Effect of modulation of enzyme inactivation on temperature optimization for reactor operation with chitin-immobilized lactase

Andrés Illanes, Lorena Wilson, Gonzalo Tomasello

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29 Scopus citations

Abstract

Temperature is a critical variable to be optimized in any enzymatic process, producing opposite effects on enzyme activity and inactivation rate. Temperature functions for all kinetic and inactivation parameters were validated for chitin-immobilized yeast lactase (CIL). Enzyme inactivation was described by a two-stage series mechanism. The effect of galactose and lactose on inactivation was determined in terms of modulation factors that were positive for galactose and negative for lactose. Modulation factors were mild functions of temperature in the first stage and strong functions in the second stage of enzyme inactivation, where galactose positive modulation factors increase while lactose negative modulation factors decrease with temperature. Temperature-explicit functions for kinetic and inactivation parameters were incorporated into a scheme to optimize temperature in the simulation of a continuous packed-bed reactor operation with chitin-immobilized lactase, based on an annual cost objective function. Optimum temperature was 20°C at enzyme replacement of 25% residual activity, and increased only slightly at higher replacement frequencies. The effect of modulation factors on reactor design and temperature optimization is presented and discussed. Software for temperature optimization that allows the introduction of variations in all parameters and operational criteria to perform sensitivity analysis was developed.

Original languageEnglish
Pages (from-to)531-540
Number of pages10
JournalJournal of Molecular Catalysis B: Enzymatic
Volume11
Issue number4-6
DOIs
StatePublished - 22 Jan 2001

Keywords

  • Enzyme inactivation
  • Enzyme reactors
  • Immobilized lactase
  • Modulation factors
  • Temperature optimization

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