Effects of cryostabilizers, low temperature, and freezing on the kinetics of the pectin methylesterase-catalyzed de-esterification of pectin

Journal of Agricultural and Food Chemistry

Volumn 53, Issue 6, 2005, Pages 2282-2288

  Terefe, Netsanet Shiferaw ^a   Delele, Mulugeta Admasu ^a   Van Loey, Ann ^a   Hendrickx, Marc ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Diffusion controlled; Glass transition; Macroviscosity; Microviscosity; Pectin methylesterase

Indexed keywords

CARBOXYMETHYLCELLULOSE; FRUCTOSE; MALTODEXTRIN; PECTIN; PECTINESTERASE; SUCROSE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DEESTERIFICATION; DIFFUSION; ENZYME CONFORMATION; ENZYME KINETICS; ESTERIFICATION; FREEZING; GLASS TRANSITION TEMPERATURE; LOW TEMPERATURE; NONHUMAN; VISCOSITY;

CARBOXYLIC ESTER HYDROLASES; CARBOXYMETHYLCELLULOSE; COLD; CRYOPROTECTIVE AGENTS; ESTERIFICATION; FREEZING; FRUCTOSE; KINETICS; PECTINS; POLYSACCHARIDES; SUCROSE; VISCOSITY;

EID: 15444370451     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf048813k     Document Type: Article

References (53)

1. Rombouts, F. M.; Versteeg, C.; Karman, A. H.; Pilnik, W. Pectinesterases in component parts of citrus fruits related to problems of cloud loss and gelation in citrus products. In Use of Enzymes in Food Technology. Proceedings of International Symposium; Dupuy, P., Ed.; Versailles, France, 1982; pp 483-487.
2. Baker, R. A.; Cameron, R. G. Clouds of Citrus Juices and Juice Drinks. Food Technol. 1999, 53 (1), 64-69.
3. Giovane, A.; Quagliuolo, L.; Castaldo, D.; Servillo, L.; Balestrieri, C. Pectin methylesterase from Actinidia Chinensis fruits. Photochemistry 1990, 29 (9), 2821-2823.
4. Javeri, H.; Wicker, L. Partial purification and characterization of peach pectinesterase. J. Food Biochem. 1991, 15, 241-252.
5. Pressey, R.; Avants, J. K. Solubilization of cell walls by tomato polygalacturonases: Effect of pectinesterases. J. Food Biochem. 1982, 6, 57-74
6. MacDonald, G. A.; Lanier, T. Carbohydrates as cryoprotectorants for meats and surimi. Food Technol. 1991, 45, 150-159.
7. Slade, L.; Levine, H. Beyond Water Activity: Recent Advances Based on an Alternative Approach to the Assessment of Food Quality and Safety. Crit. Rev. Food Sci. Nutr. 1991, 30 (2, 3).
8. Cleland, W. W. What limits the rate of an enzyme-catalyzed reaction? Acc. Chem. Res. 1975, 8 (5), 145-151.
9. Fennema, O. R. Activity of enzymes in partially aqueous systems. In Water Relations of Foods; Duckworth, R. B., Ed.; Academic Press: London, 1975; pp 397-413.
10. Silver, M.; Karel, M. The behavior of invertase in model systems at low moisture contents. Food Biochem. 1981, 5, 283-311.
11. g′ of polymers in frozen model systems. In Water Relationships in Food; Levine, H., Slade, L., Eds.; Plenum Press: New York, 1991; pp 103-122.
12. Kerr, W. L.; Lim, M. H.; Reid, D. S.; Chen, H. Chemical reaction kinetics in relation to glass transition temperatures in frozen food polymer solutions. J. Sci. Food Agric. 1993, 61, 51-56.
13. Manzocco, L.; Nicoli, M. C.; Anese, M.; Pitotti, A.; Maltini, E. Polyphenoloxidase activity in partially frozen systems with different physical properties. Food Res. Int. 1999, 31 (5), 363-370.
14. Terefe, N. S.; Hendrickx, M. Kinetics of the pectin methylesterase catalyzed de-esterification of pectin in frozen model systems. Biotechnol. Prog. 2002, 18, 1249-1256.
15. Terefe, N. S.; Mokewena, K. K.; Van Loey, A.; Hendrickx, M. Kinetics of the alkaline phosphatase catalyzed hydrolysis of disodium p-nitrophenyl phosphate in frozen model systems. Biotechnol. Prog. 2002, 18, 1249-1256.
16. Champion, D.; Blond, G.; Simatos, D. Reaction rates at subzero-temperatures in frozen sucrose solutions: A diffusion controlled reaction. Cryo-Lett. 1997, 18, 251-260.
17. Terefe, N. S.; Nhan, M. T.; Vallejo, D.; Van Loey, A.; Hendrickx, M. Modeling the kinetics of the pectin methylesterase catalyzed de-esterification of pectin in frozen systems. Biotechnol. Prog. 2004, 20, 480-490.
18. Terefe, N. S. Glass transition and kinetics of enzyme catalyzed reactions in frozen systems: Implication to frozen storage stability of foods. Ph.D. Dissertation, Katholieke Universiteit Leuven, 2004; 180 pp, available from the Laboratory of Food Technology, Faculty of Agriculture and Applied Biological Sciences, Kastelpark Arenberg 22, 3001 Leuven, Belgium.
19. Fachin, D. Temperature and pressure inactivation of tomato pectinases: a kinetic study. Ph.D. Dissertation, Katholieke Universiteit Leuven, 2004; 133 pp, available from the Laboratory of Food Technology, Faculty of Agriculture and Applied Biological Sciences, Kastelpark Arenberg 22, 3001 Leuven, Belgium.
20. Klavons, J. A.; Bennett, R. D. Determination of methanol using alcohol oxidase and its application to methyl ester content of pectins. J. Agric. Food Chem. 1986, 34, 597-599.
21. Marangoni, A. G. Enzyme Kinetics a modern approach; Wiley-Interscience: Hoboken, NJ, 2003; p 229.
22. Berg, O. G.; Von Hippel, P. H. Diffusion-controlled macromolecular interactions. Annu. Rev. Biophys. Chem. 1985, 14, 131-160.
23. Atkins, P. W. Physical Chemistry; Oxford University Press: Oxford, 1995; pp 934-938.
24. Brouwer, A. C.; Kirsch, J. F. Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation. Biochemistry 1982, 21, 1302-1307.
25. Blacklow, S. C.; Raines, R. T.; Lim, W. A.; Zamore, P. D.; Knowles, J. R. Triosephosphate isomerase catalysis is diffusion controlled. Biochemistry 1988, 27, 1158-1167.
26. Cole, P. A.; Burn, P.; Takacs, B.; Walsh, C. T. Evaluation of the catalytic mechanism of recombinant human Csk (C-terminal Src kinase) using nucleotide analogs and viscosity effects. J. Biol. Chem. 1994, 269 (49), 30880-30887.
27. Simpoulos, T.; Jencks, W. Alkaline phosphatase is an almost perfect enzyme. Biochemistry 1994, 33, 10375-10380.
28. Huang, T.-M.; Hung, H.-C.; Chang, T.-C.; Chang, G.-G. Solvent kinetic isotope effects of human placental alkaline phosphatase in reverse micelles. Biochem. J. 1998, 330, 267-275.
29. Qi, X.; Virden, R. Efficient catalysis by β-lactamase from Staphylococcus aureus PCl accompanied by accumulation of an acyl-enzyme. Biochem. J. 1996, 315, 537-541.
30. Werner, D. S.; Lee, T. R.; Lawrence, D. S. Is protein kinase substrate efficacy a reliable barometer for successful inhibitor design? J. Biol. Chem. 1996, 277 (1), 180-185.
31. Nieslanik, B. S.; Dabrowski, M. J.; Lyon, R. P.; Atkins, W. M. Stopped-Flow kinetics analysis of the ligand-induced coil-helix transistion in glutathione S-transferase Al-1: Evidence for a persistent denatured state. Biochemistry 1999, 38 (21), 6971-6980.
32. Lee, J. C.; Timasheff, S. N. The stabilization of proteins by sucrose. J. Biol. Chem. 1981, 256 (14), 7193-7201.
33. Fink, A. L.; Geeves, M. A. Cryoenzymology: The study of enzyme catalysis at subzero temperatures. In Methods in Enzymology; Purich, D. L., Ed.; Academic Press: New York, 1979; Vol. 63, pp 336-370.
34. Rusakov, D. A.; Kullmann, D. M. Geometric and viscous components of the turtuosity of the extracellular space in the brain. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 8975-8980.
35. Phillies, G. D. J. The hydrodynamic scaling model for polymer self-diffusion. J. Phys. Chem. 1989, 93, 5029-5039.
36. Busch, N. A.; Kim, T.; Bloomfield, V. A. Tracer diffusion of proteins in DNA solutions. 2. Green fluorescent protein in crowded DNA solutions. Macromolecules 2000, 33, 5932-5937.
37. Verkman, A. S. Solute and macromolecular diffusion in cellular aqueous compartments. Trends Biochem. Sci. 2002, 27 (1), 27-32.
38. Alvarez-Lorenzo, C.; Gómez-Amoza, J. L.; Martínez-pacheco, R.; Souto, C.; Concheiro, A. Microviscosity of hydroxypropylcellulose gels as a basis for prediction of drug diffusion rates. Int. J. Pharm. 1999, 180, 91-103.
39. Johansson, L.; Elivingson, C.; Löfroth, J.-E. Diffusion and interaction in gels and solutions. 2. Experimental results on the obstruction effect. Macromolecules 1991, 24 (22), 6019-6023.
40. Muhr, A. H.; Blanshard, J. M. V. Diffusion in gels. Polymer 1982, 23, 1012-1026.
41. Masaro, L.; Zhu, X. X. Physical models of diffusion for polymer solutions, gels and solids. Prog. Polym. Sci. 1999, 24, 731-775.
42. Gao, P.; Fagerness, P. E. Diffusion in HPMC gels. I. Determination of drug and water diffusivity by pulsed-field-gradient spin-echo NMR. Pharm. Res. 1995, 12 (7), 955-964.
43. Grasdalen, P.; Anderson, A. K.; Larson, B. NMR spectroscopy studies of the action pattern of tomato pectinesterase: generation of block structure in pectin by a multiple- attack mechanism. Carbohydr. Res. 1996, 289, 105-114.
44. Catoire, L.; Pierron, M.; Morvan, C.; Hervé du Penhoat, Goldberg, R. Investigation of the action patterns of pectin-methylesterase isoforms through kinetic analyses and NMR spectroscopy: Implication in cell wall expansion. J. Biol. Chem. 1998, 273 (50), 33150-33156.
45. Denès, J. M.; Baron, A.; Renard, C.; Péan, C. Different action patterns for apple pectin methylesterase at pH 7.0 and 4.5. Carbohydr. Res. 2000, 327, 385-393.
46. Wang, G. M.; Haymet, D. J. Trehalose and other sugar solutions at low temperature: Modulated differential scanning calorimetry (MDSC). J. Phys. Chem. B 1998, 102, 5341-5347.
47. Magazù, S.; Villari, V.; Migliardo, P.; Maisano, G.; Telling, M. T. F. Diffusive dynamics of water in the presence of homologous disaccharides: A comparative study by quasi elastic neutron scattering. IV. J. Phys. Chem. B 2001, 105, 1851-1855.
48. Tromp, R. H.; Parker, R.; Ring, S. G. Water diffusion in glasses of carbohydrates. Carbohydr. Res. 1997, 303, 199-205.
49. Tappel, A. L. Effects of low temperature and freezing of enzymes and enzyme systems. In Cryobiology; Meryman, H. T., Ed.; Academic Press: New York, 1966; pp 163-177.
50. Brown, W.; Jhonson, R. M. Diffusion in polyacrylamide gels. Polymer 1980, 22, 185-189.
51. Hendrickx, M.; Abeele, C. V.; Engels, C.; Tobback, P. Diffusion of glucose in carrageenan gels. J. Food. Sci. 1986, 51 (6), 1544-1546.
52. Seksek, O.; Biwersi, J.; Verkaman, A. S. Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus. J. Cell Biol. 1997, 138 (1), 131-142.
53. Champion, D.; Blond, G.; Le Meste, M.; Simatos, D. Reaction rate modeling in cryoconcentrated solutions: Alkaline phosphatase catalyzed DNPP hydrolysis. J. Agric. Food Chem. 2000, 48, 4942-4947.