Hydrolytic enzyme activities and degradation of storage components in cotyledons of germinatingPhaseolus mungo seeds

  • Takao Minamikawa
Article

Abstract

Phaseolus mungo seeds were allowed to germinate in the dark, and time-course changes in contents of protein fractions, starch, soluble α-amino nitrogen and reducing sugars and in hydrolytic enzyme activities in cotyledons were investigated. In cotyledons of germinated seeds, marked increases in proteolytic (caseolytic, globulytic and gelatin-hydrolyzing) activities and amylolytic activity occurred with concurrent mobilization of storage proteins and starch. Removal of axis organs from seeds at very early stages of germination caused the deteriorated breakdown of storage components and decreased development of proteolytic enzymes in the cotyledons, but this treatment did not significantly affect the appearance of amylolytic activity. The experimental results are discussed in comparison with the hydrolytic enzyme activities of germinating seeds of other leguminous species.

Keywords

Proteolytic Activity Storage Protein Mung Bean Embryonic Axis Amylolytic Activity 

Abbreviations

TCA

trichloroacetic acid

SDS

sodium dodecyl sulfate

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References

  1. Ashton, F.M. 1976. Mobilization of storage proteins of seeds. Ann. Rev. Plant Physiol.27: 95–117.CrossRefGoogle Scholar
  2. Basha, S.M.M. andL. Beevers. 1975. The development of proteolytic activity and protein degradation during the germination ofPisum sativum L. Planta124: 77–87.CrossRefGoogle Scholar
  3. — andJ.P. Cherry. 1978. Proteolytic enzyme activity and storage protein degradation in cotyledons of germinating peanut (Arachis hypogaea L.) seeds. J. Agr. Food Chem.26: 229–234.CrossRefGoogle Scholar
  4. Baumgartner, B. andM.J. Chrispeels. 1976. Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung beans. Plant Physiol.58: 1–6.PubMedGoogle Scholar
  5. — and —. 1977. Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings. Eur. J. Biochem.77: 223–233.PubMedCrossRefGoogle Scholar
  6. Beevers, L. 1968. Protein degradation and proteolytic activity in the cotyledons of germinating pea seeds (Pisum sativum). Phytochemistry7: 1837–1844.CrossRefGoogle Scholar
  7. Bernfeld, P. 1955. Enzymes of carbohydrate metabolism. Amylases, α and β.In: S.P. Colowick and N.O. Kaplan, ed., Methods in Enzymology1: 149–158. Academic Press, New York.CrossRefGoogle Scholar
  8. Chrispeels, M.J. andD. Boulter. 1975. Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase. Plant Physiol.55: 1031–1037.PubMedGoogle Scholar
  9. Dale, J.E. 1969. Gibberellins and early growth in seedlings ofPhaseolus vulgaris. Planta89: 155–164.CrossRefGoogle Scholar
  10. Gepstain, S. andI. Ilan. 1970. A promotive action of kinetin on amylase activity in cotyledons ofPhaseolus vulgaris. Plant Cell Physiol.11: 819–822.Google Scholar
  11. Guardiola, J.L. andJ.F. Sutcliffe. 1971. Control of protein hydrolysis in the cotyledons of germinating pea (Pisum sativum L.) seeds. Ann. Bot.35: 791–807.Google Scholar
  12. Harris, N. andM.J. Chrispeels. 1975. Histochemical and biochemical observations on storage protein metabolism and protein body autolysis in cotyledons of germinating mung beans. Plant Physiol.56: 292–299.PubMedGoogle Scholar
  13. —— andD. Boulter. 1975. Biochemical and histochemical studies on protease activity and reserve protein metabolism in the cotyledons of germinating cowpeas (Vigna unguiculata). J. Exp. Bot.26: 544–554.Google Scholar
  14. Lowry, O.H., N.J. Rosebrough, A.L. Farr andR.J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem.193: 265–275.PubMedGoogle Scholar
  15. Mikola, J. 1976. Activities of various peptidases in cotyledons of germinating peanut (Arachis hypogaea). Physiol. Plant.36: 255–258.CrossRefGoogle Scholar
  16. Pirsco, J.T., I.L. Ainouz andS. de C. Melo. 1975. Changes in nitrogenous compounds and proteases during germination ofVigna sinensis seeds. Physiol. Plant.33: 18–21.CrossRefGoogle Scholar
  17. Pusztai, A. andI. Duncan. 1971. Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta96: 317–325.CrossRefGoogle Scholar
  18. Seeschaaf, K.W. andP. Pirson. 1971. Enzymregulation in Lupinenkeimblättern. Biochem. Physiol. Pflanzen162: 177–192.Google Scholar
  19. Somogyi, M. 1952. Notes on sugar determination. J. Biol. Chem.195: 19–23.Google Scholar
  20. Weber, K. andM. Osborn. 1969. The reliability of molecular weight determinations by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem.244: 4406–4412.PubMedGoogle Scholar
  21. Yemm, E.W. andCocking, E.C.. 1955. The determination of amino-acids with ninhydrin. Analyst80: 209–213.CrossRefGoogle Scholar
  22. Yomo, H. andK. Srinivasan. 1973. Protein breakdown and formation of protease in attached and detached cotyledons ofPhaseolus vulgaris L. Plant Physiol.52: 671–673.PubMedGoogle Scholar
  23. — andJ.E. Varner. 1973. Control of the formation of amylases and proteases in the cotyledons of germinating peas. Plant Physiol.51: 708–713.PubMedGoogle Scholar
  24. Youle, R.J. andA.H.C. Huang. 1978. Albumin storage proteins in the protein bodies of castor bean. Plant Physiol.61: 13–16.PubMedCrossRefGoogle Scholar

Copyright information

© The Botanical Society of Japan 1979

Authors and Affiliations

  • Takao Minamikawa
    • 1
  1. 1.Department of BiologyTokyo Metropolitan UniversityTokyo

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