Abstract
High-pressure modification of proteins involves changes in protein secondary, tertiary, and quaternary structures from the native state through intermediate states to the fully denatured state. High pressure changes protein structure primarily by rupturing or forming non-covalent bond-electronic interactions, hydrophobic interactions, and hydrogen bonds. High pressure also induces formation of new disulfide bonds stabilizing the denatured proteins or producing protein aggregation. Generally, high pressure decreases protein volume by compressing internal cavities and changing the solvation volume. However, the conditions for high pressure to denature or modify food proteins depend on the structure of individual proteins. Large numbers of disulfide bonds in a native protein helps that protein to withstand high-pressure denaturation. Temperature is a variable that along with pressure can be manipulated to either promote or retard protein denaturation. In addition to pressure intensity and holding time, the pH, ionic strength, and solvent conditions can greatly affect high-pressure modification of food proteins. Pressure-modified protein functional properties—solubility, gelation, emulsification, foaming, binding, coagulation, and water-holding capacity—can positively or negatively affect the organoleptic and nutritional quality of ingredients or food products. To improve food quality, modification of food proteins for desirable functional properties requires careful selection of pressure-treatment conditions or parameters (pressure intensity and holding time, temperature, pH, ionic strength, etc.). High pressure is a unique and approved tool to modify protein functional properties yet needs further exploration in areas of bioactive proteins and peptides and protein allergens.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Alvarez PA, Ramaswamy HS, Ismail AA (2008) High pressure gelation of soy proteins: effect of concentration, pH and additives. J Food Eng 88:331–340
Angsupanich K, Ledward DA (1998) High pressure treatment effects on cod (Gadus morhua) muscle. Food Chem 63:39–50
Anton M, Chapleau N, Beaumal V, Delepine S, de Lamballerie M (2001) Effect of high-pressure treatment on rheology of oil-in-water emulsions prepared with hen egg yolk. Innov Food Sci Emerg Technol 2:9–12
Aouzelleg A, Bull LA, Price NC, Kelly SM (2004) Molecular studies of pressure/temperature-induced structural changes in bovine β-lactoglobulin. J Sci Food Agric 84:398–404
Balny C, Masson P (1993) Effects of high pressure on proteins. Food Rev Int 9:611–628
Balny C, Mozhaev VV, Reinhard L (1997) Hydrostatic pressure and proteins: basic concepts and new data. Comp Biochem Physiol 116:299–304
Belloque J, Chicon R, López-Fandiňo R (2007) Unfolding and refolding of β-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperature and its influence on proteolysis. J Agric Food Chem 55:5282–5288
Belloque J, López-Fandiňo R, Smith G (2000) A 1H-NMR study on the effect of high pressures on β-lactoglobulin. J Agric Food Chem 48:3906–3912
Boonyaratanakornkit BB, Park CB, Clark DS (2002) Pressure effects on intra- and intermolecular interactions within proteins. Biochim Biophys Acta 1595:235–249
Bridgman PW (1914) The coagulation of albumin by pressure. J Biol Chem 19:511–512
Camp JV, Huyghebaert A (1995a) A comparative rheological study of heat and high pressure induced whey protein gels. Food Chem 4:357–364
Camp JV, Huyghebaert A (1995b) High pressure-induce gel formation of a whey protein and haemoglobin protein concentrate. LWT-Food Sci Technol 28:111–117
Camp JV, Huyghebaert A (1996) High pressure-induced gel formation of haemoglobin and whey proteins at elevated temperatures. LWT-Food Sci Technol 29:49–57
Cheftel JC, Culioli J (1997) Effects of high pressure on meat: a review. Meat Sci 3:211–236
Chicon R, Belloque J, Alonso E, López-Fandiňo R (2008a) Immunoreactivity and digestibility of high-pressure-treated whey proteins. Int Dairy J 18:367–376
Chicon R, Belloque J, Alonso E, Martin-Alvarez J, López-Fandiňo R (2008b) Hydrolysis under high hydrostatic pressure as means to reduce the binding of β-lactoglobulin to immunoglobulin E from human sera. J Food Prot 71:1453–1459
Chicon R, Belloque J, Alonso E, López-Fandiňo R (2009) Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure. Food Hydrocolloids 23:593–599
Considine T, Patel HA, Singh H, Creamer LK (2005) Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the pressure-Induced unfolding and aggregation of β-lactoglobulin B. J Agric Food Chem 53:8010–8018
Considine T, Patel HA, Singh H, Creamer LK (2007) Influence of binding conjugated linoleic acid and myristic acid on the heat- and high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Food Chem 102:1270–1280
Crehan CM, Troy DJ, Buckley DJ (2000) Effects of salt level and high hydrostatic pressure processing on frankfurters formulated with 1.5 and 2.5% salt. Meat Sci 55:123–130
Damodaran S (1988) Interrelationship of molecular and functional properties of food proteins. In: Kinsella JE, Soucie WG (eds) Food proteins. American Oil Chemists’ Society, Champaign, IL, pp 21–52
Damodaran S (1994) Structure-function relationship of food proteins. In: Hettiarachchy NS, Ziegler GR (eds) Protein functionality in food systems. Dekker, New York, pp 1–37
Damodaran S (1996) Amino acids, peptides, and proteins. In: Fennema OR (ed) Food chemistry. Dekker, New York, pp 321–430
Elgasim EA, Kennick WH (1980) Effects of pressurization of prerigor beef muscles on protein quality. J Food Sci 45:1122–1124
Fernández-Martin F, Cofrades S, Jiménez Colmenero J (2002) Salt and phosphate effects on the gelling process of pressure/heat treated pork batters. Meat Sci 61:15–23
Fink AL, Calciano LJ, Goto Y, Kuroisu T, Palleros DR (1994) Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33:12504–12511
Frye KJ, Royer CA (1998) Probing the contribution of internal cavities to the volume change of protein unfolding under pressure. Protein Sci 7:2217–2222
Funtenberger S, Dumay E, Cheftel JC (1995) Pressure-induced aggregation of β-lactoglobulin in pH 7.0 buffers. Lebensm Wiss Technol 28:410–418
Funtenberger S, Dumay E, Cheftel JC (1997) High pressure promotes β-lactoglobulin aggregation through SH/S-S interchange reactions. J Agric Food Chem 45:912–921
Galazka VB, Dickinson E, Ledward DA (1996a) Effect of high pressure on the emulsifying behaviour of β-lactoglobulin. Food Hydrocolloids 10:213–219
Galazka VB, Dickinson E, Ledward DA (2000a) Emulsifying properties of ovalbumin in mixtures with sulphated polysaccharides: effect of pH, ionic strength, heat, and high-pressure treatment. J Sci Food Agric 80:1219–1229
Galazka VB, Dickinson E, Ledward DA (2000b) Influence of high pressure processing on protein solutions and emulsions. Curr Opin Colloid Interface Sci 5:182–187
Galazka VB, Ledward DA, Dickinson E, Langley KR (1995) High pressure effects on emulsifying behavior of whey protein concentration. J Food Sci 60:1341–1343
Galazka VB, Ledward DA, Dickinson E, Langley KR (1996b) High pressure effects on emulsifying behavior of whey protein concentrate. J Food Sci 60:1341–1343
Gomez-Estaca J, Gomez-Guillen MC, Montero P (2007) High pressure effects on the quality and preservation of cold-smoked dolphinfish (Coryphaena hippurus) fillets. Food Chem 102:1250–1259
Gross M, 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 221:617–630
Han IH, Swanson BG, Baik BK (2007) Protein digestibility of selected legumes treated with ultrasound and high hydrostatic pressure during soaking. Cereal Chem 84:518–521
Hawley SA (1971) Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10:2436–2442
Hayakawa I, Linko YY, Linko P (1996) Mechanism of high pressure denaturation of proteins. LWT-Food Sci Technol 29:756–762
Hayashi R, Kawamura Y, Nakasa T, Okinaka O (1989) Application of high pressure to food processing: pressurization of egg white and yolk, and properties of gels formed. Agric Biol Chem (Tokyo) 51:2935–2939
He JS, Azuma N, Yang H (2010) Effects of pH and ionic strength on the rheology and microstructure of a pressure-induced whey protein gel. Int Dairy J 20:89–95
He JS, Ruan K (2009) Kinetics of phase separation during pressure-induced gelation of a whey protein isolate. Food Hydrocolloids 23:1729–1733
Hendrickx M, Ludikhuyze L, Van den Broeck I, Weemaes C (1998) Effects of high pressure on enzymes related to food quality. Trends Food Sci Technol 9:197–203
Heremans K (1982) High pressure effects on proteins and other biomolecules. Annu Rev Biophys Bioeng 11:1–21
Heremans K, Smeller L (1998) Protein structure and dynamics at high pressure. Biochim Biophys Acta 1386:353–370
Huppertz T, Fox PF, Kelly A (2004) High pressure treatment of bovine milk: effects on casein micelles and whey proteins. J Dairy Sci 71:97–106
Huppertz T, Hinz K, Zobrist MR, Uniacke T, Kelly AL, Fox PF (2005) Effects of high pressure treatment on the rennet coagulation and cheese-making properties of heated milk. Innov Food Sci Emerg Technol 6:279–285
Iametti S, Transidico P, Bonomi F, Vecchino G, Pittia P, Rovere P, Dall'Aglio G (1997) Molecular modification of β-lactoglobulin upon exposure to high pressure. J Agric Food Chem 45:23–29
Ibanoglu E, Karatas S (2001) High pressure effect on foaming behaviour of whey protein isolate. J Food Eng 47:31–36
Iwasaki T, Norshiroya K, Saitoh N, Okano K, Yamamoto K (2006) Studies of the effect of hydrostatic pressure pretreatment on thermal gelation of chicken myofibrils and pork meat patty. Food Chem 95:474–483
Jiménez Colmenero J, Carballo J, Fernández P, Barreto G, Solas MT (1997) High-pressure-induced changes in the characteristics of low-fat and high-fat sausages. J Sci Food Agric 75:61–66
Jiménez Colmenero J, Fernández P, Carballo J, Fernández-Martin F (1998) High-pressure-cooked low-fat pork and chicken batters as affected by salt levels and cooking temperature. J Food Sci 63:656–659
Kanno C, Mu TH, Hagiwara T, Ametani M, Azuma N (1998) Gel formation from industrial milk whey proteins under hydrostatic pressure: effect of hydrostatic pressure and protein concentration. J Agric Food Chem 46:417–424
Kitabatake N, Kinekawa Y-I (1998) Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo. J Agric Food Chem 46:4917–4923
Knorr D (1993) Effects of high-hydrostatic-pressure processes on food safety and quality. Food Technol 47:156–161
Knorr D, Heinz V, Buckow R (2006) High pressure application for food biopolymers. Biochim Biophys Acta 1764:619–631
Kühn J, Considine T, Singh H (2006) Interactions of milk proteins and volatile flavor compounds: implications in the development of protein foods. J Food Sci 71:2006
Kühn J, Considine T, Singh S (2008) Binding of flavor compounds and whey protein isolate as affected by heat and high pressure treatments. J Agric Food Chem 56:10218–10224
Kuwata K, Li H, Yamada H, Batt CA, Goto Y, Akasaka K (2001) High pressure NMR reveals a variety of fluctuating conformers in α-lactoglobulin. J Mol Biol 305:1073–1083
Lakshmanan R, Parkinson JA, Piggott JR (2007) High-pressure processing and water-holding capacity of fresh and cold-smoked salmon (Salmo salar). Lebensm Wiss Technol 40:544–551
Lee W, Clark S, Swanson BG (2006) Functional properties of high hydrostatic pressure-treated whey protein. J Food Process Preserv 30:488–501
Lim SY, Swanson BG, Clark S (2008a) High hydrostatic pressure modification of whey protein concentrate for improved functional properties. J Dairy Sci 91:1299–1307
Lim SY, Swanson BG, Ross CF, Clark S (2008b) High hydrostatic pressure modification of whey protein concentrate for improved body and texture of low-fat ice cream. J Dairy Sci 91:1308–1316
Liu X, Powers JR, Swanson BG, Hill HH, Clark S (2005a) High hydrostatic pressure affects flavor-binding properties of whey protein concentrate. J Food Sci 70:C581–C585
Liu X, Powers JR, Swanson BG, Hill HH, Clark S (2005b) Modification of whey protein concentrate hydrophobicity by high hydrostatic pressure. Innov Food Sci Emerg Technol 6:310–317
López-Exposito I, Chicon R, Belloque J, Recio I, Alonso E, López-Fandiňo R (2008) Changes in the ovalbumin proteolysis profile by high pressure and its effect on IgG and IgE binding. J Agric Food Chem 56:11809–11816
López-Fandiňo R (2006) High pressure-induced changes in milk proteins and possible applications in dairy technology. Int Dairy J 16:1119–1131
López-Fandiňo R, Carrascosa AV, Olano A (1996) The effects of high pressure on whey protein denaturation and cheese-making properties of raw milk. J Dairy Sci 79:929–936
López-Fandiňo R, Olano A (1998) Effects of high pressure combined with moderate temperatures on the rennet coagulation properties of milk. Int Dairy J 8:623–627
López-Fandiňo R, Ramos M, Olano A (1997) Rennet coagulation of milk subjected to high pressure. J Agric Food Chem 45:3233–3237
Low PS, Somero GN (1975) Pressure effects on enzyme structure and function vitro and under simulated in vivo conditions. Comp Biochem Physiol 52:67–74
Lullien-Pellerin V, Balny C (2002) High-pressure as a tool to study some proteins’ properties: conformational modification, activity and oligomeric dissociation. Innov Food Sci Emerg Technol 3:209–221
Macfarlane JJ (1974) Pressure-induced solubilization of meat proteins in saline solution. J Food Sci 39:542–547
Macfarlane JJ, Mckenzie IJ (1984) Binding of comminuted meat: effect of high pressure. Meat Sci 10:307–320
Messens W, Van Camp J, Huyghebaert A (1997) The use of high pressure to modify the functionality of food proteins. Trends Food Sci Technol 8:107–112
Molina E, Papadopoulou A, Ledward DA (2001) Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins. Food Hydrocolloids 15:263–269
Mor-Mur M, Yuste J (2003) High pressure processing applied to cooked sausage manufacture: physical properties and sensory analysis. Meat Sci 65:1187–1191
Mozhaev VV, Heremans K, Frank J, Masson P, Balny C (1996) High pressure effects on protein structure and function. Proteins Struct Funct Genet 24:81–91
Nakai S, Li-Chan ECY (1993) Recent advances in structure and function of food protein: QSAR approach. Crit Rev Food Sci Nutr 33:477–499
Needs E, Stenning RA, Gill AL, Ferragut V, Rich GT (2000) High-pressure treatment of milk: effects on casein micelle structure and on enzymic coagulation. J Dairy Sci 67:31–42
Nielsen SS, Deshpande SS, Hermodson MA, Scott MP (2002) Comparative digestibility of legume storage proteins. J Agric Food Chem 36:896–902
Offer G, Trinick J (1983) On the mechanism of water holding in meat: the swelling and shrinking of myofibrils. Meat Sci 8:245–281
Papiz MZ, Sawyer L, Eliopoulos EF, North ACT, Findlay JBC, Sivaprasadarao R, Jones TA, Newcomer ME, Kraulis PJ (1986) The structure of β-lactoglobulin and its similarity to plasma retinol binding protein. Nature (London) 324:383–385
Penas E, Prestamo G, Gomez R (2004) High pressure and the enzymatic hydrolysis of soybean whey proteins. Food Chem 85:641–648
Penas E, Prestamo G, Polo F, Gomez R (2006a) Enzymatic proteolysis, under high pressure of soybean whey: analysis of peptides and the allergen Gly m 1 in the hydrolysates. Food Chem 99:569–573
Penas E, Restani P, Ballabio C, Prestamo G, Fiocchi A, Gomez R (2006b) Assessment of the residual immunoreactivity of soybean whey hydrolysates obtained by combined enzymatic proteolysis and high pressure. Eur Food Res Technol 222:286–290
Pittia P, Wilde PJ, Husband FA, Clark DS (1996) Functional and structural properties of β-lactoglobulin as affected by high pressure treatment. J Food Sci 61:1123–1128
Ptitisyn OB (1995) Molten globule and protein folding. Adv Protein Chem 47:83–229
Puppo C, Chapleau N, Speroni F, de Lamballerie-Anton M, Michel F, Anon C, Anton M (2004) Physicochemical modifications of high-pressure-treated soybean protein isolates. J Agric Food Chem 52:1564–1571
Puppo MC, Beaumal V, Chapleau N, Speroni F, de Lamballerie M, Anon MC, Anton M (2008) Physicochemical and rheological properties of soybean protein emulsions processed with a combined temperature/high-pressure treatment. Food Hydrocolloids 22:1079–1089
Puppo MC, Beaumal V, Speroni F, de Lamballerie M, Anon MC, Anton M (2011) β-Conglycinin and glycinin soybean protein emulsions treated by combined temperature-high-pressure treatment. Food Hydrocolloids 25:389–397
Puppo MC, Speroni F, Chapleau N, de Lamballerie M, Anon MC, Anton M (2005) Effect of high-pressure treatment on emulsifying properties of soybean proteins. Food Hydrocolloids 19:289–296
Quiros A, Chicon R, Recio I, Lopez-Fandino R (2007) The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin. Food Chem 104:1734–1739
Rodiles-López JO, Jaramillo-Flores ME, Gutierrez-López GF, Hernandez-Arana A, Fosado-Quiroz RE, Barbosa-Canovas GV, Hernandez-Sanchez H (2008) Effect of high hydrostatic pressure on bovine α-lactalbumin functional properties. J Food Eng 87:363–370
Royer CA (2002) Revisiting volume changes in pressure-induced protein unfolding. Biochimia et Biophysica Acta 1595:201–209
Sarma R, Paul S (2012) The effect of pressure on the hydration structure around hydrophobic solute: a molecular dynamics simulation study. J Chem Phys 136:114510-1–11450-10
Sawyer L, Kontopidis G (2000) The core lipocalin, bovine β-lactoglobulin. Biochim Biophys Acta 1482:136–148
Scharnagl C, Reif M, Friedrich J (2005) Stability of proteins: temperature, pressure and the role of the solvent. Biochim Biophys Acta 1947:187–213
Sikes AL, Tobin AB, Tume RK (2009) Use of high pressure to reduce cook loss and improve texture of low-salt beef sausage batters. Innov Food Sci Emerg Technol 10:405–412
Smeller L (2002) Pressure-temperature phase diagrams of biomolecules. Biochim Biophys Acta 1595:11–29
Smeller L, Rubens P, Heremans K (1999) Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin. Biochemistry 38:3816–3820
Smith D, Galazka VB, Wellner N, Sumner IG (2000) High pressure unfolding of ovalbumin. Int J Food Sci Technol 35:361–370
Speroni F, Beaumal V, de Lamballerie M, Anton M, Anon MC, Puppo MC (2009) Gelation of soybean proteins induced by sequential high-pressure and thermal treatments. Food Hydrocolloids 23:1433–1442
Stapelfeldt H, Skibsted LH (1999) Pressure denaturation and aggregation of β-lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing. J Dairy Res 66:545–558
Sun XG, Holley RA (2010) High hydrostatic pressure effects on the texture of meat and meat products. J Food Sci 75:R17–R23
Suzuki K, Miyagawa Y, Suzuki C (1963) Protein denaturation under high pressure. Measurement of turbidity of isoelectric ovalbumin and horse serum albumin under high pressure. Arch Biochem Biophys 101:225–228
Tang CH, Ma CY (2009) Effects of high pressure treatment on aggregation and structural properties of soy protein isolate. LWT-Food Sci Technol 42:606–611
Tavel L, Moreau C, Bouhallab S, Li-Chan ECY, Guichard E (2010) Interactions between aroma compounds and β-lactoglobulin in the heat-induced molten globule state. Food Chem 119:1550–1556
Tedford LA, Schaschke CJ (2000) Induced structural change of β-lactoglobulin by combined pressure and temperature. Biochem Eng J 5:73–76
Torrezan R, Tham WP, Bell AE, Frazier RA, Cristianini M (2007) Effects of high pressure on functional properties of soy protein. Food Chem 104:140–147
Uversky VN (1997) Diversity of equilibrium compact forms of denatured globular proteins. Protein Pept Lett 4:355–367
Van Camp JV, Messens W, Clement J, Huyghebaert A (1997a) Influence of pH and calcium chloride on the high-pressure-induced aggregation of a whey protein concentrate. J Agric Food Chem 45:1600–1607
Van Camp JV, Messens W, Clement J, Huyghebaert A (1997b) Influence of pH and sodium chloride on the high pressure-induced gel formation of a whey protein concentrate. Food Chem 60:417–424
Van de Ven C, Courvoisier C, Matser A (2007) High pressure versus heat treatment for pasteurisation and sterilisation of model emulsions. Innov Food Sci Emerg Technol 8:230–236
Van der Plancken I (2005) Changes in sulfhydryl content of egg white proteins due to heat and pressure treatment. J Agric Food Chem 53:5726–5733
Van der Plancken I, Loey AV, Hendrickx ME (2005) Combined effect of high pressure and temperature on selected properties of egg white proteins. Innov Food Sci Emerg Technol 2005:11–20
Van der Plancken IV, Loey AV, Hendrickx ME (2007) Foaming properties of egg white proteins affected by heat or high pressure treatment. J Food Eng 78:1410–1426
Vilela RM, Landis LC, Chan HM, Azadi B, Kubow S (2006) High hydrostatic pressure enhances whey protein digestibility to generate whey peptides that improve glutathione status in CFTR-deficient lung epithelial cells. Mol Nutr Food Res 50:1013–1029
Visschers RW, de Jongh HHJ (2005) Disulphide bond formation in food protein. aggregation and gelation. Biotechnol Adv 23:75–80
Wada S, Ogawa Y (1996) High pressure effects on fish lipid degradation: myoglobin change and water holding capacity. In: Hayashi R, Balny C (eds) High pressure bioscience and biotechnology. Elsevier, Amsterdam, pp 351–356
Walker MK, Farkas DF, Anderson SR, Meunier-Goddik L (2004) Effects of high-pressure processing at low temperature on the molecular structure and surface properties of β-lactoglobulin. J Agric Food Chem 52:8230–8235
Wang XS, Tang CH, Li BS, Yang XQ, Li L, Ma CY (2008) Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocolloids 22:560–567
Weber G, Drickamer HG (1983) The effect of high pressure upon proteins and other biomolecules. Q Rev Biophys 16:89–112
Wu SY, Perez MD, Puyol P, Sawyer L (1999) β-Lactoglobulin binds palmitate within its central cavity. J Biotechnol Chem 274:170–174
Yang J, Dunker AK, Powers JR, Clark S, Swanson BG (2001) β-Lactoglobulin molten globule induced by high pressure. J Agric Food Chem 49:3236–3243
Yang J, Powers JR, Clark S, Dunker AK, Swanson BG (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 Journal of Agricultural and Food Chemistry 50
Yang J, Powers JR, Clark S, Dunker AK, Swanson BG (2003) Ligand and flavor binding functional properties of β-lactoglobulin in the molten globule state induced by high pressure. J Food Sci 68:444–452
Yin SW, Tang CH, Wen QB, Yang XQ, Lin L (2008) Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: effect of high-pressure treatment. Food Chem 110:938–945
Zeece M, Huppertz T, Kelly A (2008) Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. Innov Food Sci Emerg Technol 9:62–69
Zipp A, Kauzmann W (1973) Pressure denaturation of metmyoglobin. Biochemistry 12:42–174228
Zobrist MR, Huppertz T, Uniacke T, Fox PF, Kelly A (2005) High-pressure-induced changes in the rennet coagulation properties of bovine milk. Int Dairy J 15:655–662
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer Science+Business Media New York
About this chapter
Cite this chapter
Yang, J., Powers, J.R. (2016). Effects of High Pressure on Food Proteins. In: Balasubramaniam, V., Barbosa-Cánovas, G., Lelieveld, H. (eds) High Pressure Processing of Food. Food Engineering Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-3234-4_18
Download citation
DOI: https://doi.org/10.1007/978-1-4939-3234-4_18
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4939-3233-7
Online ISBN: 978-1-4939-3234-4
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)