DOI QR코드

DOI QR Code

Detection of Extracellular Enzyme Activities in Ganoderma neo-japonicum

  • Jo, Woo-Sik (Department of Agricultural Environment, Gyeongbuk Agricultural Technology Administration) ;
  • Park, Ha-Na (Department of Agricultural Environment, Gyeongbuk Agricultural Technology Administration) ;
  • Cho, Doo-Hyun (Department of Agricultural Environment, Gyeongbuk Agricultural Technology Administration) ;
  • Yoo, Young-Bok (Mushroom Research Division, Department of Herbal Crop Research, National Institute of Horicultural & Herbal Science, Rural Development Administration) ;
  • Park, Seung-Chun (College of Veterinary Medicine, Kyungpook National University)
  • 투고 : 2010.12.16
  • 심사 : 2011.05.13
  • 발행 : 2011.06.30

초록

The ability of Ganoderma to produce extracellular enzymes, including ${\beta}$-glucosidase, cellulase, avicelase, pectinase, xylanase, protease, amylase, and ligninase was tested in chromogenic media. ${\beta}$-glucosidase showed the highest activity, among the eight tested enzymes. In particular, Ganoderma neo-japonicum showed significantly stronger activity for ${\beta}$-glucosidase than that of the other enzymes. Two Ganoderma lucidum isolates showed moderate activity for avicelase; however, Ganoderma neojaponicum showed the strongest activity. Moderate ligninase activity was only observed in Ganoderma neo-japonicum. In contrast, pectinase, amylase, protease, and cellulase were not present in Ganoderma. The results show that the degree of activity of the tested enzymes varied depending on the Ganoderma species tested.

키워드

참고문헌

  1. Park WH, Kim TH, Ro IH. Studies on enzymes of the higher fungi of Korea (II): identification of cellulolytic enzyme in Lenzites betulina. Kor J Mycol 1986;14:225-9.
  2. Chang ST, Buswell JA. Mushroom nutriceuticals. World J Microb Biotechnol 1996;12:473-6. https://doi.org/10.1007/BF00419460
  3. Ying J, Mao X, Ma Q, Zong Y, Wen H. Icones of medicinal fungi from China. Beijing: Science Press; 1987.
  4. Abraham L, Hoffman B, Gao Y, Breuil C. Action of Ophiostoma piceae proteinase and lipase on wood nutrients. Can J Microbiol 1998;44:698-701. https://doi.org/10.1139/w98-046
  5. Shin DS, Lee HH, Lim KP, Cho NS, Cho BM. Chemistry of forest product. Seoul: Haeng Mun Sa; 1991. p. 121-2.
  6. Hong JS, Uhm TB, Jung GT, Lee KB. Studies on the enzymes produced by Pleurotus sojor-caju (1): the production of cellulolytic enzymes. Kor J Mycol 1984;12:59-64.
  7. Hashimoto K. Biochemical studies on the mushroom. Toyo Shokuhin Kenkyusho Kenkyu Hokokusho 1972;10:163.
  8. Ro IH. Studies on protease activity of Fomes fermentarius (Fr.) Kicky. Theses Collect Sookmyoung Univ Sci 1984;25: 475-85.
  9. Min TJ, Lee SY, Kim JW. Purification and properties of protease from the Pleurotus cornucopiae (Per.) Rolland (2). Korean Biochem J 1985;18:142-6.
  10. Lee JS, Suh DS. Production and enzymatic properties of laccase from Flammulina velutipes. Kor J Mycol 1985;13:111-4.
  11. Castro GR, Ferrero MA, Mendez BS, Sineriz F. Screening and selection of bacteria with high amylolytic activity. Acta Biotechnol 1993;13:197-201. https://doi.org/10.1002/abio.370130220
  12. Hejgaard J, Gibbons GC. Screening for $\alpha$-amylase in cereals: improved gel-diffusion assay using a dye-labelled starch substrate. Carlsberg Res Commun 1979;44:21-5. https://doi.org/10.1007/BF02910868
  13. Jo WS, Bae SH, Cho DH, Park SD, Yoo YB, Park SC. Optimal medium conditions for the detection of cellulolytic activity in Ganoderma lucidum. Mycobiology 2009;37:313-6. https://doi.org/10.4489/MYCO.2009.37.4.313

피인용 문헌

  1. spp: Current status and potential applications vol.39, pp.4, 2013, https://doi.org/10.3109/1040841X.2012.722606
  2. Characterization of Lignocellulolytic Enzymes from White-Rot Fungi vol.70, pp.4, 2015, https://doi.org/10.1007/s00284-014-0743-0
  3. Application of ligninolytic potentials of a white-rot fungus Ganoderma lucidum for degradation of lindane vol.188, pp.10, 2016, https://doi.org/10.1007/s10661-016-5606-7
  4. in xylanase enzyme production and its activity using agroindustry waste vol.230, pp.1755-1315, 2019, https://doi.org/10.1088/1755-1315/230/1/012078