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ILNS > Volume 25 > Kinetics Properties of Polyphenol Oxidase in...
Kinetics Properties of Polyphenol Oxidase in Hawthorn (<i>Crataegus spp</i>)
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Kinetics Properties of Polyphenol Oxidase in Hawthorn (Crataegus spp)

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Abstract:

Polyphenol oxidase (PPO) from hawthorn was extracted and partially purified through (NH4)2SO4 precipitation, dialysis and ion exchange chromatography. The activity of polyphenol oxidase was investigated in Crataegus spp. Spectrophotometric method was used to assay the enzyme activity and the kinetic constants - maximum enzyme velocity (Vmax) and Michealis - Menten constant (Km). Of the substrates tested, catechol was the best substrate for PPO with a Km value of 2.2 mM. The optimum pH for PPO activity was found to be 7. The enzyme showed high activity over a broad pH range of 4 - 8. The optimal pH and temperature for enzyme activity were found to be 7 and 40-45 °C, respectively. km value for hawthorn PPO is calculated 22 mM for catechol and 6.7 mM for pyrogallol and 9.7 mM for L-dopa. As can be seen, affinity of PPOs for various substrates varies widely. The enzyme showed a broad activity over a broad pH and temperature range. The thermal inactivation studies showed that the enzyme is heat resistant. The enzyme showed the highest activity toward pyrogallol and no activity toward tyrosine. Of the inhibitors tested, the most potent inhibitors were kojic acid, cysteine and glycine , respectively

Info:

Periodical:
International Letters of Natural Sciences (Volume 25)
Pages:
29-38
DOI:
https://doi.org/10.18052/www.scipress.com/ILNS.25.29
Citation:
S. Saeidian, "Kinetics Properties of Polyphenol Oxidase in Hawthorn (Crataegus spp)", International Letters of Natural Sciences, Vol. 25, pp. 29-38, 2014
Online since:
September 2014
Authors:
Shahriar Saeidian
Keywords:
Hawthorns’ Thermal Inactivation, Inhibition, Kinetics, Polyphenol Oxidase, Purification
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Open Access

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References:

[1] J. Heinerman, Heinerman's Encyclopedia of Healing Herbs and Spices. West Nyack, NY: Parker, (1996).

[2] C. Hobbs, S. Foster, Herbal Gram 22 (1990) 19-33.

[3] A.Y. Leung, S. Foster. Encyclopedia of Common Natural Ingredients: Used in Food, Drugs, and Cosmetics. 2nd ed. New York: John Wiley, (1996).

[4] W. Broothaerts, J. LI.B. Mcpherson, E. Randall, W.D. Lane, P.A. Wierma, J. Agric. Food Chem. 48 (2000) 5924-5928.

[5] C.W. Van Gelder, W.H. Flurkey, H.J. Wichers, Phytochemistry 45 (1997) 1309-1323.

[6] L. Vamos-Vigyazo, Crit Rev Food Sci. 15 (1981) 49-127.

[7] D.A. Robb. In: Contie R (ed), 2 (1984) 207-241. CRC Press. Boca Raton, FL.

[8] A. Sanchez-Amat, F. Solano, Biochem Biophys. Res. Comm. 240 (1997) 787-79.

[9] O.H. Lowry, A. L. Farr, Rosebrough, R. J. Randall, J. Food Biochem 8(3) (1984) 137-162.

[10] E.J. Lourenço, J.S. Leão, V.A. Neves, Journal of Science Food and Agriculture 52 (1990) 249-259.

[11] E.M. Gonzalez, B. Ancos, M.P. Cano, Journal of Agriculture and Food Chemistry 48 (2000) 5459-5464.

[12] D. Kavrayan, T. Aydemir, Food Chemistry 74 (2001) 147-154.

[13] G. Rapeanu, A. Van Loey, C. Smout, M. Hendrickx, Food Chemistry 94 (2006) 253-261.

[14] S. Saeidian, International Journal of Advanced Biological and Biomedical Research 1(6) (2013) 637-648.

[15] K. Duangmal, RKO. Apenten. Food Chem 64 (1999) 351-359.

[16] L. Vamos-Vigyazo, Crit. Rev Food Sci. 15 (1981) 49-127.

[17] M.Ü. Ünal, Food Chem. 100 (2007) 909-913.

[18] M.Ü. Ünal, A. Fiener, J Sci Food Agric. 86 (2006) 2374-2379.

[19] U. Gawlik-Dziki, U. Szymanowska, B. Baraniak. Food Chem. 105 (2007) 1047-1053.

[20] VM. Gomez-Lopez, Food Chem. 77 (2007) 163-169.

[21] J. Halder, P. Tamuli, A.N. Phaduri, Journal of Nutritional Biochemistry 9 (1998) 75-80.

[22] M. Dogan, O. Arslan, S. Dogan, Int J Food Sci Technol 37 (2002) 415-423.

[23] CK. Ding, K. Chachin, Y. Ueda, Y. Imahori, J Agric Food Chem 46 (1998) 4144-4149.

[24] C-P. Yang, S. Fujita, K. Kohno, A. Kusubayashi, MD. Ashrafuzzaman, N. Hayashi, J Sci Food Agric 49 (2001) 1446-1449.

[25] DS. Robinson, NAM. Eskin (eds), J. Zawistowski, CG. Biliaderis,. Elsevier, New York, 1991, pp.217-273. ( Received 24 August 2014; accepted 31 August 2014 ).

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