Hydrolysis of lactose in whey permeate by immobilized #beta#-galactosidase from Kluyveromyces fragilis

摘要

Neutral ~3-galactosidase from Kluvveromyces fragilis was immobilized on silanized porous glass modified by glutaralde-hyde binding, with retention of more than 90% of its activity. Marked shifts in optimum pH (from 7.0 to 6.0) and temperature (from 350C to 500C) of the solid-phase enzyme were observed together with high catalytic activity and reasonable stability at wider pH and temperature ranges than those of the free enzyme. Highly efficient lactose saceharification (86—90%) in whey permeate was achieved both in a batch process and in a recycling packed-bed bioreactor.