Production of macerating enzymes of mandarin orange peel by fungal cultures

  • Naomichi Nishio
  • Shiro Nagai
Industrial Microbiology

Summary

Thirty-nine fungal cultures belonging to the genera of Aspergillus, Podospora, Sordaria, Cbaetomium, Iodophanus, Scleotinia, Coniella, Pellicularia and others, were examined for the production of enzymes which macerate the mandarin orange peel using a wheat bran as substrate. An isolated strain of Aspergillus niger was an excellent producer of macerating enzymes compared to other organisms tested. The peel of the mandarin orange could be macerated by the crude enzymes produced by isolated A. niger. The maceration of 1 g of peel/24 h yielded 0.57 g of reducing sugars. Expressed differently, 83% of solid peel materials were released from the peel into the water/24 h under the following conditions: a peel concentration of 8 g peel/l, a crude enzyme concentration of 1 g protein/l, a temperature of 40°C, a pH of 5, a 24 h incubation time and 120 rpm reciprocal shaking. The test of the macerating activity of commercially available hydrolases on the orange peel showed that the two samples of pectinase originating from A. niger had about the same activity as isolated A. niger whereas the two samples of cellulase originating from Trichoderma viride had remarkably lower activities than A. niger.

References

  1. Barker, K.R., Walker, J.C. (1962). Phytopathology 52, 1119–1125Google Scholar
  2. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A., Smith, F. (1956). Anal. Chem. 28, 350–356Google Scholar
  3. Endo, A. (1964). Agric. Biol. Chem. 28, 757–764Google Scholar
  4. Ghose, T.K. (1977). Bioconversion of cellulosic substances into energy, chemicals and microbial protein. Aroon Purie at Thomson Press (India)Google Scholar
  5. Hamisa, F.A., Mabrouk, S.S., Abdel-Fattah, A.F. (1977). J. Gen. Appl. Microbiol. 23, 23–27Google Scholar
  6. Koller, A. (1966). Dissertation No. 3774. ETH, ZürichGoogle Scholar
  7. Lequerica J.L., Lafuente, B. (1977). Rev. Agroquim. Tecnol. Aliment. 17, 71–78Google Scholar
  8. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951). J. Biol. Chem. 193, 265–275Google Scholar
  9. Mukherjee, S.K., Majumdar, S.K. (1971). J. Ferment. Technol. 49, 759–770Google Scholar
  10. Nelson, N. (1944). J. Biol. Chem. 153, 375–380Google Scholar
  11. Oi, S., Satomura, Y. (1965). Agric. Biol. Chem. 29, 936–942Google Scholar
  12. Shinmyo, A., Davis, I.K., Nomoto, F., Tahara, T., Enatsu, T. (1978). European J. Appl. Microbiol. Biotechnol. 5, 59–68Google Scholar

Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • Naomichi Nishio
    • 1
  • Shiro Nagai
    • 1
  1. 1.Department of Fermentation Technology, Faculty of EngineeringHiroshima UniversityHiroshimaJapan

Personalised recommendations