Temperature optimization for reactor operation with chitin-immobilized lactase under modulated inactivation

Illanes A.; Wilson, L; Tomasello, G.

Abstract

Temperature effects on all kinetic and inactivation parameters have been determined for chitin immobilized lactase from Kluyveromyces marxianus var. marxianus, and proper temperature functions have been validated. Maximum reaction rate, Michaelis constant referred to lactose. inhibition constant for galactose and inactivation rates increased with temperature. Enzyme inactivation was adequately modelled bg a two-stage series mechanism. The effect of galactose and lactose on enzyme inactivation was determined in terms of modulation factors that were positive for galactose and negative for lactose over the whole range of temperature studied, Modulation factors were mild functions of temperature in the first stage and strong functions in the second stage of CIL inactivation where galactose positive modulation factors increase with temperature and lactose negative modulation factors decrease with temperature. Temperature explicit functions for all kinetic and inactivation parameters were incorporated into a scheme to optimize the temperature of operation for a sequential batch reactor with chitin-immobilized lactase, based on an annual cost objective function for reactor operation. Software for temperature optimization was developed creating a friendly interface with user that allows the introduction of variations in all parameters and operational criteria to perform sensitivity analysis. (C) 2000 Elsevier Science Inc. All rights reserved.

Más información

Título según WOS: Temperature optimization for reactor operation with chitin-immobilized lactase under modulated inactivation
Título según SCOPUS: Temperature optimization for reactor operation with chitin-immobilized lactase under modulated inactivation
Título de la Revista: ENZYME AND MICROBIAL TECHNOLOGY
Volumen: 27
Número: 3-5
Editorial: Elsevier Science Inc.
Fecha de publicación: 2000
Página de inicio: 270
Página final: 278
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S014102290000209X
DOI:

10.1016/S0141-0229(00)00209-X

Notas: ISI, SCOPUS