Thermal inactivation of pectin methylesterase, polygalacturonase, α-mannosidase, α-galactosidase and β-galactosidase activities in papaya (Carica papaya L. cv solo 8) pericarp

Paper Details

Research Paper 01/10/2016
Views (373) Download (9)
current_issue_feature_image
publication_file

Thermal inactivation of pectin methylesterase, polygalacturonase, α-mannosidase, α-galactosidase and β-galactosidase activities in papaya (Carica papaya L. cv solo 8) pericarp

Benjamin N’zué Yao, Hubert Kouassi Konan, Clément Yao Yué Bi, Kablan Tano
Int. J. Biosci.9( 4), 48-60, October 2016.
Certificate: IJB 2016 [Generate Certificate]

Abstract

The effect of heat treatment on papaya (Carica papaya cv solo 8) pericarp Pectin methylesterase (PME), Polygalacturonase (PG), α-mannosidase (α-MAN), α-galactosidase (α-GAL) and β-galactosidase (β-GAL) activities were studied over a range of 40 to 65 °C. Denaturation of these enzymes, measured by the loss in activity, could be described as a first-order reaction with k-values between 0.0011 and 0.0303 min-1. D- and k-values decreased and increased, respectively, with increasing temperature, indicating fast enzymatic inactivation at higher temperatures. Results suggested that PME, PG, α-MAN, α-GAL and β-GAL are the relatively thermostables enzymes with a Z-value of 34.84, 19.12, 31.54, 42.69 and 17.69 °C respectively and Ea value of 39.90, 105.93, 64.38, 47.28 and 91.46 kJ mol-1 respectively. The Gibbs free energy ΔG values range from 89.21 for α-GAL to 102.95 kJ/mol for α-MAN at 40-65 °C. The results of the thermodynamic investigations indicated that the hydrolytic reactions were: (1) not spontaneous (∆G > 0), (2) slightly endothermic (∆H > 0) and (3) reversible (∆S < 0). However, Positive values of entropy (ΔS > 0) for PG indicated that this enzyme is found in a chaotic state at the end of the reaction. The high value obtained for the variation in enthalpy indicated that a high amount of energy was required to initiate denaturation, probably due to the molecular conformation of these enzymes.

VIEWS 8

Adams JB. 1991. Enzyme inactivation during heat processing of foodstuffs. International Journal of Food Technology 26, 1-20. http://dx.doi.org/10.1111/j.1365-2621.1991.tb01136.x

Ali ZM, Ng SY, Othman R, Goh LY, Lazan H. 1998. Isolation, characterization and significance of papaya β-galactanases to cell wall modification and fruits of tening during ripening. Physiologia Plantarum 104, 105–115. http://dx.doi.org/10.1034/j.13993054.1998.1040114.x

Anema SG, McKenna AB. 1996. Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. Journal of Agricultural and Food Chemistry 44, 422-428. http://dx.doi.org/10.1021/jf950217q

Anthon GE, Barrett DM. 2002. Kinetic parameters for the thermal inactivation of quality related enzymes in carrots and potatoes. Journal of Agricultural and Food chemistry 50, 4119 – 4125. http://dx.doi.org/10.1021/jf011698i

Anthon GE, Sekine Y, Watanabe N, Barrett DM. 2002. Thermal Inactivation of Pectin Methylesterase, Polygalacturonase and Peroxidase in Tomato Juice. Journal of Agricultural and Food chemistry 50, 6153 – 6159. http://dx.doi.org/10.1021/jf020462r

Arrhenius S. 1889. Ubre die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Sauren. Zeitschrift fur Physik Chimie 4, 226-248.

Bédikou EM, Ahi AP, Koné FM, Gonnety JT, Faulet BM, Kouamé LP, Niamké SL. 2009. Biochemical properties of extracellular α–mannosidases from the digestive fluid of Rhynchophorus palmarum larvae. Bulletin of Insectology 62(1), 75-84.

Barrett NE, Gryison AS, Lewis MJ. 1999. Contribution of the lactoperoxidase system to the keeping quality of pasteurized milk. Journal of Dairy Research 66, 73-80.

Carey AT, Holt K, Picard S, Wilde R, Tucker GA, Bird CR, Schuch W, Seymour GB. 1995. Tomato exo-(1–4)-β-D-galactanase: isolation, changes during ripening in normal and tomato mutant fruit, and characterization of a related cDNA clone. Plant Physiology 108, 1099–1107.

Ditchfield C, Tadini CC, Machoshvili IA, Penna TCV. 2006. Polyphenol oxidase and peroxidase thermal inactivation kinetics used as indicators for the pasteurization of acidified banana puree (Musa cavendishii, Lamb.). Brazilian Journal of Chemical Engineering 9, 77-82.

Djioua T. 2010. Amélioration de la conservation des mangues 4ème gamme par application de traitements thermiques et utilisation d’une conservation sous atmosphère modifiée. PhD thesis, University of Avignon, France, 169. https://tel.archives-ouvertes.fr/tel-00544995

Dogan S, Arslan O, Ozen F. 2005. Polyphenol oxidase activity of oregano at different stages. Food Chemistry 91, 341-345. http://dx.doi.org/10.1016/j.foodchem.2004.06.017

Dogan M, Arslan O, Dogan S. 2002. Substrate specificity, heat inactivation and inhibition of polyphenol oxidase from different aubergine cultivars. International Journal of Food Science and Technology 37, 415-423. http://dx.doi.org/10.1046/j.1365-2621.2002.00580.x

Gnangui SN, Dué EA, Kouadio JPEN, Kouamé LP. 2009. Effect of heat treatment on edible yam (Dioscorea cayenensis-rotundata cv Longbô) polyphenol oxidase activity: kinetic and thermodynamic analysis. Journal of Animal & Plant Sciences 2, 128-137.

Gross KC. 1982. A rapid and sensitive method for assaying polygalacturonase using 2-cyanoacetamide. Horticultural Science 17, 933 – 934. http://agris.fao.org/aos/records/US825695.9

Guiavarc’h YP, Deli V, Van Loey AM, Hendrickx ME. 2002. Development of an enzymic time temperature integrator for sterilization processes based on Bacillus licheniformis α-amylase at reduced water content. Journal of Food Science 67, 285-291. http://dx.doi.org/10.1111/j.1365-2621.2002.tb11399.x

Hendrickx M, Ludikhuyze L, Van den Broeck I, Weemes C. 1998. Effects of high pressure on enzymes related to food quality. Trends in Food Science & Technology 9, 197-203. http://dx.doi.org/10.1016/S0924-2244(98)000399

Lazan H, Ng SY, Goh LY, Ali ZM. 2004. Papaya β-galactosidase/galactanase isoforms in differential cell wall hydrolysis and fruit softening during ripening. Plant Physiology and Biochemistry 42, 847–853. http://dx.doi.org/10.1016/j.plaphy.2004.10.007

Lazan H, Selamat MK, Ali ZM. 1995. β-Galactosidase, polygalacturonase and pectinesterase in differential softening and cell wall modification during papaya fruit ripening. Physiologia Plantarum 95, 106–112. http://dx.doi.org/10.1111/j.13993054.1995.tb00815.x

Lazan H, Ali ZM, Selamat MK. 1993. The underlying biochemistry of the effect of modified atmosphere and storage temperature on firmness decreased in papaya. Acta Horticulturae 343, 141–147. http://dx.doi.org/10.17660/ActaHortic.1993.343.31

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951. Protein measurement with the folin phenol reagent. Journal of Molecular Biology 193, 265-75.

Luh BS, Daouf HN. 1971. Effect of break temperature and holding time on pectin and pectic enzymes in tomato pulp. Journal of Food Science 36, 1030-1043. http://dx.doi.org/10.1111/j.1365-2621.1971.tb03341.x

Mehri-Kamoun R. 2001. Effet de la pectolyase Y-23 et de la cellulase RS sur le rendement en protoplasts viables de Prunus cerasus L. “Montmorency’’. Biotecnology, Agronomy, Society and Environment 5(2), 99 – 104.

Nath N, Rao AV, Gupta RG. 1983. Thermal resistance of pectin methylesterase in juice of pusa-ruby tomatoes. Indian Food Packer 37, 30–38. http://agris.fao.org/aos/records/US201302540205

Ohtani K, Misaki A. 1983. Purification and Characterization of β-D-Galactosidase and α-D-Mannosidase from Papaya (Carica papaya) Seeds. Agricultural and Biological Chemistry 47(ll), 2441-2451. http://dx.doi.org/10.1080/00021369.1983.10865977

Ozdes D, Gundogdu A, Kemer B, Duran C, Senturk HB, Soylak M. 2009. Removal of Pb(II) ions from aqueous solution by a waste mud from copper mine industry: equilibrium, kinetic and thermodynamic study. Journal of Hazardous Materials 166(2-3), 1480 – 1487. http://dx.doi.org/10.1016/j.jhazmat.2008.12.073

Rapeanu G, Van Loey A, Smout C, Hendrickx M. 2006. Thermal and high pressure inactivatio kinetics of Victoria grape polyphenol oxidase: from model systems to grape must. Journal of Food Process Engineering 29, 269-286. http://dx.doi.org/10.1111/j.1745-4530.2006.00063.x

Raviyan P, Zhang Z, Feng H. 2005. Ultrasonication for tomato pectineméthylestérase inactivation: Effect of cavitation intensity and temperature on inactivation. Journal of Food Engineering 70, 189 – 196. http://dx.doi.org/10.1016/j.jfoodeng.2004.09.028

Smith DL, Gross KC. 2000. A family of at least seven β-galactosidase genes is expressed during tomato fruit development. Plant Physiology 123, 1173–1183.

Soh CP. 2002. α- and β-galactosidases in papaya fruit softening during ripening. Ph.D. Thesis, University Kebangsaan Malaysia, Malaysia.

Terebiznik MR, Buera MP, Pilosof AMR. 1997. Thermal stability of dehydrated α-amylase in trehalose matrices in relation to its phase transitions. LWT-Food Science and Technology 30, 513-518. http://dx.doi.org/10.1006/fstl.1996.0210

Terefe NSM, Gamage M, Vilkhu K, Simons L, Mawson R, Versteeg C. 2009. The kinetics of inactivation of pectin methylesterase and polygalacturonase in tomato juice by thermosonication. Food Chemistry 117, 20 – 27. http://dx.doi.org/10.1016/j.foodchem.2009.03.067

Timasheff SN. 1993. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annual Reviews of Biophysics and Biomolecular Structure 22, 67-97. http://dx.doi.org/10.1146/annurev.bb.22.060193.000435

Trainotti L, Spinello R, Piovan A, Spolaore SP, Casadoro G. 2001. β-Galactosidases with a lectin-like domain are expressed in strawberry. Journal of Experimental Botany 52, 1635–1645.

Van Loey A; Verachtert B; Hendrickx M. 2001. Effect of high electric field pulses on enzymes. Trends in Food Science and Technology 12, 94-102. http://dx.doi.org/10.1016/S0924-2244(01)00066-8

Stumbo CR. 1973. Thermobacteriology in food processing. In: Food Processing: Principles and Applications, Academic press Edition, New York, USA, 67 – 168.

Versteeg C, Rombouts FM, Spaansen CH, Pilnik W. 1980. Thermostability and orange juice cloud stabilizing properties of multiple pectinesterases from orange. Journal of Food Science 45(4), 969-971. http://dx.doi.org/10.1111/j.13652621.1980.tb07489.x