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Temperature

Table 4. Denaturation Constants for the Transition State of Various Food and Food-Related Proteins

Temperature

Figure 2. Parameters obtained from differential scanning calo-rimetry. N, Native state; AH, change in enthalpy; ACp, change in specific heat capacity; Td, denaturation temperature; D, denatured state.

ray crystallography and two-dimensional nuclear magnetic resonance, protein structures resulting from partial or complete denaturation are generally not well defined. The susceptibility of a protein to denaturation is dependent on the ability of the denaturant to break the bonds and/or interactions that stabilize the protein structure (Table 2). This requires energy input, ie, chemical or physical (Fig. 3). The relatively large values of denaturation constants in Table 4 (40) reflect the nature of denaturation (ie, N D transition) in that many noncovalent interactions must be broken. Because every protein possesses a characteristic or unique structure, the effects of a denaturant are protein specific. For example, the denatured state of a protein may be transitional (eg, during thermal processing), after which it renatures with full recovery of its native (functional) properties (eg, many peroxidases). Conversely, the denatured state may be formed irreversibly and correspond to a new or technological state with predictable/

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