cookery Sci. 17, 497-502
  10. Lee, S.S., J.K. Ha, and Y.J. Choi. 1996. Studies on the isolation and identification of rumen fungi, characterization of cellulolytic fungal enzymes, and its industrial utilization. Kor. J. Ankm. Nutr. Food 20, 51-63
  11. Lee, T.H. and Y.H. Han. 2001. Enzyme activities of the fruit body of Ramaria botryis DGUM 29001. Kor. J. Mycol. 29, 173-175
  12. Miller, G.L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31, 426-428
  13. Min, E.G. and Y.H. Han. 2000. Characteristics of extracellular $\beta$- glucosidase in Tricholoma matsutake. Kor. J. Biotech. Bioeng. 15, 9-13
  14. Min, E.G. and Y.H. Han. 2002. Optimal condition for mycelial growth of Beauveria bassiana and its extracellular enzyme activity. Kor. J. Microbiol. 38, 50-53
  15. Shim, J.O., S.G. Son, S.O. Yoon, and Y.S. Lee. 1998. The optimal factors for the mycelial growth of Sparassis crispa. Kor. J. Mycol. 26, 39-46
  16. Tokao, S., Y. Kamagata, and T. Sasaki. 1985. Cellulase production by Penicillum purpurogenum. J. Agri. Sci. Camb. 93, 217-222
  17. Uriyo, M. and W.E. Eigel. 1999. Duration of killing treatment on $\alpha$-amylase, $\beta$-amylase and endo-(1,3)(1,4)-$\beta$-D-glucanase activity of malted sorghum (Sofghum bicolor). Process Biochemistry 35. 31-37