Emerging technologies, such as high isostatic pressure and dynamic high pressure, have been widely studied in food processing. These technologies can be applied to several food products and ingredients in order to improve quality and increase the acceptance of processed foods. The main advantage is the replacement of thermal process by high-pressure process, aimed at the inactivation of microorganisms at room temperature. With this technology it is possible to replace the sensory changes caused by high temperature–produced foods with the characteristics of close-to-fresh foods, besides changing the structure and constituents. These changes have been studied in various foods, including milk and dairy products. The results show that depending on the conditions used with each technology, both processes can improve the consistency and increase water retention and emulsion stability in dairy products. The purpose of this chapter is to compare the evolution of these technologies in milk processing and discuss their application in improving the quality and acceptance of these products.
Table 6.1
Parameter | HIP | DHP |
---|---|---|
Type of food | Liquid/semisolid/solid | Liquid |
Operation flow | Batch/semicontinuous | Continuous |
Physical forces | Compression and decompression | Compression, cavitation, turbulence, and impact |
Pressure range | Up to 1000 MPa | Up to 350 MPa |
Residence time under pressure | Unlimited (controlled by the operator, depending on the goal) | Very fast (few seconds—variable not controlled) |
Processing temperature | Freezing, low or mild temperature | Low or mild temperature (not frozen) |
Heating during pressurization | 3–10°C per 100 MPa (adiabatic heating) | 15–25°C per 100 MPa (energy conservation) |
Capacity | Chambers up to 525 L a ; production up to 3.000 kg/h | Up to 5.000 L/h at 150 MPa b |
Filling | Product packaged in flexible packaging before processing (most common) or product without packaging (less common) | Product packed after processing |
DHP, Dynamic high pressure; HIP, high isostatic pressure. Trujillo et al. (2002), Hayes et al. (2005), Diels and Michiels (2006), Huppertz et al. (2006), Dumay et al. (2013).
a Information extracted from Hiperbaric: high pressure processing.
b GEA Process Engineering Ltd.
Table 6.2
HIP | DHP | |
---|---|---|
Fat | No changes in fat globule in bovine milk (Huppertz et al., 2003); increased number of small globules in sheep milk (Gervilla et al., 2001) | Reduction of size of fat globules (Ciron et al., 2010; Oliveira et al., 2014) |
Increased creaming (<250 MPa favors the interaction of lipoproteins; Huppertz et al., 2003) or reduced creaming (>400 MPa, inactivates agglutinin (Huppertz et al., 2003) | Increased lipolysis in raw milk (Datta et al., 2005; Pereda et al., 2008a; Serra et al., 2008a) | |
No formation of free fatty acids in sheep milk (Gervilla et al. 2001) | Better emulsification and stability (Hayes and Kelly, 2003b) | |
No emulsifying effect (Huppertz et al., 2003) | No changes in the structure of the triglyceride (Rodríguez-Alcalá et al., 2009) | |
Protein (casein) | Fragmentation of the micelle (50% reduction; pressure >400 MPa; Huppertz et al., 2006; López-Fandiño, 2006) | Fragmentation of the micelle (∼30% reduction; Roach and Harte, 2008) |
Solubilization of CCP (Huppertz et al., 2006; Huppertz and De Kruif, 2006) | Increasing the size of the micelle ∼45% (over 300 MPa; Roach and Harte, 2008) | |
Reduction of hydrophobic interactions (Huppertz et al., 2006) | Solubilization of CCP (Zamora et al., 2007) | |
Solubilization of casein fractions (in order: β-casein>κ-casein>αs1-casein>αs2-casein; López-Fandiño et al., 1998) | Reduction of hydrophobic interactions (Zamora et al., 2007) | |
Whey protein | Denaturation of β-lactoglobulin (β-Lg) at 100 MPa and α-lactalbumin (α-La) at 400 MPa (Huppertz et al., 2004c) | No denaturation of β-Lg (little formation of disulfide bonds; Sørensen et al., 2014) |
Immunoglobulins (IgG, IgM, and IgA) more resistant to pressure than the thermal process (Contador et al., 2013; Sousa et al., 2014) | α-Lg resistant to pressure (Sørensen et al., 2014) | |
Reduction of protein size (>200 MPa; Bouaouina et al., 2006) | ||
Sensitivity to denaturation: Lactoferrin<β-Lg<immunoglobulin<BSA<α-La (Patel et al., 2006) | Increase in solubility of whey proteins (Dissanayake and Vasilejvic, 2009) | |
Enzymes | Higher resistance of alkaline phosphatase (800 MPa inactivation for 8 min; Rademacher et al., 1998) | Alkaline phosphatase: activation from 100 to 150 MPa and inactivation above 175 MPa (Picart et al., 2006) |
Plasmin resistant at 400 MPa/30 min at 25°C. 87% inactivation of plasmin at 400 MPa/15 min at 60°C; Garía-Risco et al., 2000; Huppertz et al., 2004b) | Plasmin resistant up to 200 MPa (Iucci et al., 2008) | |
Lactoperoxidase very stable (50% reduction after 800 MPa/4 h at 60°C; Rademacher et al., 1998) | Lactoperoxidase increased activity at 75 MPa (Vannini et al., 2004) | |
Lysozyme very resistant (Viazis et al., 2007) | Lysozyme activity increased at 75 MPa (Vannini et al., 2004) | |
Lipase resistance up to 400 MPa at 3°C (Pandey and Ramaswamy, 2004) | Lipase activated at 200 MPa at <58°C of outlet temperature or inactivated at 200 MPa at outlet temperature >71°C (Datta et al., 2005) | |
Minerals | Solubilization of colloidal calcium phosphate (63% at 350 MPa; Kielczewska et al., 2009) | Solubilization of colloidal calcium phosphate (8%–30% from 150 to 300 MPa; Serra et al., 2008b) |
CCP, Colloidal calcium phosphate; DHP, dynamic high pressure; HIP, high isostatic pressure.
Table 6.3
Product | HIP | DHP |
---|---|---|
Milk | Can replace pasteurization and sterilization processes (Vazquez-Landaverde et al., 2006) | Can replace pasteurization processes (Pedras et al., 2012) or used in combination with thermal process for sterilization (Amador Espejo et al., 2014a) |
Skimmed milk appears semi transparent due to casein fragmentation (>400 MPa; Devi et al., 2015) | No changes in milk appearance (Hernández and Harte, 2008) | |
Absence of undesirable volatile compounds generated in the thermal process (Trujillo et al., 2002) | Absence of undesirable volatile compounds generated in the thermal process (Amador-Espejo et al., 2014b) | |
No significant reduction of vitamins, amino acids, simple sugars and flavor compounds (Trujillo et al., 2002) | High stability of the fat emulsion, preventing phase separation (Zamora et al., 2012) | |
Processed milk for cheese manufacture | Moderate pressures (<300 MPa) accelerates coagulation (casein fragmentation; López-Fandiño et al., 1996; Ohmiya et al., 2014) | Acceleration or no effects on coagulation (with no denaturation of β-Lg; Hayes and Kelly, 2003b; Sandra and Dalgleish, 2007; Zamora et al., 2007) |
Higher pressures (>400 MPa) increase coagulation time and cheese yield (better retention capacity due to denaturation of β-Lg; Huppertz et al., 2004a,c, 2005) | Increase in lipolysis during ripening (200 MPa, <58°C) or no effects (200 MPa, >71°C; Datta et al., 2005; Juan et al., 2015) | |
Fresh cheese is more soft, less brittle and more rigid (Molina et al., 2000) | Can accelerate cheese ripening (Juan et al., 2016; Lanciotti et al., 2004; Vannini et al., 2008) | |
Cheese manufacture | Reduction of contamination and extension of shelf life (>400 MPa; Evert-Arriagada et al., 2014; O’Reilly et al., 2000) | It cannot be used in cheese (only fluids) |
Accelerating or delaying the ripening process depending on the conditions and microbial cultures (Costabel et al., 2016; Delgado et al., 2012) | ||
Fresh cheese more compact and elastic (Sandra et al., 2004) | ||
Yogurt | Increased consistency (Harte et al., 2002), mainly in set yogurt | Increased consistency, mainly in stirred yogurt (Serra et al., 2007) |
Reduction of spoilage microorganisms (Penna et al., 2007; Shah et al., 2008) | Reduction of post acidification (Patrignani et al., 2007; Serra et al., 2009a) | |
Increased water retention capacity | Increased water retention capacity (Oliveira et al., 2014) | |
Extension of shelf life (Penna et al., 2007; Shah et al., 2008) | ||
Ice cream | Improved foaming stability of whey protein (Liu et al., 2005) | Improved foaming capacity of whey protein (Bouaouina et al., 2006; Dissanayake and Vasilejvic, 2009) |
Better interaction with aromas (Kühn et al., 2006; Liu et al., 2005) | Enables to produce low-fat ice creams with texture similar to full-fat ice creams (Innocente et al., 2009) | |
Smooth texture (controlling small crystals formation; Eberhard et al., 1999; Huppertz et al., 2011) | ||
Butter | Extension of shelf life (Dumay et al., 1996) | |
Improving aggregation of fat and consistency (Dumay et al., 1996) |
DHP, Dynamic high pressure; HIP, high isostatic pressure.