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2013 | 05 |

Tytuł artykułu

Effect of temperature on guaiacol peroxidase of Pyrus communis

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Peroxidase (EC 1.11.1.7; donor: hydrogen-peroxide oxidoreductase, POD) is one of the key enzymes controlling plant growth, differentiation and development. The enzyme participates in construction, rigidification and eventual lignification of cell walls, biosynthesis of ethylene from 1-aminocyclopropane-1-carboxylic acid and H2O2, regulation of auxin level through auxin catabolism, protection of tissue from damage and infection by pathogenic microorganisms, the oxidation of indoleacetic acid. For peroxidase activity in wild pears extract one pH optimum was observed at 6.5 that probably belong to atleast one isoenzyme. Activity of peroxidase in presence of guaiacol and H2O2 was optimum after incubation at 40 °C. Maximum activity of peroxidase is 300 % .Activity increased to 240 %, 300 %, 70 % and 10 % after 60 minute incubation at 30, 40, 45 and 60 °C for peroxidase. Incubation at high temperature (70 °C) was accompanied with decrease of activity to 10 % peroxidase activity.

Wydawca

-

Rocznik

Tom

05

Opis fizyczny

p.46-51,fig.,ref.

Twórcy

autor
  • Department of Biology, Payame Noor University, I.R.of Iran, Iran
  • Department Of Biology, Payame Noor University, I.R. of Iran, Iran

Bibliografia

  • [1] W. Adam, M. Lazarus, C. R. Saha-Moller, O. Weichold, U. Hoch, P. Schreier, Advance Biochemical Engineering 63 (1999) 74-108.
  • [2] H. B. Dunford (1991). Horseradish peroxidase: structure and kinetic properties. In: Everse J., Everse K. E., Grisham M. B. (eds.). Peroxidase in Chemistry and Biology (pp. 1-24) CRC Press, Boca Raton, FL.
  • [3] K. Ghafoor, Y. H. Choi, Journal of Food Engineering 35 (2012) 391-402.
  • [4] A. A. Khan, D. S. Robinson, Food Chemistry 46 (1993) 61-64.
  • [5] H. W. Krell, (1991). Peroxidase. An important enzyme for diagnostic test kits. In: Lobarsewski J, Greppin H, Penel C and Gaspar Th (eds.) Biochemical, Molecular and Physiological Aspects of Plant Peroxidases (pp. 469-478) Univ. M. Curie-Sklodowska and Univ. Geneva, Lublin and Geneva.
  • [6] D. W. Stanley, M. C. Bourne, A. P. Stone, W. V. Wismer, Journal of Food Science 60 (1995) 327-333.
  • [7] K. Wakamatsu, U. Takahama, Physiology of Plants 88 (1993) 167-171.
  • [8] J. R. Whitaker, C. Y. Lee (1995). Recent advances in chemistry of enzymatic browning. In Lee C. Y. and Whitaker J. R. eds. Enzymatics Browning and it’s prevention, p. 2-7. ACS symposium series 600, Washington, DC, America Chemical Society.
  • [9] O. H. Lowry, N. J. Rosebrough, A. L. Farr, R. J. Randall, J. Biol. Chem. 193 (1951) 265-27.
  • [10] H. Zhou, X. Feng, J. Sci. Food Agric. 57 (1991) 307-313.
  • [11] E. H. Lowrenco, J. D. H. Leao, V. A. Neves, J. Sci. Food and Agri. 52 (1990) 249-260.
  • [12] Y. Jiang, X. Duan , D. Joyce, Z. Li, J Zhang, Food Chemistry 88 (2004) 443-446.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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