The invertase activity has been studied in the presence of a temperature gradient by interposing the enzyme onto a polymeric membrane between two solutions, kept at different temperatures. The enzyme activity has been determined as a function of average temperature (T(av)) and of the applied temperature difference DELTAT= T(w) - T(c). It has been found that in the non-isothermal state the activity is higher than in comparable isothermal conditions, the increase being proportional to the applied transmembrane temperature difference. Mathematical relationships between the isothermal and non-isothermal enzyme activity have been derived. The rapid product removal from the enzyme complex by means of a process of matter transport associated to the flux of thermal energy is indicated as the way by which the temperature gradient affects the enzyme activity. Some practical applications are suggested.

Effect of temperature gradients on the activity of enzymes immobilized on natural polymeric matrices.

Mita DG;Russo P;Rossi S;Bencivenga U;
1993

Abstract

The invertase activity has been studied in the presence of a temperature gradient by interposing the enzyme onto a polymeric membrane between two solutions, kept at different temperatures. The enzyme activity has been determined as a function of average temperature (T(av)) and of the applied temperature difference DELTAT= T(w) - T(c). It has been found that in the non-isothermal state the activity is higher than in comparable isothermal conditions, the increase being proportional to the applied transmembrane temperature difference. Mathematical relationships between the isothermal and non-isothermal enzyme activity have been derived. The rapid product removal from the enzyme complex by means of a process of matter transport associated to the flux of thermal energy is indicated as the way by which the temperature gradient affects the enzyme activity. Some practical applications are suggested.
1993
IMMOBILIZED ENZYMES
THERMODIALYSIS
BIOSEPARATION PROCESSES
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/179303
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