Skip to main content
Log in

Cellular localization of acid carboxypeptidase inAspergillus oryzae

  • Published:
Current Microbiology Aims and scope Submit manuscript

Abstract

Fresh mycelia ofAspergillus oryzae were shown to have strong acid carboxypeptidase (EC 3.4.12.-) activity. The cellular localization of acid carboxypeptidase was investigated using the broken mycelia and the protoplasts of the fungusAspergillus oryzae IAM 2640. In the broken mycelia, about 40% of the total activity was found in the “cell wall” fraction (2,000×g), with most of the remainder in the soluble fraction (100,000×g supernatant). During the formation of protoplasts, most of the acid carboxypeptidase in the mycelia was solubilized and released. The specific activity of acid carboxypeptidase in the lysed protoplasts was about 10-fold lower than that found in the broken mycelial preparation. These data indicate that most of the acid carboxypeptidase is probably located in the cell surface, which includes the cell wall, the periplasm, and the cell membrane.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Literature Cited

  1. Arai, T., Ichishima, E. 1974. Mode of action on proteins of acid carboxypeptidase fromAspergillus saitoi. Journal of Biochemistry76:765–769.

    PubMed  CAS  Google Scholar 

  2. De Waard, M. A. 1976. Formation of protoplasts fromUstilago maydis. Antonie van Leeuwenhock42:211–216.

    Article  CAS  Google Scholar 

  3. Ichishima, E. 1972. Purification and characterization of a new type of acid carboxypeptidase fromAspergillus. Biochimica et Biophysica Acta258:274–288.

    Article  PubMed  CAS  Google Scholar 

  4. Ichishima, E. 1972. A new type of carboxypeptidase. Protein, Nucleic Acid and Enzyme17:874–886.

    CAS  Google Scholar 

  5. Ichishima, E., Arai, T. 1973. Specificity and mode of action of acid carboxypeptidase fromAspergillus saitoi. Biochimica et Biophysica Acta293:444–450.

    Article  PubMed  CAS  Google Scholar 

  6. Ichishima, E., Sonoki, S., Hirai, K., Torii, Y., Yokoyama, S. 1972. Comparative study on enzymatic properties of acid carboxypeptidase of molds of the genusAspergillus. Journal of Biochemistry72:1045–1048.

    PubMed  CAS  Google Scholar 

  7. Ichishima, E., Takeuchi, M., Yasuda, R., Suzuki, Y., Kobayashi, S. 1977. C-Terminal peptidyl-l-proline hydrolase activity ofAspergillus acid carboxypeptidase. Journal of Biochemistry81:1733–1737.

    PubMed  CAS  Google Scholar 

  8. Ichishima, E., Yamane, A., Nitta, T., Kinoshita, M., Nikkuni, S., Oka, Y., Yokoyama, S. 1973. Production of a new type of acid carboxypeptidase of molds of theAspergillus niger group. Applied Microbiology26:327–331.

    PubMed  CAS  Google Scholar 

  9. Lowry, O. H., Rosenbrough, H. J., Farr, A. L., Randall, R. I. 1951. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry193:265–275.

    PubMed  CAS  Google Scholar 

  10. Moore, P. M., Peberdy, J. F. 1976. A particulate chitin synthase fromAspergillus flavas link: The properties, location and levels of activity in mycelium and regenerating protoplast preparation. Canadian Journal of Microbiology22:915–921.

    Article  PubMed  CAS  Google Scholar 

  11. Peberdy, J. F., Moore, P. M. 1975. Chitin synthase inMortierella vinacea: Properties, cellular location and synthesis in growing cultures. Journal of General Microbiology90:228–236.

    PubMed  CAS  Google Scholar 

  12. Villanueva, J. R., Garcia-Acha, I., Gascon, S., Uruburu, F. 1973. Yeast, mould and plant protoplasts. New York: Academic Press.

    Google Scholar 

  13. Yokoyama, S., Ichishima, E. 1972. A new type of acid carboxypeptidase of molds of gee genusPenicillium. Agricultural and Biological Chemistry36:1259–1261.

    CAS  Google Scholar 

  14. Yokoyama, S., Oobayashi, A., Tanabe, O., Ichishima, E. 1975. Action of crystalline acid carboxypeptidase fromPenicillium janthinellum. Biochimica et Biophysica Acta377:443–448.

    Google Scholar 

  15. Yokoyama, S., Oobayashi, A., Tanabe, O., Ohata, K., Shibata, Y., Ichishima, E. 1975. Kininase and anti-inflammatory activities of acid carboxypeptidase fromPenicillium janthinellum. Experientia31:1122–1123.

    Article  PubMed  CAS  Google Scholar 

  16. Yokoyama, S., Oobayashi, A., Tanabe, O., Sugawara, S., Araki, E., Ichishima, E. 1974. Production and some properties of a new type of acid carboxypeptidase ofPenicillum molds. Applied Microbiology27:953–960.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Nomi, T., Mikami, S., Yamane, A. et al. Cellular localization of acid carboxypeptidase inAspergillus oryzae . Current Microbiology 1, 25–28 (1978). https://doi.org/10.1007/BF02601702

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02601702

Keywords

Navigation