Mycobiology

The Korean Society of Mycology (한국균학회)
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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)
  • Received : 2010.12.16
  • Accepted : 2011.05.13
  • Published : 2011.06.30
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Abstract

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.

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References

  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

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