Corn Gluten Hydrolysis By Alcalase: Effects of Process Parameters on Hydrolysis, Solubilization and Enzyme Inactivation

The aim of this study was to investigate the influences of substrate concentration, enzyme concentration, temperature and pH on hydrolysis and solubilization of corn gluten as well as enzyme stability. The corn gluten was hydrolyzed by Alcalase enzyme (a bacterial protease produced by a selected strain of Bacillus Licheniformis) that was chosen among five commercial enzymes examined. The optimum process conditions for hydrolysis and solubilization were obtained as 30 g L-1 substrate mass concentration, 2.5 mL L-1 enzyme volume concentration, 55 °C and pH 8. Under these conditions, the values of degree of hydrolysis and solubilization were found as 28.4 % and 85.3 % respectively; and enzyme lost its activity by approx. 74 % at the end of 120 min processing time. Modeling studies were performed to determine the kinetics of hydrolysis, solubilization and enzyme inactivation. The relationship between hydrolysis and solubilization was found linear for all experimental conditions examined. The inactivation energy of Alcalase at the temperature range of 40-55 °C was determined to be 67.864 kJ mol-1

Milk Lactose Hydrolysis In A Batch Reactor: Optimisation Of Process Parameters, Kinetics Of Hydrolysis And Enzyme Inactivation

The present investigation describes the effects of the process quantities on enzymatic hydrolysis of milk lactose and enzyme stability. The lactose hydrolysis reactions were carried out in 250 mL of milk by using a commercial β-galactosidase produced from Kluyveromyces marxianus lactis. The residual lactose mass concentration (g L-1) and residual enzyme activity (%) against time were investigated vs. process variables such as temperature, impeller speed and enzyme concentration. Optimum conditions for hydrolysis were obtained as 37 °C, 300 rpm, 1 mL L-1 enzyme concentration and 30 min of processing time. The lactose hydrolysis process resulted in 84 % of hydrolysis degree and 52 % of residual enzyme activity at the optimum experimental conditions obtained. After evaluation of the data, it was found that the kinetics of hydrolysis and enzyme inactivation could be represented by a first order kinetic model and a single-step non-first-order enzyme inactivation kinetic model for all process conditions applied. Also, to illustrate the effect of process variables on hydrolysis and enzyme stability, some modelling studies were performed. The activation energy for hydrolysis reaction (EA) was calculated as 50.685 kJ mol-1