The effect of pulsed electric fields on the inactivation and structure of lysozyme

Food Chemistry

Volumn 110, Issue 2, 2008, Pages 334-343

  Zhao, Wei ^a   Yang, Ruijin ^a  

^a JIANGNAN UNIVERSITY   (China)

Author keywords

Lysozyme; Pulsed electric fields (PEF); Secondary structure; Tertiary structure

Indexed keywords

BUFFER; LYSOZYME; PHOSPHATE; TRYPTOPHAN;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; ELECTRIC CONDUCTIVITY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ENZYME STRUCTURE; FLUORESCENCE; PROTEIN SECONDARY STRUCTURE; PULSED ELECTRIC FIELD; STORAGE TEMPERATURE; ULTRAVIOLET SPECTROSCOPY;

EID: 41949138699     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2008.02.008     Document Type: Article

References (51)

1. Álvarez I., Pagán R., Condón S., and Raso J. The influence of process parameters for the inactivation of Listeria monocytogenes by pulsed electric fields. International Journal of Food Microbiology 87 (2003) 87-95
2. Ayhan Z., Yeom H.W., Zhang Q.H., and Min D.B. Flavor, color, and vitamin C retention of pulsed electric field processed orange juice in different packaging materials. Journal of Agricultural and Food Chemistry 49 (2001) 669-674
3. Back J.F., Oakenfull D., and Smith M.B. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18 (1979) 5191-5196
4. Barbosa-Canovas G.V., Pothakamury U.R., Palou E., and Swanson B.G. Nonthermal preservation of foods (1998), Marcel Dekker, New York
5. Barsotti L., and Cheftel J.C. Food processing by pulsed electric fields. II. Biological aspects. Food Review International 15 (1999) 181-213
6. Blake C.C.F., Mair G.A., North A.C.T., Phillips D.C., and Sarma V.R. On the conformation of the hen egg-white lysozyme molecule. Proceedings of the Royal Society of London. Series B 167 (1967) 365-377
7. Clérico E.M., Peisajovich S.G., Ceolín M., Ghiringhelli P.D., and Ermácora M.R. Engineering a compact non-native state of intestinal fatty acid-binding protein. Biochimica et Biophysica Acta 1476 (2000) 203-218
8. Cortés C., Esteve M.J., Frígola A., and Torregrosa F. Quality characteristics of horchata (a Spanish vegetable beverage) treated with pulsed electric fields during shelf-life. Food Chemistry 91 (2005) 319-325
9. Cowgill R.W. Fluorescence and protein structure. Biochimica et Biophysica Acta 140 (1967) 37-44
10. Davidson P.M. Chemical preservatives and natural antimicrobial compounds. In: Doyle M.P. (Ed). Food microbiology (2001), ASM Press, Washington, DC 601-602
11. Delben F., and Crescenzi V. Thermal denaturation of lysozyme. A differential scanning calorimetry investigation. Biochimica et Biophysica Acta 194 (1969) 615-618
12. Demchenko A.P. Ultraviolet spectroscopy of protein (1986), Springer-Verlag, Germany
13. Dutreux N., Notermans S., Wijtzes T., Góngora-Nieto M.M., Barbosa-Cánovasb G.V., and Swanson B.G. Pulsed electric fields inactivation of attached and free-living Escherichia coli and Listeria innocua under several conditions. International Journal of Food Microbiology 54 (2000) 91-98
14. Elez-Martínez P., and Martín-Belloso O. Effects of high intensity pulsed electric field processing conditions on vitamin C and antioxidant capacity of orange juice and gazpacho, a cold vegetable soup. Food Chemistry 102 1 (2007) 201-209
15. Fujita Y., and Noda Y. Effect of alkylation with different sized substituents on thermal stability of lysozyme. International Journal of Peptide and Protein Research 40 (1992) 103-109
16. Giner J., Ortega M., Mesegué M., Gimeno V., Barbosa-Cánovas G.V., and Martín O. Inactivation of peach polyphenoloxidase by exposure to pulsed electric fields. Journal of Food Science 67 4 (2002) 1467-1472
17. Granero G., Garnero C., and Longhi M. Second derivative spectrophotometric determination of trimethoprime and sulfamethoxazole in the presence of hydroxypropyl-β-cyclodextrin (HP-β-CD). Journal of Pharmaceutical and Biomedical Analysis 29 (2002) 51-59
18. Greenfield N., and Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8 (1969) 4108-4116
19. Hirai M., Arai S., and Iwase H. Concentration dependence of thermal structural transition of hen egg-white lysozyme under constant heating rate studied by time-resolved SAXS. Thermochimica Acta 344 (2000) 95-102
20. Ho S.Y., Mittal G.S., and Cross J.D. Effect of high field electric pulses on the activity of selected enzymes. Journal of Food Engineering 31 (1997) 69-84
21. Jeyamkondan S., Jayas D.S., and Holley R.A. Pulsed electric field processing of foods: A review. Journal of Food Protection 62 (1999) 1088-1096
22. Knorr D. Novel approaches in food-processing technology: New technologies for preserving foods and modifying function. Current Opinion in Biotechnology 10 (1992) 485-491
23. Korolczuk J., Keag J.R.M., Fernandez J.C., Baron F., Grosset N., and Jeantet R. Effect of pulsed electric field processing parameters on Salmonella enteritidis inactivation. Journal of Food Engineering 75 (2006) 11-20
24. Laberge M. Intrinsic protein electric fields: basic noncovalent interactions and relationship to protein-induced Stark effects. Biochimica et Biophysica Acta 138 (1998) 305-350
25. Lange R., and Balny C. UV-visible derivative spectroscopy under high pressure. Biochimica et Biophysica Acta 1595 (2002) 80-93
26. Lopes D.C.F., Delvivo F.M., and Silvestre M.P.C. Use of activated carbon for removing phenylalanine from reconstituted skim milk powder hydrolysates. LWT - Food Science and Technology 38 (2005) 447-453
27. Makki F., and Durance T.D. Thermal inactivation of lysozyme as influenced by pH, sucrose and sodium chloride and inactivation and preservative effect in beer. Food Research International 29 (1996) 635-645
28. Maňas P., Muňoz B., Sanz D., and Condón S. Inactivation of lysozyme by ultrasonic waves under pressure at different temperatures. Enzyme and Microbial Technology 39 (2006) 1177-1182
29. McHale J.L. Fermi resonance of tyrosine and related compounds. Analysis of the Raman doublet. Journal of Raman Spectroscopy 13 (1982) 21-24
30. Mertens B., and Knorr D. Developments of nonthermal processes for food preservation. Food Technology 46 (1992) 125-133
31. Musante L., Bruschi M., Candiano G., Petretto A., Dimasi N., Boccio P.D., et al. Characterization of oxidation end product of plasma albumin 'in vivo'. Biochemical and Biophysical Research Communications 349 (2006) 668-673
32. Padros E., Morros A., Manosa J., and Dunach M.A. The state of tyrosine and phenylalanine residues in proteins analyzed by fourth-derivative spectrophotometry. Histone H1 and ribonuclease A. European Journal of Biochemistry 127 (1982) 117-122
33. Parisia M., Mazzinia A., Sorbia R., Ramonic R., Grollic S., and Favillaa R. Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: Equilibrium studies at neutral pH. Biochimica et Biophysica Acta 1652 (2003) 115-125
34. Peng Z.G., Hidajat K., and Uddin M.S. Adsorption and desorption of lysozyme on nano-sized magnetic particles and its conformational changes. Colloids and Surfaces B: Biointerfaces 35 (2004) 169-174
35. Petersen S.B., Jonson V., Fojan P., Wimmer R., and Pedersen S. Sorbitol prevents the self-aggregation of unfolded lysozyme leading to an up to 13 °C stabilisation of the folded form. Journal of Biotechnology 114 (2004) 269-278
36. Qin B., Zhang Q., Barbosa-Canovas G., Swanson B., and Pedrow P. Pulsed electric field treatment chamber design for liquid food pasteurization using a finite element method. Transactions of the ASAE 38 2 (1995) 557-565
37. Ragone R., Colonna G., Balestrieri C., Servillo L., and Irace G. Determination of tyrosine exposure in proteins by second derivative spectroscopy. Biochemistry 23 (1984) 1871-1875
38. Sepulveda D.R., Guerrero J.A., and Barbosa-Cánovas G.V. Influence of electric current density on the bactericidal effectiveness of pulsed electric field treatments. Journal of Food Engineering 76 (2006) 656-663
39. Torreggiania A., Tambaa M., Mancob I., Rosaria M., Faraone-Mennellab, Ferreria C., et al. Radiation damage of lysozyme in a biomimetic model: Some insights by Raman spectroscopy. Journal of Molecular Structure 744-747 (2005) 767-773
40. Townend R., Kumosinski T.F., Timasheff S.N., Fasman G.D., and Davidson B. The circular dichroism of the beta structure of poly-l-lysine. Biochemical and Biophysical Research Communications 23 (1966) 63-69
41. Vega-Mercado H., Martín-Belloso O., Qin B., Chang F.J., Góngora-Nieto M.M., Barbosa-Cánovas G.V., et al. Non-thermal food preservation: Pulsed electric fields. Trends in Food Science & Technology 8 (1997) 151-157
42. Venyaminov S.Y., and Vassilenko K.S. Determination of protein tertiary structure class from circular dichroism spectra. Analytical Biochemistry 222 (1994) 176-184
43. Venyaminov S.Y., and Yang J.T. Determination of protein secondary structure. In: Fasman G.D. (Ed). Circular dichroism and the conformational analysis of biolecules (1996), Plenum Press, New York and London 69-107
44. Viseu M.I., Carvalho T.I., and Costa S.M.B. Conformational transitions in β-lactoglobulin induced by cationic amphiphiles: equilibrium studies. Biophysical Journal 86 (2004) 2392-2402
45. Yang R.J., Li S.Q., and Zhang Q.H. Effects of pulsed electric fields on the activity and structure of pepsin. Journal of Agricultural and Food Chemistry 52 (2004) 7400-7406
46. Yang R.J., Li S.Q., and Zhang Q.H. Effects of pulsed electric fields on the activity of enzymes in aqueous solution. Journal of Food Science 69 (2004) 241-248
47. Yeom H.W., Zhang Q.H., and Dunne C.P. Inactivation of papain by pulsed electric fields in a continuous system. Food Chemistry 67 (1999) 53-59
48. Yokota A., Izutani K., Takai M., Kubo Y., Noda Y., Koumoto Y., et al. The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: The role of each disulfide bridge. Journal of Molecular Structure 295 (2000) 1275-1288
49. Zakin M.R., and Herschbach D.R. Vibrational frequency shifts induced by molecular compression of pyridine in solution. Journal of Chemical Physics 85 (1986) 2376-2383
50. Zhong K., Hu X.S., Zhao G.H., Chen F., and Liao X.J. Inactivation and conformational change of horseradish peroxidise induced by pulsed electric field. Food Chemistry 92 (2005) 473-479
51. Zhong K., Wu J., Wang Z., Chen F., Liao X., Hu X., and Zhang Z. Inactivation kinetics and secondary structural change of PEF-treated POD and PPO. Food Chemistry 100 (2007) 115-123