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Effect of Temperature on Guaiacol Peroxidase of Pyrus communis

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Peroxidase (EC; 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.


International Letters of Natural Sciences (Volume 5)
S. Saeidian and E. Ghasemifar, "Effect of Temperature on Guaiacol Peroxidase of Pyrus communis", International Letters of Natural Sciences, Vol. 5, pp. 46-51, 2013
Online since:
November 2013

W. Adam, M. Lazarus, C. R. Saha-Moller, O. Weichold, U. Hoch, P. Schreier, Advance Biochemical Engineering 63 (1999) 74-108.

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.

K. Ghafoor, Y. H. Choi, Journal of Food Engineering 35 (2012) 391-402.

A. A. Khan, D. S. Robinson, Food Chemistry 46 (1993) 61-64.

H. W. Krell, (1991).

D. W. Stanley, M. C. Bourne, A. P. Stone, W. V. Wismer, Journal of Food Science 60 (1995) 327-333.

K. Wakamatsu, U. Takahama, Physiology of Plants 88 (1993) 167-171.

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, pp.2-7. ACS symposium series 600, Washington, DC, America Chemical Society.

O. H. Lowry, N. J. Rosebrough, A. L. Farr, R. J. Randall, J. Biol. Chem. 193 (1951) 265-27.

H. Zhou, X. Feng, J. Sci. Food Agric. 57 (1991) 307-313.

E. H. Lowrenco, J. D. H. Leao, V. A. Neves, J. Sci. Food and Agri. 52 (1990) 249-260.

Y. Jiang, X. Duan , D. Joyce, Z. Li, J Zhang, Food Chemistry 88 (2004) 443-446. ( Received 11 November 2013; accepted 15 November 2013 ).

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[1] d. Marcio, M. Juliana, P. Francisco, F. Natoniel, V. Katia, "Purification and characterization of a peroxidase present in xilopodium exsudates of umbu plants (Spondias tuberosa A.)", African Journal of Biotechnology, Vol. 14, p. 1838, 2015


[2] J. Gouot, J. Smith, B. Holzapfel, C. Barril, "Grape Berry Flavonoid Responses to High Bunch Temperatures Post Véraison: Effect of Intensity and Duration of Exposure", Molecules, Vol. 24, p. 4341, 2019


[3] N. Netithammakorn, E. Smith, C. Lerpiniere, J. Shen, "Peroxidase‐catalysed coloration of wool fabrics", Coloration Technology, 2020