High pressure application for food biopolymers

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 3, 2006, Pages 619-631

  Knorr, Dietrich ^a   Heinz, Volker ^a   Buckow, Roman ^a  

^a TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Enzyme; High pressure; Phase diagrams; Prion; Starch

Indexed keywords

AMYLASE; BIOPOLYMER; GLUCAN GLUCOSIDASE; PRION PROTEIN; STARCH;

CHEMICAL MODIFICATION; DENATURATION; ENZYME ACTIVITY; ENZYME MECHANISM; FOOD BIOTECHNOLOGY; FOOD PROCESSING; GELATINIZATION; HYDROSTATIC PRESSURE; PRIORITY JOURNAL; PROTEIN STABILITY; REVIEW; TEMPERATURE; THERMODYNAMICS;

ANIMALS; BIOPOLYMERS; ENZYMES; FOOD HANDLING; HYDROSTATIC PRESSURE; PRIONS; PROTEINS; STARCH; TEMPERATURE; THERMODYNAMICS;

EID: 33646014759     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.01.017     Document Type: Review

References (105)

1. Van Eldik R., Asano T., and Le Noble W.J. Activation and reaction volumes in solution. 2. Chem. Rev. 89 (1989) 549-688
2. Hei D.J., and Clark D.S. Pressure stabilization of proteins from extreme thermophiles. Appl. Environ. Microbiol. 60 (1994) 932-939
3. Boonyaratanakornkit B.B., Park C.B., and Clark D.S. Pressure effects on intra- and intermolecular interactions within proteins. Biochim. Biophys. Acta 1595 (2002) 235-249
4. Tauscher B. Pasteurization of food by hydrostatic high pressure: chemical aspects. Z. Lebensm.-Unters. Forsch. 200 (1995) 3-13
5. Eyring H. The activated complex and the absolute rate of chemical reactions. Chem. Rev. 17 (1935) 65-77
6. Cheftel J.C. Effects of high hydrostatic pressure on food constituents: an overview. In: Balny C., Hayashi R., Heremans K., and Masson P. (Eds). High Pressure and Biotechnology (1992), John Libbey Eurotext, Montrouge 195-209
7. Heremans K. High pressure effects on proteins and other biomolecules. Ann. Rev. Biophys. Bioeng. 11 (1982) 1-21
8. Balny C., and Masson P. Effects of high pressure on proteins. Food Rev. Int. 9 (1993) 611-628
9. Heremans R., and Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta 1386 (1998) 353-370
10. Zhang J., Peng X., Jonas A., and Jonas J. NMR study of the cold, heat, and pressure unfolding of ribonuclease A. Biochemistry 34 (1995) 8631-8641
11. Nash D.P., and Jonas J. Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates. Biochemistry 36 (1997) 14375-14383
12. Smeller L. Pressure-temperature phase diagram of biomolecules. Biochim. Biophys. Acta 1595 (2002) 11-29
13. Priev A., Almagor A., Yedgar S., and Gavish B. Glycerol decreases the volume and compressibility of protein interior. Biochemistry 35 (1996) 2061-2066
14. 1-ATPase complex against pressure inactivation. Biochim. Biophys. Acta 1546 (2001) 164-170
15. Buckow R., Heinz V., and Knorr D. Two fractional model for evaluating the activity of glucoamylase from Aspergillus niger under combined pressure and temperature conditions. Food Bioprod. Process. 83 (2005) 220-228
16. Kunugi S., and Tanaka N. Cold denaturation of proteins under high pressure. Biochim. Biophys. Acta 1595 (2002) 329-344
17. Northrop D.B. Effects of high pressure on enzyme activity. Biochim. Biophys. Acta 1595 (2002) 71-79
18. Jaenicke R. Enzymes under extremes of physical conditions. Ann. Rev. Biophys. Bioeng. 10 (1981) 1-67
19. Gross M., and Jaenicke R. Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. Eur. J. Biochem. 221 (1994) 617-630
20. Mozhaev V.V., Lange R., Kudryashova E.V., and Balny C. Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotechnol. Bioeng. 52 (1996) 320-331
21. Tsou C.-L. Location of the active sites of some enzymes in limited and flexible molecular regions. Trends Biochem. Sci. 11 (1986) 427-429
22. Zipp A., and Kauzmann W. Pressure denaturation of metmyoglobin. Biochemistry 12 (1973) 4217-4228
23. Weemaes C.A., De Cordt S.V., Ludikhuyze L.R., Van den Broeck I., Hendrickx M.E., and Tobback P. Influence of pH, benzoic acid, EDTA, and glutathione on the pressure and/or temperature inactivation kinetics of mushroom polyphenoloxidase. Biotechnol. Prog. 13 (1997) 25-32
24. Riahi E., and Ramaswamy H.S. High pressure inactivation kinetics of amylase in apple juice. J. Food Eng. 64 (2004) 151-160
25. Ludikhuyze L., De Cordt S., Weemaes C., Hendrickx M., and Tobback P. Kinetics for heat and pressure-temperature inactivation of Bacillus subtilis a-amylase. Food Biotechnol. 10 (1996) 105-129
26. Lullien-Pellerin V., and Balny C. High pressure as a tool to study some proteins properties: conformational modification, activity and oligomeric dissociation. Innov. Food Sci. Emerg. Technol. 3 (2002) 209-221
27. Morild E. The theory of pressure effects on enzymes. Adv. Prot. Chem. 34 (1981) 93-166
28. Ludikhuyze L., Van Loey A., Indrawati, Denys S., and Hendrickx M. Effects of high pressure on enzymes related to food quality. In: Hendrickx M., and Knorr D. (Eds). Ultra High Pressure Treatments of Food (2002), Kluwer Academic/Plenum Publisher, New York 115-166
29. Scharnagl C., Reif M., and Friedrich J. Stability of proteins: temperature, pressure and the role of the solvent. Biochim. Biophys. Acta 1749 (2005) 187-213
30. Nienhaus G.U. Physik der Proteine. Phys. J. 4 (2004) 37-43
31. Hawley S.A. Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10 (1971) 2436-2442
32. Brandts J.F., Oliveira R.J., and Westort C. Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry 9 (1970) 1038-1047
33. Lesch H., Stadlbauer H., Friedrich J., and Vanderkooi J.M. Stability diagram and unfolding of a modified cytochrome c: what happens in the transformation regime?. Biophys. J. 82 (2002)
34. Lassalle M.W., Yamada H., and Akasaka K. The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by 1H NMR. J. Mol. Biol. 298 (2000) 293-302
35. Yamaguchi A., Yamada T.H., and Akasaka K. Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR. J. Mol. Biol. 250 (1995) 689-694
36. Ly-Nguyen B., Van Loey A.M., Fachin D., Verlent I., Indrawati, and Hendrickx M. Partial purification, characterization, and thermal and high-pressure inactivation of pectin methylesterase from carrots (Daucus carrota L.). J. Agric. Food Chem. 50 (2002) 5437-5444
37. Indrawati, Van Loey A., Fachin D., Ly Nguyen B., Verlent I., and Hendrickx M. Overview: effect of high pressure on enzymes related to food quality-Kinetics as a basic for process engineering. High Press. Res. 22 (2002) 613-618
38. Rapeanu G., Van Loey A., Smout C., and Hendrickx M. Thermal and high-pressure inactivation kinetics of polyphenol oxidase in victoria grape must. J. Agric. Food Chem. 53 (2005) 2988-2994
39. Smeller L., and Heremans K. Some thermodynamic and kinetic consequences of the phase diagram of protein denaturation. In: Heremans K. (Ed). High Pressure Research in Bioscience and Biotechnology (1997), Leuven Univ. Press, Louvain 55-58
40. Kaya H., and Chan H.S. Towards a consistent modeling of protein thermodynamic and kinetic cooperativity: how applicable is the transition state picture to folding and unfolding?. J. Mol. Biol. 315 (2002) 899-909
41. Guiavarc'h Y., Segovia O., Hendrickx M., and Ann Van Loey A. Purification, characterization, thermal and high-pressure inactivation of a pectin methylesterase from white grapefruit (Citrus paradisi). Innov. Food Sci. Emerg. Technol. 6 (2005) 363-371
42. Ly-Nguyen B., Van Loey A.M., Smout C., Verlent I., Duvetter T., and Hendrickx M.E. Effect of mild-heat and high-pressure processing on banana pectin methylesterase: a kinetic study. J. Agric. Food Chem. 51 (2003) 7974-7979
43. Christensen T., Frandsen T.P., Kaarsholm N.C., Svensson B., and Sigurskjold B.W. Physicochemical characterisation of the two active site mutants Trp52-Phe and Asp55-Val of glucoamylase from Aspergillus niger. Biochim. Biophys. Acta 1601 (2002) 163-171
44. Gomes M.R.A., Clark R., and Ledward D.A. Effects of high pressure on amylases and starch in wheat and barley flours. Food Chem. 63 (1998) 363-372
45. Raabe E., and Knorr D. Kinetics of starch hydrolysis with Bacillus amyloliquefaciens-a-amylase under high hydrostatic pressure. Starch 48 (1996) 409-414
46. Tanaka N., Mitani D., and Kunugi S. Pressure-induced perturbation on the active site of beta-amylase monitored from the sulfhydryl reaction. Biochemistry 40 (2001) 5914-5920
47. Weemaes C., De Cordt S., Goossens K., Ludikhuyze L., Hendrickx M., Heremans K., and Tobback P. High pressure, thermal, and combined pressure-temperature stabilities of a-amylases from Bacillus species. Biotechnol. Bioeng. 50 (1996) 49-56
48. Ludikhuyze L., Van den Broeck I., Weemaes C., Herremans C., Van Impe J., Hendrickx M., and Tobback P. Kinetics for isobaric-isothermal inactivation of Bacillus subtilis a-amylase. Biotechnol. Prog. 13 (1997) 532-538
49. Heinz V., Buckow R., and Knorr D. Catalytic activity of b-amylase from barley in different pressure/temperature domains. Biotechnol. Prog. 21 (2005) 1632-1638
50. Buckow R., Heinz V., and Knorr D. Effect of high hydrostatic pressure-temperature combinations on the activity of b-glucanase from barley malt. J. Inst. Brew. 111 (2005) 282-289
51. Buckow R., Heinz V., and Knorr D. Acceleration of the beer mashing process by applying high hydrostatic pressure. In: Fito P., and Toldra F. (Eds). IntradFood-EFFoST Conference 2005 vol. 2 (2005), Elsevier, Valencia 1359-1362
52. Seyderhelm I., Boguslawski S., Michaelis G., and Knorr D. Pressure induced inactivation of selected food enzymes. J. Food Sci. 61 (1996) 308-310
53. Narziss L. b-glucan and filterability. Brauwelt Int. 5 (1993) 435-442
54. Yoshigi N., Okada Y., Maeba H., Sahara H., and Tamaki T. Construction of a plasmid used for the expression of a seven-mutant barley b-amylase with increased thermostability in Escherichia coli and properties of the sevenfold-mutant b-amylase. J. Biochem. 118 (1995) 562-567
55. Svensson B., Larsen K., and Gunnarsson A. Characterization of a glucoamylase G2 from Aspergillus niger. FEBS Biochem. 154 (1986) 497-502
56. Svensson B., Pedersen T.G., Svendsen I., Sakai T., and Ottesen M. Characterization of two forms of glucoamylase from Aspergillus niger. Carlsberg Res. Commun. 47 (1982) 55-69
57. Christensen T., Svensson B., and Sigurskjold B.W. Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry. Biochemistry 38 (1999) 6300-6310
58. Masson P., Bec N., Frement M.T., Nachon F., Balny C., Lockridge O., and Schopfer L.M. Rate-determining step of butyrylcholinesterase-catalyzed hydrolysis of benzoylcholine and benzoylthiocholine. Eur. J. Biochem. 271 (2004) 1980-1990
59. Dallet S., and Legoy M.-D. Hydrostatic pressure induces conformational and catalytic changes on two alcohol dehydrogenases but no oligomeric dissociation. Biochim. Biophys. Acta 1294 (1996) 15-24
60. Gekko K. Compressibility gives new insights into protein dynamics and enzyme function. Biochim. Biophys. Acta 1595 (2002) 382-386
61. Makimoto S., and Taniguchi Y. Pressure effects on substrate activation phenomena in the a-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate. Biochim. Biophys. Acta 954 (1988) 343-346
62. Matsumoto T., Makimoto S., and Taniguchi Y. Effect of pressure on the mechanism of hydrolysis of maltotetraose, maltopentaose, and maltohexose catalyzed by porcine pancreatic a-amylase. Biochim. Biophys. Acta 1343 (1997) 243-250
63. Masson P., and Balny C. Linear and non-linear pressure dependence of enzyme catalytic parameters. Biochim. Biophys. Acta 1724 (2005) 440-450
64. Kunugi S., Kitayaki M., Yanagi Y., Tanaka N., Lange R., and Balny C. The effect of high pressure on thermolysin. Eur. J. Biochem. 248 (1997) 567-574
65. Cohen F.E., and Prusiner S.B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67 (1998) 793-819
66. Prusiner S.B. Molecular biology of prion diseases. Science 252 (1991) 1515-1522
67. Baskakov I.V., Legname G., Baldwin M.A., Prusiner S.B., and Cohen F.E. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 277 (2002) 21140-21148
68. Bosque P.J., Ryou C., Telling G., Peretz D., Legname G., and DeArmond S.J. Prions in skeletal muscle. Proc Natl. Acad. Sci. 99 (2002) 3812-3817
69. Brown P., Meyer R., Cardone F., and Pocchiari M. Ultra-high-pressure inactivation of prion infectivity in processed meat: a practical method to prevent human infection. Proc. Natl. Acad. Sci. 100 (2003) 6093-6097
70. Brown P., Rau E.H., Johnson B.K., Bacote A.E., Gibbs C.J., and Gajdusek C. New studies on the heat resistance of hamster adapted scapie agent: threshold survival after ashing at 600 °C suggests an inorganic template of replication. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 3418-3421
71. ANA. Precautions in handling tissues, fluids, and other contaminated materials from patients with documented or suspected Creutzfeldt-Jacob disease. Ann. Neurol. 19 (1986) 75-77
72. Zhou J.-M., Zhu L., Balny C., and Perrett S. Pressure denaturation of the yeast prion protein Ure 2. Biochem. Biophys. Res. Commun. 287 (2001) 147-152
73. Alvarez-Martinez M.A., Torrent J., Lange R., Verdier J.-M., Balny C., and Liautard J.-P. Optimized overproduction, purification, characterization and high-pressure sensitivity of the prion protein in the native (PrPC-like) or amyloid (PrP(Sc)-like) conformation. Biochim. Biophys. Acta 1645 (2003) 228-240
74. Kuwata K., Li H., Yamada H., Legname G., Prusiner S.B., Akasaka K., and James T.L. Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc. Biochemistry 41 (2002) 12277-12283
75. Torrent J., Alvarez-Martinez M.T., Heitz F., Liautard J.P., Balny C., and Lange R. Alternative prion structural changes revealed by high pressue. Biochemistry 42 (2003) 1318-1325
76. Torrent J., Alvarez-Martinez M.T., Harricane M.C., Heitz F., Liautard J.P., Balny C., and Lange R. High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation. Biochemistry 43 (2004) 7162-7170
77. Garcia A.F., Heindl P., Voigt H., Büttner M., Wienhold D., Butz P., Stärke J., Tauscher B., and Pfaff E. Reduced proteinase K resistance and infectivity of prions after pressure treatment at 60 °C. J. Gen. Virol. 85 (2004) 261-264
78. Heindl P., Garcia A.F., Buttner M., Voigt H., Butz P., Tauscher B., and Pfaff E. Some physico-chemical parameters that influence proteinase K resistance and the infectivity of PrPSc after high pressure treatment. Braz. J. Med. Biol. Res. 38 (2005) 1223-1231
79. Garcia A.F., Heindl P., Voigt H., Buttner M., Butz P., Tauber N., Tauscher B., and Pfaff E. Dual nature of the infectious prion protein revealed by high pressure. J. Biol. Chem. 280 (2004) 9842-9847
80. sc in a targeted manner, Patent, WO 02/49460, (2002).
81. Casolari A. Heat resistance of prions and food processing. Food Microbiol. 15 (1998) 59-63
82. Appel T.R., Wolff M., von Rheinbaben F., Heinzel M., and Riesner D. Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures. J. Gen. Virol. 82 (2001) 465-473
83. DHSS. Health hazard note. Management of patients with spongiform encephalopathy (CJD). DHSS Circular DA 84 (1984)
84. Nishida N., Katamine S., and Manuelidis L. Reciprocal interference between specific CJD and scrapie agents in neural cell cultures. Science 310 (2005) 493-496
85. Chen H., Hoover D.G., and Kingsley D.H. Temperature and treatment time influence high hydrostatic pressure inactivation of feline calicivirus, a norovirus surrogate. J. Food Prot. 68 (2005) 2389-2394
86. Tian S.-M., Ruan K.-C., Qian J.-F., Shao G.-Q., and Balny C. Effects of hydrostatic pressure on the structure and biological activity of infectious bursal disease virus. Eur. J. Biochem. 267 (2000) 4486-4494
87. Kingsley D.H., Chen H., and Hoover D.G. Inactivation of selected picornaviruses by high hydrostatic pressure. Virus Res. 102 (2004) 221-224
88. Kingsley D.H., Hoover D.G., Papafragkou E., and Richards G.P. Inactivation of hepatitis A virus and a calicivirus by high hydrostatic pressure. J. Food Protect. 65 (2002) 1605-1609
89. Calci K.R., Meade G.K., Tezloff R.C., and Kingsley D.H. High-pressure inactivation of hepatitis A virus within oysters. Appl. Environ. Microbiol. 71 (2005) 339-343
90. Gallant D.J., Bouchet B., Buléon A., and Pérez S. Physical characteristics of starch granueles and susceptibility to enzymatic degradation. Eur. J. Clin. Nutr. 46 (1992) S3-S16
91. Zobel H.F. Starch crystal transformations and their industrial importance. Starch 40 (1988) 44-50
92. Oates C.G. Towards an understanding of starch granule structure and hydrolysis. Trends Food Sci. Technol. 8 (1997) 375-382
93. Parker R., and Ring S.G. Aspects of the physical chemistry of starch. J. Cereal Sci. 34 (2001) 1-17
94. Waigh T.A., Gidley M.J., Komanshek B.U., and Donald A.M. The phase transformations in starch during gelatinisation: a liquid crystalline approach. Carbohydr. Res. 328 (2000) 165-176
95. Waigh T.A., Hopkinson I., Donald A.M., Butler M.F., Heidelbach F., and Riekel C. Analysis of the native structure of starch granules with X-ray microfocus diffraction. Macromolecules 30 (1997) 3813-3820
96. Muhr A.H., Wetton R.E., and Blanshard J.M.V. Effect of hydrostatic pressure on starch gelatinisation, as determined by DTA. Carbohydr. Polym. 2 (1982) 91-102
97. Thevelein J.M., Van Assche J.A., Heremans K., and Gerlsma S.Y. Gelatinisation temperature of starch, as influenced by high pressure. Carbohydr. Res. 93 (1981) 304-307
98. Rubens P., and Heremans K. Pressure-temperature gelatinization phase diagram of starch: an in situ Fourier transform infrared study. Biopolymers 54 (2000) 524-530
99. Douzals J.P., Perrier-Cornet J.M., Coquille J.C., and Gervais P. Pressure-temperature phase diagram for wheat starch. J. Agric. Food Chem. 49 (2001) 873-876
100. Stolt M., Oinonen S., and Autio K. Effect of high pressure on the physical properties of barley starch. Innov. Food Sci. Emerg. Technol. 1 (2001) 167-175
101. Stute R., Kingler R.W., Boguslawski S., Eshtiaghi M.N., and Knorr D. Effects of high pressure treatment on starches. Starch 48 (1996) 399-408
102. Jacobs H., Mischenko N., Koch M.H.J., Eerlingen R.C., Delcour J.A., and Reynaers H. Evaluation of the impact of annealing on gelatinisation at intermediate water content of wheat and potato starches: a differential scanning calorimetry and small angle X-ray scattering study. Carbohydr. Res. 306 (1998) 1-10
103. Katopo H., Song Y., and Jane J. Effect and mechanism of ultrahigh hydrostatic pressure on the structure and properties of starches. Carbohydr. Polym. 47 (2001) 233-244
104. Bauer B.A., and Knorr D. The impact of pressure, temperature and treatment time on starches: pressure-induced starch gelatinisation as pressure time temperature indicator for high hydrostatic pressure processing. J. Food Eng. 68 (2005) 329-334
105. B.A. Rumpold, Impact of high hydrostatic pressure on wheat, tapioca, and potato starches, Doctoral thesis at Berlin Technical University, Department of Food Biotechnology and Food Process Engineering, Berlin (2005), p. 120.