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Current IssueEditorial BoardOnline First ArticlesArchive

volume 33 issue 3 (september 2010) : 157 -163

COMPARISON OF CATECHOLASE (PPO) ACTIVITY IN WHOLE SEEDS AND THEIR COMPONENTS (TESTA, COTYLEDON AND EMBRYO) OF FOUR LEGUME SPECIES FROM GENUS LUP/NUS

T
T. Aniszewski
1Research and Teaching Laboratory of Applied Botany, University of Eastern Fintand, Joensuu Campus, Joensuu. Finland.

  • Submitted|

  • First Online |

  • doi

Cite article:- Aniszewski T. (2025). COMPARISON OF CATECHOLASE (PPO) ACTIVITY IN WHOLE SEEDS AND THEIR COMPONENTS (TESTA, COTYLEDON AND EMBRYO) OF FOUR LEGUME SPECIES FROM GENUS LUP/NUS. Legume Research. 33(3): 157 -163. doi: .

ABSTRACT

Catecholase activity was studied polarographically in whole seeds and their three laboratory separated components (seed testa, cotyledons and embryo) of Lupinus a/bus, Lupinus angustilo/ius, Lupinus /uteus and Lupinuspo/yphy//us. The weight of seeds and their components and hydration varied noticeably between species. The weight of seeds and their components is not visible in catecholase activity. This enzyme was active in whole seeds and their components but with different intensites. The smallest activity across the four species waS measured in Lupinus a/busand Lupinuspo/yphy//usand the highest in Lupinus /uteus. The smallest values were found in the embryo and the highest in the cotyledons (Lupinus a/bus, Lupinus angustilo/iusand Lupinus /uteus) and seed testa (Lupinus po/yphyJ/us). The present results indirectly provide evidence of the protective potential of seed catecholase activity in cells after mechanical destruction of seed cellular structures. The most relevant explanation for the differences in catecholase activity between lupin species would appear to be genetic. The activity of this enzyme can be used as a taxon parameter and gene expression marker, and has possible implications for use in the intensification of germination and in biotechnological and molecular applications of legumes

REFERENCES

  1. Aniszewski, T. (2005) Plant biology. American Society of Plant Biologists, Seattle, Washington. pp. 198-199.
  2. Aniszewski, T. (2006) Acta BioI. Cracov. Bot., 48: 59-65.
  3. Aniszewski, T. et al. (2008) Acta BioI. Cracov. Bot.. 50: 7-18.
  4. Arslan,o. eta!. (1997) J AgJic. Food Chem., 45: 2861-2863.
  5. Borek, S. et al. (2009) J Exp. Bot., 60 : 453-3466.
  6. Ciesiolka, D. eta!. (2008) Acta Soc. Bot. Poloniae, 77 : 93-98.
  7. Demeke, T. etal. (2001) PlantBreed., 120:369-373.
  8. Duenas. M. etal. (2009) Food Chem., 117: 599-607. Gawlik-Dziki, U. eta!. (2008) FoodChem., 107: 129-135.
  9. Halder. J. etal. (1998) J NutI'. Biochem., 9: 75-80.
  10. Hela, E.o. eta!. (2008) Caryol.. 61: 354-362.
  11. Kavravan, D. and Aydemir, T. (2001) Food Chem" 74: 147-154.
  12. Lei, D.F. eta!. (2004) Prog. Nat. Sci., 14: 553-56l.
  13. Liao, Z. etal. (2006) Mol. Biol., 40: 907-913.
  14. Maki, H. and Morohashi, Y. (2006) J Plant Physioi., 163: 1-10.
  15. Marshall, M. R. et al. (2000) Enzymatic Browning in Fruits, Vegetable and Seafoods. FAO, Rome, Italy.
  16. Mayer, A. M. (2006) Phytochem. 67: 193-215.
  17. McCaig, T. N. et a!. (1999) Can. J Plant Sel, 79 : 507-514.
  18. Mourato, M. P et al. (2009) Bioi. Plant., 53 . 105-111.
  19. Pastor-Cavada, E. et al. (2009) Food Chem., 117: 466-469.
  20. Rapeanu, G. etal. (2006) FoodChem., 94; 253-261.
  21. Rommens, C. M. etai. (2006) J. Agric. Food Chem., 54: 9882-9887.
  22. Sahbaz, R. etal. (2009) J Appl. Bot. Food Quai., 82: 163-169.
  23. Unal, M.U. and Sener, A. (2006) J Sci. Food Agric., 86: 2374-2379.
  24. Yoruk, R. and Marshall, M. R. (2003) J Food Biochem., 27: 361-422
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    volume 33 issue 3 (september 2010) : 157 -163

    COMPARISON OF CATECHOLASE (PPO) ACTIVITY IN WHOLE SEEDS AND THEIR COMPONENTS (TESTA, COTYLEDON AND EMBRYO) OF FOUR LEGUME SPECIES FROM GENUS LUP/NUS

    T
    T. Aniszewski
    1Research and Teaching Laboratory of Applied Botany, University of Eastern Fintand, Joensuu Campus, Joensuu. Finland.

    • Submitted|

    • First Online |

    • doi

    Cite article:- Aniszewski T. (2025). COMPARISON OF CATECHOLASE (PPO) ACTIVITY IN WHOLE SEEDS AND THEIR COMPONENTS (TESTA, COTYLEDON AND EMBRYO) OF FOUR LEGUME SPECIES FROM GENUS LUP/NUS. Legume Research. 33(3): 157 -163. doi: .

    ABSTRACT

    Catecholase activity was studied polarographically in whole seeds and their three laboratory separated components (seed testa, cotyledons and embryo) of Lupinus a/bus, Lupinus angustilo/ius, Lupinus /uteus and Lupinuspo/yphy//us. The weight of seeds and their components and hydration varied noticeably between species. The weight of seeds and their components is not visible in catecholase activity. This enzyme was active in whole seeds and their components but with different intensites. The smallest activity across the four species waS measured in Lupinus a/busand Lupinuspo/yphy//usand the highest in Lupinus /uteus. The smallest values were found in the embryo and the highest in the cotyledons (Lupinus a/bus, Lupinus angustilo/iusand Lupinus /uteus) and seed testa (Lupinus po/yphyJ/us). The present results indirectly provide evidence of the protective potential of seed catecholase activity in cells after mechanical destruction of seed cellular structures. The most relevant explanation for the differences in catecholase activity between lupin species would appear to be genetic. The activity of this enzyme can be used as a taxon parameter and gene expression marker, and has possible implications for use in the intensification of germination and in biotechnological and molecular applications of legumes

    REFERENCES

    1. Aniszewski, T. (2005) Plant biology. American Society of Plant Biologists, Seattle, Washington. pp. 198-199.
    2. Aniszewski, T. (2006) Acta BioI. Cracov. Bot., 48: 59-65.
    3. Aniszewski, T. et al. (2008) Acta BioI. Cracov. Bot.. 50: 7-18.
    4. Arslan,o. eta!. (1997) J AgJic. Food Chem., 45: 2861-2863.
    5. Borek, S. et al. (2009) J Exp. Bot., 60 : 453-3466.
    6. Ciesiolka, D. eta!. (2008) Acta Soc. Bot. Poloniae, 77 : 93-98.
    7. Demeke, T. etal. (2001) PlantBreed., 120:369-373.
    8. Duenas. M. etal. (2009) Food Chem., 117: 599-607. Gawlik-Dziki, U. eta!. (2008) FoodChem., 107: 129-135.
    9. Halder. J. etal. (1998) J NutI'. Biochem., 9: 75-80.
    10. Hela, E.o. eta!. (2008) Caryol.. 61: 354-362.
    11. Kavravan, D. and Aydemir, T. (2001) Food Chem" 74: 147-154.
    12. Lei, D.F. eta!. (2004) Prog. Nat. Sci., 14: 553-56l.
    13. Liao, Z. etal. (2006) Mol. Biol., 40: 907-913.
    14. Maki, H. and Morohashi, Y. (2006) J Plant Physioi., 163: 1-10.
    15. Marshall, M. R. et al. (2000) Enzymatic Browning in Fruits, Vegetable and Seafoods. FAO, Rome, Italy.
    16. Mayer, A. M. (2006) Phytochem. 67: 193-215.
    17. McCaig, T. N. et a!. (1999) Can. J Plant Sel, 79 : 507-514.
    18. Mourato, M. P et al. (2009) Bioi. Plant., 53 . 105-111.
    19. Pastor-Cavada, E. et al. (2009) Food Chem., 117: 466-469.
    20. Rapeanu, G. etal. (2006) FoodChem., 94; 253-261.
    21. Rommens, C. M. etai. (2006) J. Agric. Food Chem., 54: 9882-9887.
    22. Sahbaz, R. etal. (2009) J Appl. Bot. Food Quai., 82: 163-169.
    23. Unal, M.U. and Sener, A. (2006) J Sci. Food Agric., 86: 2374-2379.
    24. Yoruk, R. and Marshall, M. R. (2003) J Food Biochem., 27: 361-422
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