Consequences of Matrix Structural Changes on Functional Stability of Enzymes as Affected by Electrolytes

  • M. F. Mazzobre
  • P. R. Santagapita
  • N. Gutiérrez
  • M. P. De Buera
Part of the Food Engineering series book series (FSES)

The conservation of labile biomolecules in fields such us biology, pharmaceuticals, and food science is generally performed in dehydrated or frozen media. An equilibrium state does not exist in these systems, but they can reach several states of metastability. The conservation of desirable properties in foods and ingredients is then governed by conditions of metastability, often based on the maintenance of amorphous metastable properties of the systems (Suzuki et al., 1997; Sun and Leopold, 1997; Mazzobre and Buera, 1999). While biomolecules are not under a thermodynamically stable condition, they are kinetically stabilized. The action of cryo- and dehydro-protectants can be ascribed to both kinetic and specific effects. At the kinetic level, the protectants promote the formation of amorphous, glassy systems and influence the kinetics of reactions responsible for deterioration during storage. At the specific level, they are believed to interact with biological structures and to stabilize them during freezing or drying, although by different mechanisms (Carpenter et al., 1986). During freezing of aqueous solutions or biological material, ice formation leads to a freeze-concentrated unfrozen phase with properties (such as pH, ionic strength, and viscosity) significantly different from those of the original system (Pikal, 1999).


Glass Transition Temperature Differential Scanning Calorimeter Water Crystallization Freeze System Trehalose Dihydrate 
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Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • M. F. Mazzobre
    • 1
  • P. R. Santagapita
    • 1
  • N. Gutiérrez
    • 1
  • M. P. De Buera
    • 1
  1. 1.Departamento de IndustriasUniversidad de Buenos AiresArgentina

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