Simulação de alternativas de processos para a hidrólise de sacarose

• Autor(a) principal: Berti, Claudinei
• Data de Publicação: 1996
• Tipo de documento: Dissertação
• Idioma: por
• Título da fonte: Repositório Institucional da Universidade Estadual de Maringá (RI-UEM)
• Texto Completo: http://repositorio.uem.br:8080/jspui/handle/1/3821
• topic: Cinética (Química); Hidrólise enzimática da sacarose; Sacarose; Processo de inversão; Hidrólise da sacarose; Processos alternativos; Frutose; Inversão da sacarose; Enzima invertase; Brasil.; Engenharias; Engenharia Química

This work had as main objective, to contribute to the study of the kinetics of sucrose hydrolysis by invertase, in a homogeneus reactor, aimining at increasing the knowledge necessary to project an industrail scale reactor for this process. The catalytic properties of the enzyme and experimental data used to verify the quality of the developed models were taken from BERGAMASCO (1989). Sucrose hydrolysis has been modeled from conversion data obtained at pH 5,0, 55 °C and 85% w/v sucrose concentration. Modeling results have shown that experimental data was well modeled by BOWSKI et alii (1971) model when the effects of enzyme deactivation and product inibition were included. The hypothesis of varying water concentration as a function of the hydrolysis reaction has been included in the model. Simulation results have shown that increasing initial substrate concentration leads to longer reaction times to reach equivalent high conversions. From simulation it also can be observed that for shorter conversion times, the temperatures of 50 and 55 °C are indicated, while for 60 °C enzyme deactivation is noticeable, leading to a reduction in the maximum conversion that can be reached. Staged enzyme addition was studied, varying the fraction of enzyme added at reaction time zero and subsequent addition at constant flow rate up to complete the same quantity added in the simple batch system. Simulation has shown that there is no advantage in staged enzyme addition in spite off the noticeable enzyme deactivation.