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Original Articles

Functional Improvement of Milk Whey Proteins Induced by High Hydrostatic Pressure

Pages 351-363 | Published online: 18 Jan 2007

REFERENCES

  • Ahmed, J., and Ramaswamy, H. S., 2003. Effect of hydrostatic pressure and temperature on rheological characteristics of α -lactalbumin, Australian J. Dairy Technol. 58 (2003), pp. 233–237, [CSA].
  • Balny, C., and Masson, P., 1993. Effects of high pressure on proteins, Food Rev. Int 9 (1993), pp. 611–628, [CSA].
  • Belloque, J., López-Fandiño, R., and Smith, G. M., 2000. A 1H-NMR study on the effect of high pressures on β -lactoglobulin, J. Agric. Food Chem 48 (2000), pp. 3906–3912, [INFOTRIEVE][CROSSREF][CSA].
  • Bonomi, F., Fiocchi, A., Frøkiær, H., Gaiaschi, A., Iametti, S., Poiesi, C., Rasmussen, P., Restain, P., and Rovere, P., 2003. Reduction of immunoreactivity of bovine β -lactoglobulin upon combined physical and proteolytic treatment, J. Dairy Res 70 (2003), pp. 51–59, [INFOTRIEVE][CROSSREF][CSA].
  • Boonyaratanakornkit, B. B., Park, C. B., and Clark, D. S., 2002. Pressure effects on intra- and intermolecular interactions within proteins, Biochim. Biophys. Acta. 1595 (2002), pp. 235–249, [INFOTRIEVE][CSA].
  • Boye, J. I., Ma, C. -Y., Ismail, A., Harwalkar, V. R., and Kalab, M., 1997. Molecular and microstructural studies of thermal denaturation and gelation of β -lactoglobulins A and B, J. Agric. Food Chem 45 (1997), pp. 1608–1618, [CROSSREF][CSA].
  • Bristow, M., and Isaacs, N. S., 1999. The effect of high pressure on the formation of volatile products in a model Maillard reaction, J. Chem. Soc., Perkin Trans. 2 10 (1999), pp. 2213–2218, [CROSSREF][CSA].
  • Bull, L. A., and Schaschke, C. J., 2002. Interactive effects of pressure, temperature and time on the molecular structure of ovalbumin, lysozyme and β -lactoglobulin, High Pressure Res 22 (2002), pp. 689–691, [CROSSREF][CSA].
  • Cuoghi, F., 1993. [Use of high pressure in the food industry; “cold sterilization” of milk and influence on its properties], Industrie Alimentari 32 (1993), pp. 956–964, [CSA].
  • Cheftel, J. C., 1995. Review: high-pressure, microbial inactivation, and food preservation, Food Sci. Technol. Int 1 (1995), pp. 75–90, [CSA].
  • Cheftel, J. C., Lévy, J., and Dumay, E., 2000. Pressure-assisted freezing and thawing: principles and potential applications, Food Rev. Int 16 (2000), pp. 453–483, [CROSSREF][CSA].
  • Cheftel, J. C., Thiebaud, M., and Dumay, E., 2002. Pressure-assisted freezing and thawing of foods: a review of recent studies, High Pressure Res 22 (2002), pp. 601–611, [CROSSREF][CSA].
  • Dickinson, E., 1998. Stability and rheological implications of electrostatic milk protein-polysaccharide interactions, Trends Food Sci. Technol 9 (1998), pp. 347–354, [CROSSREF][CSA].
  • Dickinson, E., and Galazka, V. B., 1991. Emulsion stabilization by ionic and covalent complexes of β-lactoglobulin with polysaccharides, Food Hydrocolloids 5 (1991), pp. 281–296, [CSA].
  • Dickinson, E., and James, J. D., 1998. Rheology and flocculation of high-pressure-treated β-lactoglobulin-stabilized emulsions: comparison with thermal treatment, J. Agric. Food Chem. 46 (1998), pp. 2565–2571, [CROSSREF][CSA].
  • Dickinson, E., and James, J. D., 1999. Influence of competitive adsorption on flocculation and rheology of high-pressure-treated milk protein-stabilized emulsions, J. Agric. Food Chem 47 (1999), pp. 25–30, [INFOTRIEVE][CROSSREF][CSA].
  • Dickinson, E., and James, J. D., 2000. Influence of high-pressure treatment on β -lactoglobulin-pectin associations in emulsions and gels, Food Hydrocolloids 14 (2000), pp. 365–376, [CROSSREF][CSA].
  • Dickinson, E., and Pawlowsky, K., 1996. Effect of high-pressure treatment of protein on the rheology of flocculated emulsions containing protein and polysacchride, J. Agric. Food Chem 44 (1996), pp. 2992–3000, [CROSSREF][CSA].
  • Dufour, E., Hui Bon Hoa, G., and Haertlé, T., 1994. High pressure effects on β -lactoglobulin interactions studied by fluorescence, Biochim. Biophys. Acta 1206 (1994), pp. 166–172, [INFOTRIEVE][CSA].
  • Dufour, E., Hervé, G., and Haertlé, T., 1995. Hydrolysis of β -lactoglobulin by thermolysin and pepsin under high hydrostatic pressure, Biopolymers 35 (1995), pp. 475–483, [CROSSREF][CSA].
  • Dumay, E. M., Kalichevsky, M. T., and Cheftel, J. C., 1994. High-pressure unfolding and aggregation of β -lactoglobulin and the baroprotective effects of sucrose, J. Agric. Food Chem 42 (1994), pp. 1861–1868, [CROSSREF][CSA].
  • Dumay, E., Lambert, C., Funtenberger, S., and Cheftel, J. C., 1996. Effects of high pressure on the physico-chemical characteristics of dairy creams and model oil/water emulsions, Lebensm.-Wiss. u.-Technol 29 (1996), pp. 606–625, [CROSSREF][CSA].
  • Dumay, E. M., Kalichevsky, M. T., and Cheftel, J. C., 1998. Characteristics of pressure-induced gels of β -lactoglobulin at various times after pressure release, Lebensm.-Wiss. u.-Technol 31 (1998), pp. 10–19, [CROSSREF][CSA].
  • Dumay, E., Laligant, A., Zasypkin, D., and Cheftel, J. C., 1999. Pressure- and heat-induced gelation of mixed β -lactoglobulin/polysaccharide solutions: scanning electron microscopy of gels, Food Hydrocolloids 13 (1999), pp. 339–351, [CROSSREF][CSA].
  • Dumolin, M., and Hayashi, R., 1998. High pressure, a unique tool for food texturization, Food Sci. Technol. Int 4 (1998), pp. 99–113, [CSA].
  • Dumolin, M., Ozawa, S., and Hayashi, R., 1998. Textural properties of pressure-induced gels of food proteins obtained under different temperatures, including subzero, J. Food Sci 63 (1998), pp. 92–95, [CSA].
  • Dzwolak, W., Kato, M., Shimizu, A., and Taniguchi, Y., 1999. Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α -lactalbumin: the stabilizing role of the calcium ion, Biochim. Biophys. Acta 1433 (1999), pp. 45–55, [INFOTRIEVE][CSA].
  • Famelart, M. -H., Chapron, L., Piot, M., Brulé, G., and Durier, C., 1998. High pressure-induced gel formation of milk and whey concentrates, J. Food Eng 36 (1998), pp. 149–164, [CROSSREF][CSA].
  • Farkas, D. F., and Hoover, D. G., 2001. High pressure procesing, J. Food Sci. (2001), pp. 47–64, suppl[CSA].
  • Farr, D., 1990. High pressure technology in the food industry, Trends Food Sci. Technol 1 (1990), pp. 14–16, [CROSSREF][CSA].
  • Farrell, H. M., Jimenez-Flores, R., Bleck, G. T., Brown, E. M., Butler, J. E., Creamer, L. K., Hicks, C. L., Hollar, C. M., Ng-Kwai-Hang, K. F., and Swaisgood, H. E., 2004. Nomenclature of the proteins of cows' milk - Sixth revision, J. Dairy Sci. 87 (2004), pp. 1641–1674, [INFOTRIEVE][CSA].
  • Fertsch, B., Müller, M., and Hinrichs, J., 2003. Firmness of pressure-induced casein and whey protein gels modulated by holding time and rate of pressure release, Innovative Food Science and Emerging Technologies 4 (2003), pp. 143–150, [CROSSREF][CSA].
  • Funtenberger, S., Dumay, E. M., and Cheftel, J. C., 1995. Pressure-induced aggregation of β -lactoglobulin in pH 7.0 buffers, Lebensm.-Wis. u.-Technol 28 (1995), pp. 410–418, [CROSSREF][CSA].
  • Funtenberger, S., Dumay, E. M., and Cheftel, J. C., 1997. High pressure promotes β -lactoglobulin aggregation through SH/S-S interchange reactions, J. Agric Food Chem 45 (1997), pp. 912–921, [CROSSREF][CSA].
  • Galazka, V. B., Ledward, D. A, Dickinson, E., and Langley, K. R., 1995. High pressure effects on emulsifying behaviour of whey protein concentrate, J. Food Sci 60 (1995), pp. 1341–1343, [CSA].
  • Galazka, V. B., Dickinson, E., and Ledward, D. A., 1996a. Effect of high pressure on the emulsifying behaviour of β -lactoglobulin, Food Hydrocolloids 10 (1996a), pp. 213–219, [CSA].
  • Galazka, V. B., Summer, I. G., and Ledward, D. A., 1996b. Changes in protein-protein and protein-polysaccharide interactions induced by high pressure, Food Chem. 57 (1996b), pp. 393–398, [CROSSREF][CSA].
  • Galazka, V. B., Ledward, D. A, Summer, I. G., and Dickinson, E., 1997. Influence of high pressure on bovine serum albumin and its complex with dextran sulfate, J. Agric. Food Chem 45 (1997), pp. 3465–3471, [CROSSREF][CSA].
  • Galazka, V. B., Dickinson, E., and Ledward, D. A., 1999a. Emulsifying behaviour of 11S globulin Vicia faba in mixtures with sulphated polysaccharides: comparison of thermal and high-pressure treatments, Food Hydrocolloids 13 (1999a), pp. 425–435, [CROSSREF][CSA].
  • Galazka, V. B., Smith, D., Ledward, D. A., and Dickinson, E., 1999b. Complexes of bovine serum albumin with sulphated polysaccharides: effects of pH, ionic strength and high pressure treatment, Food Chem. 64 (1999b), pp. 303–310, [CROSSREF][CSA].
  • Galazka, V. B., Dickinson, E., and Ledward, D. A., 2000a. Emulsifying properties of ovalbumin in mixtures with sulphated polysaccharides: effects of pH, ionic strength, heat and pressure treatments, J. Sci. Food Agric. 80 (2000a), pp. 1219–1229, [CROSSREF][CSA].
  • Galazka, V. B., Dickinson, E., and Ledward, D. A., 2000b. Effect of high-pressure on surface behaviour of adsorbed films formed from mixtures of sulfated polysaccharides with various proteins, Innovative Food Science and Emerging Technologies 1 (2000b), pp. 177–185, [CROSSREF][CSA].
  • Galazka, V. B., Dickinson, E., and Ledward, D. A., 2000c. Influence of high-pressure processing on protein solutions and emulsions, Current Opinion in Colloid and Interface Science 5 (2000c), pp. 182–187, [CROSSREF][CSA].
  • Grinberg, V. Y., and Heartlé, T., 2000. Reducer driven baric denaturation and oligomerisation of whey proteins, J. Biochem 79 (2000), pp. 205–209, [CSA].
  • Gross, M., and Jaenicke, R., 1994. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes, Eur. J. Biochem 221 (1994), pp. 617–630, [INFOTRIEVE][CROSSREF][CSA].
  • Haertlé, T., and Chobert, J. M., 1999. Recent progress in processing of dairy proteins: a review, J. Food Chem 23 (1999), pp. 367–407, [CSA].
  • Hayakawa, I., Kajihara, J., Morikawa, K., Oda, M., and Fujio, Y., 1992. Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals, J. Food Sci 57 (1992), pp. 288–292, [CSA].
  • Hayakawa, I., Linko, Y. -Y., and Linko, P., 1996. Mechanism of high pressure denaturation of proteins, Lebensm.- Wiss. u-Technol 29 (1996), pp. 756–762, [CROSSREF][CSA].
  • Hayashi, R., Kawamura, Y., and Kunugi, S., 1987. Introduction of high pressure to food processing: preferential proteolysis of β-lactoglobulin in milk whey, J. Food Sci. 52 (1987), pp. 1107–1108, [CSA].
  • Heremans, K., 1995. "High pressure effects on biomolecules". In: Ledward, D. A., Earnshaw, R. G., Johnston, D. E., and Hasting, A. P. M., eds. High pressure processing of foods. Nottingham, UK: Nottingham University Press; 1995. pp. 81–98.
  • Heremans, K., and Smeller, L., 1998. Protein structure and dynamics at high pressure, Biochim. Biophys. Acta 1386 (1998), pp. 353–370, [INFOTRIEVE][CSA].
  • Hill, V. M., Ledward, D. A., and Ames, J. M., 1996. Influence of high hydrostatic pressure and pH on the rate of Maillard browning in a glucose-lysine system, J. Agric. Food Chem 44 (1996), pp. 594–598, [CSA].
  • Hill, V. M., Ames, J. M., Ledward, D. A., and Royle, L., 1998. "The use of capillary electrophoresis to investigate the effect of high hydrostatic pressure on the Maillard reaction". In: O'Brien, J., Nursten, H. E., Crabbe, M. J. C., and Ames, J. M., eds. The Maillard reaction in foods and medicine. Cambridge, UK: Royal Society of Chemistry; 1998. pp. 121–126.
  • Hill, V. M., Isaacs, N. S., Ledward, D. A., and Ames, J. M., 1999. Effect of high hydrostatic pressure on the volatile components of a glucose-lysine model system, J. Agric. Food Chem 47 (1999), pp. 3675–3681, [INFOTRIEVE][CSA].
  • Hinrichs, J., Rademacher, B., and Kessler, H. G., 1996. Reaction kinetics of pressure-induced denaturation of whey proteins, Milchwissenschaft 51 (1996), pp. 504–509, [CSA].
  • Hosseini-nia, T., Ismail, A. A., and Kubow, S., 1999. Pressure-induced conformational changes of β -lactoglobulin by variable-pressure Fourier Transform Infrared Spectroscopy, J. Agric. Food Chem 47 (1999), pp. 4537–4542, [INFOTRIEVE][CROSSREF][CSA].
  • Hosseini-nia, T., Ismail, A. A., and Kubow, S., 2002. Effect of high hydrostatic pressure on the secondary structures of BSA and Apo- and Holo-α-lactalbumin employing Fourier Transform Infrared Spectroscopy, J. Food Sci 67 (2002), pp. 1341–1347, [CSA].
  • Huffman, L. M., and Harper, W. J., 1999. Maximizing the value of milk through separation technologies, J. Dairy Sci 82 (1999), pp. 2238–2244, [INFOTRIEVE][CSA].
  • Iametti, S., Transidico, P., Bonomi, F., Vecchio, G., Pittia, P., Rovere, P., and Dall'Aglio, G., 1997. Molecular modifications of β-lactoglobulin upon exposure to high pressure, J. Agric. Food Chem. 45 (1997), pp. 23–29, [CROSSREF][CSA].
  • İbanoğlu, E., 2001. High pressure effect on foaming properties of β-lactoglobulin and dextran sulfate mixture, Nahrung/Food 45 (2001), pp. 342–346, [CROSSREF][CSA].
  • İbanoğlu, E., and Karata, S., 2001. High pressure effect on foaming behaviour of whey protein isolate, J. Food Eng. 47 (2001), pp. 31–36, [CROSSREF][CSA].
  • Ikeuchi, Y., Nakagawa, K., Endo, T., Suzuki, A., Hayashi, T., and Ito, T., 2001. Pressure-induced denaturation of monomer β -lactoglobulin is partially reversible: comparison of monomer form (highly acidic pH) with dimer form (neutral pH), J. Agric. Food Chem 49 (2001), pp. 4052–4059, [INFOTRIEVE][CROSSREF][CSA].
  • Ipsen, R., Olsen, K., Skibsted, L. H., and Qvist, K. B., 2002. Gelation of whey protein induced by high pressure, Michwissenschaft 67 (2002), pp. 650–653, [CSA].
  • Isaacs, N. S., and Coulson, M., 1996. Effect of pressure on processes modeling the Maillard reaction, J. Phys. Org. Chem 9 (1996), pp. 639–644, [CROSSREF][CSA].
  • Jegouic, M., Grinberg, V. Y., Guingant, A., and Hartlé, T., 1996. Thiol-induced oligomerisation of αlactalbumin at high pressure, J. Protein Chem 15 (1996), pp. 501–509, [INFOTRIEVE][CROSSREF][CSA].
  • Jegouic, M., Grinberg, V. Y., Guingant, A., and Hartlé, T., 1997. Baric oligomerization in αlactalbumin/β -lactoglobulin mixtures, J. Agric. Food Chem 45 (1997), pp. 19–22, [CROSSREF][CSA].
  • Jonas, J., 2002. High-resolution nuclear magnetic resonance studies of proteins, Biochim. Biophys. Acta. 1595 (2002), pp. 145–159, [INFOTRIEVE][CSA].
  • Kanno, C., Mu, T., Hagiwara, T., Ametani, M., and Azuma, N., 1998. Gel formation from industrial whey proteins under hydrostatic pressure: effect of hydrostatic pressure and protein concentration, J. Agric. Food Chem 46 (1998), pp. 417–424, [INFOTRIEVE][CROSSREF][CSA].
  • Keim, S., and Hinrichs, J., 2004. Influence of stabilizing bonds on the texture properties of high-pressure-induced whey protein gels, Int. Dairy J 14 (2004), pp. 355–363, [CROSSREF][CSA].
  • Kitamura, Y., and Itoh, T., 1987. Reaction volume of protonic ionization for buffering agents. Prediction of pressure dependence of pH and pOH, Journal of Solution Chemistry 16 (1987), pp. 715–725, [CROSSREF][CSA].
  • Knorr, D., 1993. Effects of high-hydrostatic-pressure processes on food safety and quality, Food Technol 47 (1993), pp. 156–161, [CSA].
  • Knorr, D., 2002. High pressure processesing for preservation, modification and transformation of foods, High Pressure Res 22 (2002), pp. 595–599, [CROSSREF][CSA].
  • Knorr, D., Schlueter, O., and Heinz, V., 1998. Impact of high hydrostatic pressure on phase transitions of foods, Food Technol 52 (1998), pp. 42–45, [CSA].
  • Knudsen, J. C., Otte, J., Olsen, K., and Skibsted, L. H., 2002. Effect of high hydrostatic pressure on the conformation of β -lactoglobulin A as assessed by proteolytic peptide profiling, Int. Dairy J 12 (2002), pp. 791–803, [CROSSREF][CSA].
  • Kolakowski, P., Dumay, E., and Cheftel, J. -C., 2001. Effects of high pressure and low temperature on β -lactoglobulin unfolding and aggregation, Food Hydrocolloids 15 (2001), pp. 215–232, [CROSSREF][CSA].
  • Kontopidis, G., Holt, C., and Sawyer, L., 2004. β -lactoglobulin: binding properties, structure, and function., J. Dairy Sci. 87 (2004), pp. 785–796, [INFOTRIEVE][CSA].
  • Kudryashova, E. V., Mozhaev, V. V., and Balny, C., 1998. Catalytic activity of thermolysin under extremes of pressure and temperature: modulation by metal ions, Biochim. Biophys. Acta 1386 (1998), pp. 199–210, [INFOTRIEVE][CSA].
  • Kunugi, S., Kitayaki, M., Yanagi, Y., Tanaka, N., Lange, R., and Balny, C., 1997. The effect of high pressure on themolysin, Eur. J. Biochem 248 (1997), pp. 567–574, [INFOTRIEVE][CROSSREF][CSA].
  • Kuwata, K., Li, H., Yamada, H., Batt, C. A., Goto, Y., and Akasaka, K., 2001. High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin, J. Mol. Biol 305 (2001), pp. 1073–1083, [INFOTRIEVE][CROSSREF][CSA].
  • Lauber, S., Noack, I., Klostermeyer, H., and Henle, T., 2001a. Stability of microbial transglutaminase to high pressure treatment, Eur. Food Res. Technol. 213 (2001a), pp. 273–276, [CROSSREF][CSA].
  • Lauber, S., Noack, I., Klostermeyer, H., and Henle, T., 2001b. Oligomerization of β-lactoglobulin by microbial transglutaminase during high pressure treatment, Eur. Food Res. Technol. 213 (2001b), pp. 246–247, [CROSSREF][CSA].
  • Lauber, S., Krause, I., Klostermeyer, H., and Henle, T., 2003. Microbial transglutaminase crosslinks β -casein and β -lactoglobulin to heterologous oligomers under high pressure, Eur. Food Res. Technol 216 (2003), pp. 15–17, [CSA].
  • Lillford, P. J., and Howker, R., 2000. And what would you like for lunch Dr. Frankesnstein? The food supply chain: past history and future visions, J. Sci. Food Agric 80 (2000), pp. 2165–2168, [CROSSREF][CSA].
  • Lullien-Pellerin, V., and Balny, C., 2002. High pressure as a tool to study some proteins' properties: conformational modification, activity and oligomeric dissociation, Innovative Food Science and Emerging Technologies 3 (2002), pp. 209–221, [CROSSREF][CSA].
  • Matser, A. M., Krebbers, B., van den Berg, R. W., and Bartels, P. V., 2004. Advantages of high pressure sterilisation on quality of food products, Trends Food Sci. Technol 15 (2004), pp. 79–85, [CROSSREF][CSA].
  • Maynard, F., Weingand, A., Hau, J., and Jost, R., 1998. Effect of high-pressure treatment on the tryptic hydrolysis of bovine β -lactoglobulin AB, Int. Dairy J 8 (1998), pp. 125–133, [CROSSREF][CSA].
  • Mermerlstein, N. H., 1998. High pressure processing begins, Food Technol 52 (1998), pp. 104–106, [CSA].
  • Messens, W., Van Camp, J., and Huyghebaert, A., 1997. The use of high pressure to modify the functionality of food proteins, Trends Food Sci. Technol 8 (1997), pp. 107–112, [CROSSREF][CSA].
  • Meyer, R. S., Cooper, K. L., Knorr, D., and Lelieveld, H. L. M., 2000. High-pressure sterilization of foods, Food Technol 54 (2000), pp. 67–72, [CSA].
  • Michel, M., Leser, M. E., Syrbe, A., Clerc, M., Bauwens, F. I., Bovetto, L., von Schack, M. L., and Watzke, H. J., 2001. Pressure effects on whey protein-pectin mixtures, Lebensm. -Wiss. u-Technol 34 (2001), pp. 41–52, [CROSSREF][CSA].
  • Moller, R. E., Stapelfeldt, H., and Skibsted, L. H., 1998. Thiol reactivity in pressure-unfolded β -lactoglobulin. Antioxidative properties and thermal refolding, J. Agric. Food Chem 46 (1998), pp. 425–430, [INFOTRIEVE][CROSSREF][CSA].
  • Moreno, F. J., Molina, E., Olano, A., and López-Fandiño, R., 2003. High pressure effects on Maillard reaction between glucose and lysine, J. Agric. Food Chem. 51 (2003), pp. 394–400, [INFOTRIEVE][CROSSREF][CSA].
  • Mozhaev, V. V., Lange, R., Kudrashova, E. V., and Balny, C., 1996. Application of high hydrostatic pressure for increasing activity and stability of enzymes, Biotechnol. Bioeng 52 (1996), pp. 320–331, [CROSSREF][CSA].
  • Nakamura, K., Hatano, S., Matsuoka, A., Furukawa, N., Takahashi, T., and Yamanaka, Y., 2001. Optimum condition of high pressure treatment for the preparation of lysozyme-dextran complex found by random-centroid optimization, Food Sci. Technol. Res 7 (2001), pp. 81–87, [CSA].
  • Nakamura, T., Sado, H., and Syukunobe, Y., 1993. Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and denaturation with high pressure, Milchwissenschaft 48 (1993), pp. 141–145, [CSA].
  • Okamoto, M., Hayashi, R., Enomoto, A., Kaminogawa, S., and Yamauchi, K., 1991. High pressure proteolytic digestion of food proteins: selective elimination of β -lactoglobulin in bovine milk whey concentrate, Agric. Biol. Chem 55 (1991), pp. 1253–1257, [CSA].
  • Olsen, K., Ipsen, R., Otte, J., and Skibsted, L. H., 1999. Effect of high pressure on aggregation and thermal gelation of β -lactoglobulin, Milchwissenschaft 54 (1999), pp. 543–546, [CSA].
  • Olsen, K., Kristiansen, K. R., and Skibsted, L. H., 2003. Effect of high hydrostatic pressure on the steady-state kinetics of tryptic hydrolysis of β -lactoglobulin, Food Chem 80 (2003), pp. 255–260, [CROSSREF][CSA].
  • Otte, J., Zakora, M., Qvist, K. B., Olsen, C. E., and Barkholt, V., 1997. Hydrolysis of bovine β -lactoglobulin by various proteases and identification of selected peptides, Int. Dairy J 7 (1997), pp. 835–848, [CROSSREF][CSA].
  • Panick, G., Malessa, R., and Winter, R., 1999. Differences between the pressure- and temperature-induced denaturation and aggregation of β -lactoglobulin A, B and AB monitored by FTIR spectroscopy and small-angle X-ray scattering, Biochemistry 38 (1999), pp. 6512–6519, [INFOTRIEVE][CROSSREF][CSA].
  • Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C.T., Findlay, J. B.C., Sivaprasadarao, R., Jones, T. A., Newcomer, M. E., and Kraulis, P. J., 1986. The structure of β -lactoglobulin and its similarity to plasma retinol-binding protein, Nature (London) 324 (1986), pp. 383–385, [CROSSREF][CSA].
  • Pittia, P., Wilde, P. J., Husband, F. A., and Clark, D. C., 1996. Functional and structural properties of β -lactoglobulin as affected by high pressure treatment, J. Food Sci. 61 (1996), pp. 1123–1128, [CSA].
  • Qi, P. X., Brown, E. M., and Farrell, H. M., 2001. “New views” on structure-function relationships in milk proteins, Trends Food Sci. Technol. 12 (2001), pp. 339–346, [CROSSREF][CSA].
  • San Martín, M. F., Barbosa-Cánovas, G. V., and Swanson, B. G., 2002. Food processing by high hydrostatic pressure, Crit. Rev. Food Sci. Nutr 42 (2002), pp. 627–645, [CSA].
  • Sizer, C. E., Balasubramaniam, V. M., and Ting, E., 2002. Validating high-pressure processes for low-acid foods, Food Technol 56 (2002), pp. 36–41, [CSA].
  • Smelt, J. P. P. M., 1998. Recent advances in the microbiology of high pressure processing, Trends Food Sci. Technol. 9 (1998), pp. 152–158, [CROSSREF][CSA].
  • Stapelfeldt, H., and Skibsted, L. H., 1999. Pressure denaturation and aggregation of β -lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing, J. Dairy Res 66 (1999), pp. 545–558, [INFOTRIEVE][CROSSREF][CSA].
  • Stapelfeldt, H., Petersen, P. H., Kristiansen, K. R., Qvist, K. B., and Skibsted, L. H., 1996. Effect of high hydrostatic pressure on the enzymic hydrolysis of β -lactoglobulin B by trypsin, thermolysin and pepsin, J. Dairy Res 63 (1996), pp. 111–118, [INFOTRIEVE][CSA].
  • Stapelfeldt, H., Olsen, C. E., and Skibsted, L. H., 1999. Spectrofluorometric characterization of β –lactoglobulin B covalently labeled with 2-(4′-maleimidylanilino)naphthalene-6-sulfonate, J. Agric. Food Chem 47 (1999), pp. 3986–3990, [INFOTRIEVE][CROSSREF][CSA].
  • Tamaoka, T., Itoh, N., and Hayashi, R., 1991. High pressure effect on Maillard reaction, Agric. Biol. Chem 55 (1991), pp. 2071–2074, [CSA].
  • Tanaka, N., and Kunugi, S., 1996. Effect of pressure on the denaturation exchange reaction of α -lactalbumin and β -lactoglobulin, Int. J. Biol. Macromol 18 (1996), pp. 33–39, [INFOTRIEVE][CROSSREF][CSA].
  • Tanaka, N., Koyasu, A., Kobayashi, I., and Kunugi, S., 1996a. Pressure-induced change in proteins studied through chemical modifications, Int. J. Biol. Macromol. 18 (1996a), pp. 275–280, [INFOTRIEVE][CROSSREF][CSA].
  • Tanaka, N., Nakajima, K., and Kunugi, S., 1996b. The pressure-induced structural change of bovine α -lactabumin as studied by fluorescence hydrophobic probe, Int. J. Peptide Protein Res. 48 (1996b), pp. 259–264, [CSA].
  • Tanaka, N., Tsurui, Y., Kobayashi, I., and Kunugi, S., 1996c. Modification of the single unpaired sulfhydryl group of β -lactoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation, Int. J. Biol. Macromol. 19 (1996c), pp. 63–68, [INFOTRIEVE][CROSSREF][CSA].
  • Tauscher, B., 1995. Pasterurization of food by hydrostatic high pressure: chemical aspects, Z. Lebensm. Unters. Forsch 200 (1995), pp. 3–13, [INFOTRIEVE][CROSSREF][CSA].
  • Tedford, L. A., and Schaschke, C. J., 1999. Combined influence of high pressure and thermal processing on egg white and milk protein, Leatherhead Food RA Food Industry Journal 2 (1999), pp. 125–132, [CSA].
  • Tedford, L.-A., and Schaschke, C. J., 2000. Induced structural change to β -Lactoglobulin by combined temperature and pressure, Biochem Eng J 5 (2000), pp. 73–76, [CROSSREF][CSA].
  • Tedford, L. -A., Smith, D., and Schaschke, C. J., 1999a. High pressure processing effects on the molecular structure of ovalbumin, lysozyme and β -lactoglobulin, Food Res. Int. 32 (1999a), pp. 101–106, [CROSSREF][CSA].
  • Tedford, L. -A., Kelly, S. M., Price, N. C., and Schaschke, C. J., 1999b. Interactive effects of pressure, temperature and time on the molecular structure of β -lactoglobulin, J. Food Sci. 64 (1999b), pp. 396–399, [CSA].
  • Tewari, G., Jayas, D. S., and Holley, R. A., 1999. High pressure processing of foods: and overview, Sci. Aliments 19 (1999), pp. 619–661, [CSA].
  • Thakur, B. R., and Nelson, P. E., 1998. High-pressure processing and preservation of foods, Food Rev. Int 14 (1998), pp. 427–447, [CSA].
  • Van Camp, J., and Huyghebaert, A., 1995a. A comparative rheological study of heat and high pressure induced whey protein gels, Lebesnm.-Wiss. u.-Technol. 28 (1995a), pp. 111–117, [CSA].
  • Van Camp, J., and Huyghebaert, A., 1995b. High pressure-induced gel formation of whey protein and haemoglobin protein concentrate, Food Chem. 54 (1995b), pp. 357–364, [CROSSREF][CSA].
  • Van Camp, J., Feys, G., and Huyghebaert, A., 1996. High pressure-induced gel formation of haemoglobin and whey proteins at elevated temperatures, Lebesnm.-Wiss. u.-Technol 29 (1996), pp. 49–57, [CROSSREF][CSA].
  • Van Camp, J., Messens, W., Clément, J., and Huyghebaert, A., 1997. Influence of pH and sodium chloride on the high pressure-induced gel formation of a whey protein concentrate, Food Chem 60 (1997), pp. 417–424, [CROSSREF][CSA].
  • Van Hooydonk, A. C. M., de Koster, P. G., and Boerrigter, I. J., 1987. The renneting properties of heated milk, Neth. Milk Dairy J 41 (1987), pp. 3–18, [CSA].
  • Van Willige, R. W. G., and Fitzgerald, R. J., 1995. Tryptic and chymotryptic hydrolysis of βlactoglobulin A, B and AB at ambient and high pressure, Milchwissenschaft 50 (1995), pp. 183–186, [CSA].
  • Vélez-Ruiz, J. F., Swanson, B. G., and Barbosa-Cánovas, G. V., 1998. Flow and viscoelastic properties of concentrated milk treated by high hydrostatic pressure, Lebensm.-Wiss. u.-Technol. 31 (1998), pp. 182–195, [CROSSREF][CSA].
  • Walkenström, P., and Heremansson, A. -M., 1996. Fine-stranded mixed gels of whey proteins and gelatin, Food Hydrocolloids 10 (1996), pp. 51–62, [CSA].
  • Walkenström, P., and Heremansson, A. -M., 1997a. High-pressure treated mixed gels of gelatin and whey proteins, Food Hydrocolloids 11 (1997a), pp. 195–208, [CSA].
  • Walkenström, P., and Heremansson, A. -M., 1997b. Mixed gels of gelatin and whey proteins formed by combining temperature and high pressure, Food Hydrocolloids 11 (1997b), pp. 457–470, [CSA].
  • Wong, D. W. S., Camirand, W. M., and Pavlath, A. E., 1996. Structures and functionalities of milk proteins, Crit. Rev. Food Sci. Nutr 36 (1996), pp. 807–844, [INFOTRIEVE][CSA].
  • Wu, S. -Y., Pérez, M. D., Puyol, P., and Sawyer, L., 1999. β-Lg binds palmitate within its central cavity, J. Biol. Chem. 274 (1999), pp. 170–174, [INFOTRIEVE][CROSSREF][CSA].
  • Yang, J., Dunker, A. K., Powers, J. R., Clark, S., and Swanson, B. G., 2001. β -lactoglobulin molten globule state induced by high pressure, J. Agric. Food Chem 49 (2001), pp. 3236–3243, [INFOTRIEVE][CROSSREF][CSA].
  • Yang, J., Powers, J. R., Clark, S., Dunker, A. K., and Swanson, B. G., 2002. Hydrophobic probe binding of β -lactoglobulin in the native and molten globule state induced by high pressure as affected by pH, KIO3 and N-ethylmaleimide, J. Agric. Food Chem 50 (2002), pp. 5207–5214, [INFOTRIEVE][CROSSREF][CSA].
  • Yang, J., Powers, J. R., Clark, S., Dunker, A. K., and Swanson, B. G., 2003. Ligand and flavor binding functional properties of β -lactoglobulin in the molten globule state induced by high pressure, J. Food Sci 68 (2003), pp. 444–452, [CSA].
  • Method for accelerating cheese ripening. Patent number European Patent Aplication EP 0469857 A1. 1992.
  • Zasypkin, C. V., Dumay, E., and Cheftel, J. C., 1996. Pressure- and heat-induced gelation of mixed β -lactoglobulin-xantan solutions, Food Hydrocolloids 10 (1996), pp. 203–211, [CSA].

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