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Most carbohydrates are not affected by high pressure (29). As mentioned, reactions with negative reaction and activation volumes are accelerated under pressure. As an example methylglycosides may be hydrolyzed under pressure into aglycone and MeOH. Because of the slightly positive activation volume, disaccharides are stable at process conditions. At very high pressure over 1000 MPa solvolysis reactions of the glycosidic bonds can occur (32). Concerning the effects on water-binding and gel-forming properties, polysaccharides can be affected by high isostatic pressure (42). These examples relate to the functional properties and do not involve structural changes. 5.3.4 Proteins
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High pressure-induced reversible or irreversible changes of the protein native structure (43, 44) are analogous to the changes occurring with heat and chemicals, but the residual molecular structure can vary signi cantly. Knorr et al. (45) have published a review regarding the changes of the protein structure under pressure and temperature. For analyzing the pressure and temperature landscape of proteins, a twostate transition is assumed, which is at equilibrium at the phase transition line (Fig. 5.6, e.g., between native and denatured). These phenomena can be modeled by an empirical model with a thermodynamic background by using the three-dimensional free energy landscape in response to pressure and temperature (Fig. 5.6). In Gibbs function of free energy (Eq. 5.8), pressure and temperature are the independent variables. Integration of Equation 5.8 using a Taylor series expansion up to second-order terms (46) yields Equation 5.18:
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G (T, p) p DENATURED p c
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Free energy p State B G < 0 Equilib G = 0 r
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State A G > 0
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Figure 5.6 Relation between cold (c), pressure (p) and heat (h) denaturation of proteins and three-dimensional free energy landscape in response to pressure and temperature (18). Reprinted with kind permission of Springer Science and Business Media.
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2 G = G0 + V0 ( p p0 ) S0 (T T0 ) + ( 2) ( p p0 ) ( c p 2T0 ) (T T0 )2 + ( p p0 ) (T T0 )
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(5.18)
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where denotes the change of the corresponding parameter during unfolding. This quadratic two-variable approximation of the difference in Gibbs free energy yields to an ellipsoidal phase transition line in the pressure and temperature landscape for equilibrium condition ( G = 0 in Fig. 5.6) (47). This model can be treated as a general approach, where state A and state B could denote molecular or physicochemical states. In the case of spore inactivation, state A could represent the recoverable and B the not recoverable spores, respectively. The transition line would run along the equilibrium G = 0 as elliptical shape at various pressures and temperatures (18). The mode of action of the high hydrostatic pressure in the treated foods is not fully understood but it is theorized that this treatment inactivates the microbial ora by inactivating overall enzyme activity in the living cells, thus interrupting all cellular functions during the high-pressure phase. In contrast to heat, HPP does not denature covalent bonds, which in turn leaves primary protein structure largely unaffected. According to the document of the DFG-Senate Commission for Food Safety (SKLM) (29) high pressure in uences the quaternary structure of the protein through hydrophobic interactions, the tertiary structure through reversible unfolding, and the secondary structure through irreversible unfolding. There are different rheological properties of pressure-induced gels in comparison to heat-induced gels. The higher protease sensitivity of pressure-modi ed proteins is probably related to a higher water-binding capacity. Another interesting point is that the resistance to proteolysis of hamster and cattle prion proteins could be reduced by high-pressure processing at higher temperatures over 80 C (48, 49). The activity and substrate speci city of enzymes can be also affected by high pressure. There might be a risk of the formation of undesirable substances by reactivation of enzymes during storage. Also an increase of the enzyme activity under pressure could be observed. The substrate speci city of enzymes in the eld of foodstuffs is not well understood. As an example peroxidases are inactivated at low pressures in the presence of some substrates but not others (50, 51). Currently, no formations of toxic compounds caused by changed substrate speci city under pressure were observed (29). Butz et al. (52) showed that the antioxidative and antimutagenic potential of fruit and vegetable juices remains intact after high-pressure treatment. The main issue in terms of safety aspects is to prove the potential formations of biological active peptides. Peptides with pyroglutamate (2-oxyprolin) at the N-terminal are more resistant to breakdown by peptidases and such substances are occasionally biologically active (29). It was observed that the conversion of glutamine into pyroglutamate (2-oxyprolin) is favored under elevated pressure and temperature conditions (53 55).
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