Abstract
Previous models based on the Michaelis–Menten kinetic equation, that glucose was not used as an acceptor, did not explain our experimental data for lactose conversion by a recombinant β-galactosidase from Kluyeromyces lactis. In order to create a new kinetic model based on the data, the effects of galactose and glucose on β-galactosidase activity were investigated. Galactose acted as an inhibitor at low concentrations of galactose and lactose, but did not inhibit the activity of β-galactosidase at high concentrations of galactose (above 50 mM) and lactose (above 100 mM). The addition of glucose at concentrations below 50 mM resulted in an increased reaction rate. A new model of K. lactis β-galactosidase for both hydrolysis and transgalactosylation reactions with glucose and lactose as acceptors was proposed. The proposed model was fitted well to the experimental data of the time-course reactions for lactose conversion by K. lactis β-galactosidase at various concentrations of substrate.
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