Operational stability and kinetics of lactose hydrolysis by β-galactosidase from Kluyveromyces fragilis - DOI: 10.4025/actascihealthsci.v25i1.2244

Abstract

The kinetic modeling of the lactose hydrolysis and the operational stability of the enzyme β-galactosidase of Kluyveromyces fragilis was determined using as substrate skimmed powdered milk, reconstituted in a way to supply two lactose concentrations: 5% and 10% (w/v). For the operational stability both lactose concentrations were studied in the presence and in the absence of the buffer pH 6.5. Every 40 minutes the residual activity was determined by the method of the initial velocities. The experimental results showed that the buffer leads to enzyme inactivation. However, for lactose solutions without buffer, the residual activity only declines 15% in 6 hours and later it decreases abruptly. In the kinetic modeling the hydrolysis reaction was led to 40ºC/7h, being used enzyme concentrations equivalent to 1500 and 8100 LAU/L. The adjusted model allowed us to conclude that it is necessary to use the quantity of 3450 LAU/L of the enzyme to obtain the hydrolysis from 70% to 80% of the milk lactose in two to three hours of reaction.