Kinetics of Thermal Inactivation of Peroxidases and Polyphenol Oxidase in Pineapple (Ananas comosus)

  • Lee, Ting Hun (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Chua, Lee Suan (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Tan, Eddie Ti Tjih (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Yeong, Christina (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Lim, Chew Ching (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Ooi, Siew Yin (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Aziz, Ramlan bin Abdul (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Aziz, Azila binti (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia) ;
  • Sarmidi, Mohd Roji bin (Chemical Engineering Pilot Plant (CEPP), Faculty of Chemical and Natural Resources Engineering, University Technology Malaysia)
  • Published : 2009.06.30

Abstract

The heat tolerance and the inactivation kinetics of peroxidase (POD) and polyphenol oxidase (PPO) in pineapples (Ananas comosus) were studied in the temperature range $45-95^{\circ}C$. The kinetic parameters, such as deactivation rate constant (k), activation energy ($E_a$), and decimal reduction rate (D) of the thermal inactivation process, were determined. POD in pineapples showed biphasic inactivation behavior at temperatures range $45-75^{\circ}C$ but was monophasic at $85-95^{\circ}C$. This indicate that POD has 2 isozymes, namely heat labile and heat resistant, with $E_a$ of 68.79 and 93.23 kJ/mol, respectively. On the other hand, the heat denaturation of pineapple PPO could be described as simple monophasic first-order behavior with $E_a$ of 80.15 kJ/mol. Thus, the results of this study is useful in blanching technology where it shows a shortened time with higher temperature can be applied. The determination of the heat tolerance and inactivation POD and PPO, at different temperature range as done in the present work, was very important to improve the blanching process. This also will help to optimize the pineapple canning process which is one of the most important food industries in many tropical regions.

Keywords

References

  1. Anthon GE, Barret DM. Kinetic parameters for the thermal inactivation of quality-related enzymes in carrots and potatoes. J. Agr. Food Chem. 50: 4119-4125 (2002) https://doi.org/10.1021/jf011698i
  2. William DC, Lim MH, Chen AO, Pangborn RM, Whitaker JR. Blanching of vegetables for freezing - which indicator enzyme to use. Food Technol. -Chicago 4: 130-140 (1986)
  3. Hammer FE. Oxidoreductases. pp. 221-277. In: Enzymes in Food Processing. 3rd. Nagodawithana TT, Reed G (eds). Academic Press Inc., San Diago, CA, USA(1993)
  4. Rodrigo C, Rodrigo M, Alvarruiz A, Frigola A. Thermal inactivation at high temperatures and regeneration of green asparagus peroxidase. J. Food Protect. 59: 1065-1071 (1996) https://doi.org/10.4315/0362-028X-59.10.1065
  5. Yemenicioglu A, Ozkan M, Chemroglu B. Thermal stabilities of peroxidase from fresh pinto beans. J. Food Sci. 63: 978-990 (1998)
  6. Zhou Y, Dahler JM, Underhill SJR, Wills RBH. Enzymes associated with blackheart development in pineapple fruit. Food Chem. 80: 565-572 (2002) https://doi.org/10.1016/S0308-8146(02)00375-8
  7. Whitaker JR. Mechanisms of oxidoreductases important in food component modification. pp. 121-176. In: Chemical Changes in Food During Processing. Richardson T, Finley JW (eds). Avi Publishing Company, Inc., Westport, CT, USA (1985)
  8. Rutledge P. Preparation procedure. pp. 42-67. In: Vegetable Processing. Arthey D, Dennis C (eds). VCH Publishers, New York, NY, USA (1990)
  9. Vora HM, Kyle WSA, Small DM. Activity, localization, and thermal inactivation of deteriorative enzymes in Australian carrot (Daucus carota L) variety. J. Sci. Food Agr. 79: 1129-1135 (1999) https://doi.org/10.1002/(SICI)1097-0010(199906)79:8<1129::AID-JSFA338>3.0.CO;2-1
  10. Cano MP, Hernandez A, De Ancos B. High pressure and temperature effects on enzyme inactivation in strawberry and orange products. J. Food Sci. 62: 85-88 (1997) https://doi.org/10.1111/j.1365-2621.1997.tb04373.x
  11. Soliva-Fortury RC, Elez-Martinez P, Sebastian-Caldero M, Martin-Belloso O. Kinetics of polyphenol oxidase activity inhibition and browning of avocado puree preserved by combined methods. J. Food Eng. 55: 131-137 (2002) https://doi.org/10.1016/S0260-8774(02)00027-4
  12. Ohlsson T. Pasteurisation of meat, fish, and convenience food products. pp. 163-180. In: Food Quality and Nutrition Research Priority for Thermal Processing. Downey WK (ed). Applied Science Publisher Ltd., Essex, England (1986)
  13. Campos CF, Sauza IEA, Virgi CJ, Gloria MBA. Chemical composition, enzyme activity, and effect of enzyme inactivation in flavour quality of green coconut water. J. Food Process. Pres. 20: 487-500 (1996) https://doi.org/10.1111/j.1745-4549.1996.tb00761.x
  14. Cruz RMS, Vieira MC, Silva CLM. Effect of heat and thermosonication treatments on peroxidase inactivation kinetics in watercress. J. Food Eng. 72: 8-15 (2004) https://doi.org/10.1016/j.jfoodeng.2004.11.007
  15. Ganthavorn C, Nagel CW, Powers JR. Thermal inactivation of asparagus lipoxygenase and peroxidase. J. Food Sci. 56: 47-49 (1991) https://doi.org/10.1111/j.1365-2621.1991.tb07972.x
  16. Lee YC, Hammes JK. Heat inactivation of peroxidase in corn-onthe-cob. J. Food Sci. 44: 785-787 (1979) https://doi.org/10.1111/j.1365-2621.1979.tb08501.x
  17. Tijskens LMM, Rodis PS, Hertog MLA, Waldron KW, Ingham L, Proxenia N, van Dijk C. Activity of peroxidase during blanching of peaches, carrots, and potatoes. J. Food Eng. 34: 355-370 (1997) https://doi.org/10.1016/S0260-8774(97)00101-5
  18. Alice TLU, Whitaker JR. Some factors affecting rates of heat inactivation and reactivation of horseradish peroxidase. J. Food Sci. 39: 1173-1177 (1974) https://doi.org/10.1111/j.1365-2621.1974.tb07347.x
  19. McLellan KM, Robinson DS. The effect of heat on cabbage and brussels sprout peroxidase enzymes. Food Chem. 7: 257-266 (1980) https://doi.org/10.1016/0308-8146(81)90031-5
  20. Adam JB. The kinetics and mechanism of thermal inactivation of peroxidase in buffer and vegetable, systems with reference to the high temperature short time processing of food. Campden Food Preserv. Res. Assoc. Tech. Bull. 34: 71-80 (1977)
  21. Chutintrasri B, Noomhorm A. Thermal inactivation of PPO in pineapple puree. LWT−Food Sci. Technol. 39: 492-495 (2006) https://doi.org/10.1016/j.lwt.2005.04.006
  22. Yemenicioglu A, Ozkan M, Chemroglu B. Heat inactivation kinetics of apple polyphenoloxidase and activation of its latent form. J. Food Sci. 62: 508-510 (1997) https://doi.org/10.1111/j.1365-2621.1997.tb04417.x
  23. Lee CY, Smith NL. Blanching effect on polyphenol oxidase activity in table beets. J. Food Sci. 44: 84-87 (1979) https://doi.org/10.1111/j.1365-2621.1979.tb10010.x
  24. Halim DH, Montgomery MY. Polyphenol oxidase of d'Anjou pears. J. Food Sci. 43: 603-605 (1978) https://doi.org/10.1111/j.1365-2621.1978.tb02363.x
  25. Jackson JM, Vegetables. pp. 210-233. In: Fundamentals of Food Canning Technology. Jackson JM, Shinn BM (eds). The Avi Publishing Company, Inc., Westport, CT, USA (1979)
  26. Leniger HA, Beverloo WA. Heat transfer. pp. 53-95. In: Food Processing Engineering. D. Reidel Publishing Company, Dordrechet, Holland (1975)
  27. Soysal C, Soylemez Z. Kinetics and inactivation of carrot peroxidase by heat treatment. J. Food Eng. 68: 349-356 (2005) https://doi.org/10.1016/j.jfoodeng.2004.06.009
  28. Morales-Blancas EF, Chandia VE, Cisneros-Zevallos L. Thermal inactivation kinetics of peroxidase and lipoxygenase from broccoli, green asparagus, and carrots. J. Food Sci. 67: 146-154 (2002) https://doi.org/10.1111/j.1365-2621.2002.tb11375.x
  29. Ismail N, Revathi R. Studies on the effects of bleaching time, evaporation time, temperature, and hydrocolloid on physical properties of chili (Capsicum annum var. Kulai) purer. LWT−Food Sci. Technol. 39: 19-97 (2006)
  30. Gunes B, Bayindirh, A. Peroxidase and lipoxygenase inactivation during blanching of green bean, green peas and carrots. LWT−Food Sci. Technol. 26: 406-410 (1993) https://doi.org/10.1006/fstl.1993.1080
  31. Sarikaya A, Ozilgen M. Kinetics of peroxidase inactivation during thermal processing of whole potatoes. LWT−Food Sci. Technol. 24: 159-163 (1991)
  32. Ling MH, Lund DB. Determining kinetics of parameters for thermal inactivation of heat resistant and heat labile isozymes from thermal destruction curves. J. Food Sci. 43: 1307-1310 (1978) https://doi.org/10.1111/j.1365-2621.1978.tb15295.x
  33. Oktay M, Kufrevioglu I, Kocacaliskan I, Sakiroglu H. Polyphenoloxidase from amasya apple. J. Food Sci. 60: 494-496 (1995) https://doi.org/10.1111/j.1365-2621.1995.tb09810.x
  34. Rapeanu G, Loey AV, Smout C, Hendrickx M. Biochemical characterization and process stability of polyphenoloxidase extracted from Victoria grape (Vitis vinifera spp. Sativa). Foood Chem. 94: 253-261 (2006) https://doi.org/10.1016/j.foodchem.2004.10.058