Reactivation of broccoli peroxidases: Structural changes of partially denatured isoenzymes

Journal of Agricultural and Food Chemistry

Volumn 55, Issue 3, 2007, Pages 1009-1018

  Thongsook, Tipawan ^a   Whitaker, John R ^b   Smith, Gary M ^b   Barrett, Diane M ^b  

^a NARESUAN UNIVERSITY   (Thailand)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Absorption spectroscopy; Broccoli; Circular dichroism; Horseradish; Peroxidase; Reactivation

Indexed keywords

ARMORACIA RUSTICANA; BOVINAE; BRASSICA OLERACEA VAR. ITALICA;

ENZYME ACTIVATOR; ISOENZYME; PEROXIDASE;

ARTICLE; BRASSICA; CHEMISTRY; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYMOLOGY; HEAT; METABOLISM; PROTEIN DENATURATION; SPECTROPHOTOMETRY;

BRASSICA; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME REACTIVATORS; HEAT; ISOENZYMES; PEROXIDASE; PROTEIN DENATURATION; SPECTROPHOTOMETRY;

EID: 34247859257     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf062242+     Document Type: Article

References (44)

1. Schwimmer, S. Regeneration of heat inactivated peroxidase. J. Biol. Chem. 1944, 154, 487.
2. Lu, A. T.; Whitaker J. R. Some factors affecting rates of heat inactivation and reactivation of horseradish peroxidase. J. Food Sci. 1974, 39, 1173-1178.
3. Adams, J. B. The inactivation and regeneration of peroxidase in relation to the high temperature-short time processing of vegetables. J. Food Technol. 1978, 13, 281-297.
4. Rodrigo, C.; Rodrigo, M.; Alvarruiz, A.; Frigola, A. Thermal inactivation at high temperatures and regeneration of green asparagus peroxidase. J. Food Prot. 1996, 59, 1065 - 1071.
5. Tamura, Y.; Morita Y. Thermal denaturation and regeneration of Japanese-radish peroxidase. J. Biochem. (Tokyo) 1975, 78, 561-571.
6. Rodrigo, C.; Rodrigo, M.; Alvarruiz, A.; Frigola, A. Inactivation and regeneration kinetics of horseradish peroxidase heated at high temperatures. J. Food Prot. 1997, 60, 961-966.
7. Joffe, F. M.; Ball, C. O. Kinetics and energetics of thermal inactivation and the regeneration rates of a peroxidase system. J. Food Sci. 1962, 27, 587-592.
8. Halpin, B.; Pressey, R.; Jen, J.; Mondy, N. Purification and characterization of peroxidase isoenzymes from green peas (Pimm sativum). J. Food Sci. 1989, 54, 644-649.
9. McLellan, K. M.; Robinson, D. S. Purification and heat-stability of Brussels-sprout peroxidase isoenzymes. Food Chem. 1987, 23, 305-319.
10. Thongsook, T.; Barrett, D. M. Heat inactivation and reactivation of broccoli peroxidase. J. Agrie. Food Chem. 2005, 53, 3215-3222.
11. Chattopadhyay, K.; Mazumdar, S. Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 2000, 39, 263-270.
12. Kamal, J. K. A.; Behere, D. V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 2002, 41, 9034-9042.
13. Thongsook, T.; Barrett, D. M. Purification and partial characterization of broccoli (Brassica oieracea var. italica) peroxidase. J. Agric. Food Chem. 2005, 53, 3206-3214.
14. Anthon, G. E.; Barrett, D. M. Kinetic parameters for the thermal inactivation of quality-related enzymes in carrots and potatoes. J. Agric. Food Chem. 2002, 50, 4119-4125.
15. Pina, D. G.; Shnyrova, A. V.; Gavilanes, F.; Rodriguez, A.; Leal, F.; Roig, M. G.; Sakharov, I. Y.; Zhadan, G. G.; Villar, E.; Shnyrov, V. L. Thermally induced conformational changes in horseradish peroxidase. Eur. J. Biochem. 2001, 268, 120-126.
16. Stryer, L. In Biochemistry, 3rd ed.; Stryer, L., Ed.; Freeman: New York, 1988; pp 32-34.
17. Saxena, V. P.; Wetlaufer, D. B. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 1970, 9, 5015-5023.
18. Pappa, H. S.; Cass, A. E. G. A step towards understanding the folding mechanism of horseradish peroxidase. Eur. J. Biochem. 1993, 212, 227-235.
19. 2O. Biochemistry 1996, 35, 5488-5494.
20. Dunford, H. B. Spectroscopy of horseradish peroxidase. I: Optical, resonance Raman, magnetic circular dichroism, X-ray absorption, and diffraction. In Heme Peroxidases; Dunford, H. B., Ed.; Wiley: New York, 1999; pp 135-174.
21. Shannon, L.; Kay, E.; Lew, J. Peroxidase isozymes from horseradish roots. I. Isolation and physical properties. J. Biol. Chem. 1966, 241, 2166-2172.
22. Van Huystee, R. B.; Xu, Y. J.; O'Donnell, J. P. Variation in Soret band absorption of peroxidase due to calcium. Plant Physiol. Biochem. 1992, 30, 293-297.
23. Tarns, J. W.; Welinder, K. G. Unfolding and refolding of Coprinus cinereus peroxidase at high pH, in urea, and at high temperature. Effect of organic and ionic additives on these processes. Biochemistry 1996, 35, 7573-7579.
24. Tsaprailis, G.; Chan, D. W. S.; English A. M. Conformational states in dénaturants of cytochrome c and horseradish peroxidases examined by fluorescence and circular dichroism. Biochemistry 1998, 37, 2004-2016.
25. Gazaryan, I. G.; Doseeva, V. V.; Galkin, A. G.; Tishkov, V. I. Effect of single-point mutations Phe41 → His and Phe 143 → Glue on folding and catalytic properties of recombinant horseradish peroxidase expressed in E. coli. FEBS Lett. 1994, 14 [354(3)], 248-250.
26. Adams, P. A.; Berman, M. C. Kinetics and mechanism of the interaction between human-serum albumin and monomeric hemin. Biochem. J. 1980, 191, 95-102.
27. Chakraborti, A. S. Interaction of porphyrins with heme proteins-a brief review. Mol. Cell. Biochem. 2005, 253, 49-54.
28. Sutherland, G. R. J.; Aust, S. D. The effects of calcium on the thermal stability and activity of manganese peroxidase. Arch. Biochem. Biophys. 1996, 332, 128-134.
29. Haschke, R. H.; Friedhoff, J. M. Calcium-related properties of horseradish peroxidase. Biochem. Biophys. Res. Commun. 1978, 80, 1039-1042.
30. Peters, T., Jr. In All About Albumin: Biochemistry, Genetics, and Medical Applications; Peters Jr., T., Ed.; Academic Press: San Diego, CA, 1996; pp 9-54.
31. Dockal, M.; Carter, D. C.; Ruker, F. The three recombinant domains of human serum albumin - structural characterization and ligand binding properties. J. Biol. Chem. 1999, 274, 29303-29310.
32. Brown, J. R.; Shockley, P. Lipid - protein interaction. In Serum Albumin: Structure and Characterization of its Ligand Binding Sites; Jost, P.; Griffith, O. H., Eds.; Wiley: New York, 1982; Vol. 1, pp 25-68.
33. Honore, B. Conformational changes in human serum albumin induced by ligand binding. Pharmacol. Toxicol. 1990, 66 (Suppl. 2), 7-26.
34. Kragh-Hansen, U. Structure and ligand binding properties of human serum albumin (review). Dan. Med. Bull. 1990, 37, 57-84.
35. Peters, T. Serum-albumin. Adv. Protein. Chem. 1985, 37, 161-245.
36. Curry, S.; Brick, P.; Franks, N. P. Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochim. Biophys. Acta - Mol. Cell Biol. Lipids 1999, 1441, 131 - 140.
37. Ouameur, A. A.; Marty, R.; Tajmir-Riahi, H. A. Human serum albumin complexes with chlorophyll and chlorophyllin. Biopolymers 2005, 77, 129-136.
38. Papadopoulou, A.; Green, R. J.; Frazier, R. A. Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study. J. Agric. Food Chem. 2005, 53, 158-163.
39. Beaven, G. H.; Chen, S. H.; d'Albis, A.; Gratzer, W. B. A spectroscopic study of the haemin - human-serum-albumin system. Eur. J. Biochem. 1974, 41, 539-546.
40. Rotenberg, M.; Cohen, S.; Margalit, R. Thermodynamics of porphyrin binding to serum-albumin - effects of temperature, of porphyrin species and of albumin-carried fatty-acids. Photochem. Photobiol. 1987, 46, 689-693.
41. Morgan, W. T.; Liera, H. H.; Sutor, R. P.; Mullereberhard, U. Transfer of heme from heme-albumin to hemopexin. Biochim. Biophys. Acta 1976, 444, 435-445.
42. Grinberg, L. N.; O'Brien, P. J.; Hrkal, Z. The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin. Free Radical Biol. Med. 1999, 27, 214-219.
43. Naitoh, Y.; Taketani, S.; Tokunaga, R.; Sameshima, Y. Mechanisms involved in the cellular uptake of hematoporphyrin by rat hepatoma-cells. J. Biochem. 1988, 103, 973-978.
44. Smulevich, G.; Paoli, M.; DeSanctis, G.; Mantini, A. R.; Ascoli, F.; Coletta, M. Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH. Biochemistry 1997, 36, 640-649.