β-galactosidase is an important enzyme that acts on lactose hydrolysis and can be used to obtain food for consumers intolerant to this disaccharide. The yeast Kluyveromyces marxianus presents a good growth yield, is a safe microorganism for industrial applications and has been used for enzyme production using the submerged process. The β-galactosidase obtained was fractionated with ammonium sulphate and characterized with respect to its optimum temperature and pH, thermal stability and its D and z values, as well as its kinetic and thermodynamic parameters. The optimum temperature and pH were 45-50 °C and 7.0, respectively. The activation energy and the deactivation reaction of the enzymatic reaction were, respectively, 9.8 kcal.mol-1 and 64.2 kcal.mol-1. The Km and Vmax values obtained were 3.7 mM and 99.0 U.mL-1, respectively. The Gibbs free energy decreased with increasing temperature and the enzyme was more stable at 30 °C (∆G* = 106.8 kJ.mol-1). The enthalpy was 313.04 kJ.mol-1 and entropy 0.68 kJ.mol.k-1. The D value confirmed that the enzyme was more stable at temperatures around 30 °C (D = 11,513.0 min) and the z value was 5.8 °C.
Enzyme; Optimum temperature; Optimum pH; Enthalpy; Entropy; Gibbs free energy
