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. 1976 Nov;58(5):618–621. doi: 10.1104/pp.58.5.618

Starch Degradation in the Cotyledons of Germinating Lentils

Jorge Fernández Tárrago a, Gregorio Nicolás a,1
PMCID: PMC542269  PMID: 16659730

Abstract

Starch, total amylolytic and phosphorylase activities were determined in lentil cotyledons during the first days of germination. Several independent criteria show that the amylolytic activity is due mainly to an amylase of the α type. Starch is degraded slowly in the first days; during this time, α- and β-amylase activity are very low, while phosphorylase increases and reach a peak on the 3rd day. On the 4th day, there is a more rapid depletion of starch which coincides with an increase in α-amylase activity. By polyacrylamide gel electrophoresis of the crude starch-degrading enzyme, five bands were obtained: one phosphorylase, three α-amylases, and one β-amylase. Based on their heat lability or heat stability, two sets of α-amylase seem to exist in lentil cotyledons.

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Selected References

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  1. Allen R. J. The estimation of phosphorus. Biochem J. 1940 Jun;34(6):858–865. doi: 10.1042/bj0340858. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  3. Dure L. S. Site of Origin and Extent of Activity of Amylases in Maize Germination. Plant Physiol. 1960 Nov;35(6):925–934. doi: 10.1104/pp.35.6.925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Goldstein L. D., Jennings P. H. The Occurrence and Development of Amylase Enzymes in Incubated, De-embryonated Maize Kernels. Plant Physiol. 1975 May;55(5):893–898. doi: 10.1104/pp.55.5.893. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Juliano B. O., Varner J. E. Enzymic degradiation of starch granules in the cotyledons of germinating peas. Plant Physiol. 1969 Jun;44(6):886–892. doi: 10.1104/pp.44.6.886. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Murata T. Enzymic mechanism of starch breakdown in germinating rice seeds I. An analytical study. Plant Physiol. 1968 Dec;43(12):1899–1905. doi: 10.1104/pp.43.12.1899. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Swain R. R., Dekker E. E. Seed germination studies. 3. Properties of a cell-free amino acid incorporating system from pea cotyledons; possible origin of cotyledonary alpha-amylase. Plant Physiol. 1969 Mar;44(3):319–325. doi: 10.1104/pp.44.3.319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Swain R. R., Dekker E. E. Seed germination studies. I. Purification and properties of an alpha-amylase from the cotyledons of germinating peas. Biochim Biophys Acta. 1966 Jul 6;122(1):75–86. doi: 10.1016/0926-6593(66)90092-0. [DOI] [PubMed] [Google Scholar]
  10. Swain R. R., Dekker E. E. Seed germination studies. II. Pathways for starch degradation in germinating pea seedlings. Biochim Biophys Acta. 1966 Jul 6;122(1):87–100. doi: 10.1016/0926-6593(66)90093-2. [DOI] [PubMed] [Google Scholar]
  11. Tanaka Y., Ito T., Akazawa T. Enzymic Mechanism of Starch Breakdown in Germinating Rice Seeds: III. alpha-Amylase Isozymes. Plant Physiol. 1970 Nov;46(5):650–654. doi: 10.1104/pp.46.5.650. [DOI] [PMC free article] [PubMed] [Google Scholar]

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