• 검색어에 아래의 연산자를 사용하시면 더 정확한 검색결과를 얻을 수 있습니다.
  • 검색연산자
검색연산자 기능 검색시 예
() 우선순위가 가장 높은 연산자 예1) (나노 (기계 | machine))
공백 두 개의 검색어(식)을 모두 포함하고 있는 문서 검색 예1) (나노 기계)
예2) 나노 장영실
| 두 개의 검색어(식) 중 하나 이상 포함하고 있는 문서 검색 예1) (줄기세포 | 면역)
예2) 줄기세포 | 장영실
! NOT 이후에 있는 검색어가 포함된 문서는 제외 예1) (황금 !백금)
예2) !image
* 검색어의 *란에 0개 이상의 임의의 문자가 포함된 문서 검색 예) semi*
"" 따옴표 내의 구문과 완전히 일치하는 문서만 검색 예) "Transform and Quantization"
쳇봇 이모티콘
ScienceON 챗봇입니다.
궁금한 것은 저에게 물어봐주세요.

논문 상세정보

Characterization of Two Forms of Glucoamylase from Traditional Korean Nuruk Fungi, Aspergillus coreanus NR 15-1


Some characteristics of two forms of glucoamylase (glucan 1 A-$\alpha$-glucosidase, EC 3. 2. I. 3) purified from Aspergillus coreanus NR 15-1 were investigated. The enzymes were produced on a solid, uncooked wheat bran medium of A. coreanus NR 15-1 isolated from traditional Korean Nuruk. Two forms of glucoamylase, GA-I and GA-II, were purified to homogenity after 5.8-fold and 9.6-fold purification, respectively, judged by disc- and SDS-polyacrylamide gel electrophoresis. The molecular mass of GA-I and GA-II were estimated to be 62 kDa and 90 kDa by Sephadex G-1OO gel filtration, and 64 kDa and 91 kDa by SDS-polyacrylarnide gel electrophoresis, respectively. The optimum temperatures of GA-I and GA-II were 60$^circ$C and 65$^circ$C, respectively, and the optimum pH was 4.0. The activation energy (Ea value) of GA-I and GA-II was 11.66 kcal/mol and 12.09 kcal/mol, respectively, and the apparent Michaelis constants (K_{m}) of GA-I and GA-II for soluble starch were found to be 3.57 mg/ml and 6.25 mg/ml, respectively. Both enzymes were activated by 1 mM Mn^{2+} and Cu^{2+}, but were completely inhibited by 1 mM N­bromosuccinimide. The GA-II was weakly inhibited by 1 mM p-CMB, dithiothreitol, EDTA, and pyridoxal 5-phosphate, but GA-I was not inhibited by those compounds. Both enzymes had significant ability to digest raw wheat starch and raw rice starch, and hydrolysis rates of raw wheat starch by GA-I and GA-II were 7.8- and 7.3-fold higher than with soluble starch, respectively.

참고문헌 (31)

  1. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248- 254 
  2. Chung, M. J., W. N. Hou, J. H. Jeong, and H. Taniguchi. 1990. Studies on the development and the characteristics of the powerful raw starch digesting enzyme. Kor. J. Appl. Microbiol. Biotechnol. 18: 251- 259 
  3. Hansen, S. A. 1975. Thin-layer chromatographic method for identification of oligosacchatides in starch hydrolysates. J. Chromatogr. 105: 388- 390 
  4. Kim, H. S., J. S. Hyun, J. Kim, H. P. Ha, and T. S. Yu. 1998. Enzymological characteristics and identification of useful fungi isolated from traditional Korean Nuruk. Kor. J. Appl. Microbiol. Biotechnol. 26: 456- 464 
  5. Nakasaka, Y., K. Kurosawa, A. Yokota, and F. Tomita. 1998. Purification and properties of the raw-starch-digesting glucoamylases from Corticium rolfsii. Appl. Microbiol. Biotechnol. 50: 323- 330 
  6. Ono, K., S. Shigeta, and S. Oka. 1988. Effective purification of glucoamylase in koji, a solid culture of Aspergillus oryzae on steamed rice, by affinity chromatography using an immobilized acabose (Bay g-5421). Agric. Biol. Chem. 52: 1707- 1714 
  7. Song, M. H., K. Selvam, H.-Y. Jeong, and K.-S. Chae. 2003. Inhibition of asexual sporulation and growth of Aspergillus niger and Aspergillus oryzae by propylamine. J. Microbiol. Biotechnol. 13: 146- 148 
  8. Takahashi, T., N. Inokuchi, and M. Irie. 1981. Purification and characterization of a glucoamylase from Aspergillus saitoi. J. Biochem. 89: 125- 134 
  9. Yasuda, M., M. Kuwae, and H. Matsushita. 1989. Purification and properties of two forms of glucoamylase from Monasocus sp. No. 3403. Agric. Biol. Chem. 53: 247- 249 
  10. Taniguch, H., F. Odashima, M. Igarashi, Y. Maruyama, and M. Nakamura. 1982. Characterization of a potato starchdigesting bacterium and its production of amylase. Agric. Biol. Chem. 46: 2107- 2115 
  11. Ji, J.-H, J.-S. Yang, and J.-W. Hur. 2003. Purification and characterization of the exo-B- D-glucosaminase from Aspergillus flavus IAM2044. J. Microbiol. Biotechnol. 13: 269- 275 
  12. Yamasaki, Y., Y. Suzuki, and J. Ozawa. 1977. Purification and properties of two forms of glucoamylase from Penicillium oxalicum. Agric. Biol. Chem. 41: 755- 762 
  13. Yu, T. S., S. H. Yeo, and H. S. Kim. 2004. A new species of Hyphomycetes, Aspergillus coreanus sp. nov., isolated from traditional Korean Nuruk. J. Microbiol. Biotechnol. 14: 182-187 
  14. Hayashida, S., S. Kunisaki, M. Nakao, and P. Q. Flor. 1982. Evidence for raw starch-affinity site on Aspergillus awamori glucoarnylase I. Agric. Biol. Chem. 46: 83- 89 
  15. Razzaque, A. and S. Ueda. 1978. Glucoamylase of Aspergillus oryzae. J. Ferment. Technol. 56: 296- 302 
  16. Weber, K. and M. Osborn. 1969. The reliability of molecular weight determination by sodium dodecyl sulfate polyacrylamide gel electrophoresis. J. Biol. Chem. 244: 4406- 4412 
  17. Yamasaki, Y., Y. Suzuki, and J. Ozawa. 1977. Properties of two forms of glucoamylase from Penicillium oxalicum. Agric. Biol. Chem. 41: 1443- 1449 
  18. Takahashi, T., Y. Tsuchida, and M. Irie. 1978. Purification and some properties of three forms of glucoamylase from a Rhizopus species. J. Biochem. 84: 1183-1194 
  19. Kim, C. J., M. J. Oh, and J. S. Lee. 1986. Purification characterization of raw starch digesting enzyme from Rhizopus oryzae. Korean J. Food Sci. Technol. 18: 288-293 
  20. Yu, T. S., T. H. Kim. and C. Y Joo. 1999. Purification and characteristics of glucoamylase in Aspergillus oryzae NR 36 isolated traditional Korean Nuruk. J. Microbiol. 37: 80-85 
  21. Segel, I. H. 1975. Biochemical Calculations (2nd Ed.), New York, John Wiley and Sons, p. 203 
  22. Chung, M. J. 1997. Purification and characteristics of raw starch hydrolyzing enzyme from Aspergillus niger. Kor. J. Appl. Microbiol. Biotechnol. 25: 166- 172 
  23. Davis, B. J. 1964. Disc electrophoresis II. Method and application to human serum protein. Ann. New York Acad. Sci. 121: 404-427 
  24. Sohn, C. B. 1983. Studies on the raw starch saccharifying enzyme from Aspergillus niger and its mutant. The graduate school of Chungnam National University. Thesis for the degree of Doctor 
  25. Kim, C. J., M. J. Oh, and J. S. Lee. 1985. Studies on digestion of raw starch by Rhizopus oryzae. Kor. J. Appl. Microbiol. Bioeng. 13: 329- 337 
  26. Yamasaki, Y., A. Tsuboi, and Y. Suzuki. 1977. Two forms of glucoamylase from Mucor rouxianus. Agric. Biol. Chem. 41: 2139-2148 
  27. The Brewing Society of Japan. 1993. The Annotation of the Official Method of Analysis of the National Tax Administration Agency. 4th Ed., Tokyo: 218- 226 
  28. Andrews, P. 1964. Estimation of the molecular weights of proteins by Sephadex gel filtration. J. Biochem. 91: 222- 233 
  29. Allain, C. C., L. S. Poon, C. S. G. Chan, W. Richmond, and P. C. Fu. 1974. Enzymatic determination of total serum cholesterol. Clin. Chem. 20: 470-475 
  30. Witkop, B. 1961. Nonenzymatic methods for the preferential and selective cleavage and modification of protein, pp. 221-321. In C. B. Anfinsen, Jr., M. L. Anson, K. Bailey. and J. T. Edsall (eds.), Advances in Protein Chemistry, Vol. 16. Academic Press Inc., New York, U.S.A 
  31. Yu, T. S., H. S. Kim, J. J. Hong, J. P. Ha, T. Y Kim, and I. W. Yoon. 1996. Bibliographical study on microorganisms of Nuruk (until 1945). J. Korean Soc. Food. Nutri. 25: 170-179 

이 논문을 인용한 문헌 (3)

  1. Lee, Jung-Hoon ; Park, Sung-Min ; Park, Chi-Duck ; Jung, Hyuck-Jun ; Kim, Hyun-Soo ; Yu, Tae-Shick 2007. "Characteristics of Ju-Back and Effect of Ju-Back Fertilizer on Growth of Crop Plants" 생명과학회지 = Journal of life science, 17(11): 1562~1570 
  2. 2008. "" Food science and biotechnology, 17(6): 1160~1164 
  3. 2008. "" Journal of microbiology and biotechnology, 18(3): 545~551 


원문 PDF 다운로드

  • ScienceON :
  • KCI :

원문 URL 링크

원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다. (원문복사서비스 안내 바로 가기)

상세조회 0건 원문조회 0건

DOI 인용 스타일