Continuous production of α,α-trehalose by immobilised fungal trehalose phosphorylase

Abstract

Immobilisation of trehalose phosphorylase from Schizophyllum commune by adsorption onto anion-exchange materials stabilised the enzyme activity at 30 °C by approx. 35-fold. Immobilised and free enzymes showed similar pH-dependence of activity but different inactivation behavior above 30 °C. A fixed-bed enzyme reactor produced α,α-trehalose at a stable substrate conversion of 80% with a productivity of 2.6 g l−1 h−1 for 72 h. Inhibition of trehalose phosphorylase by phosphate limited the productivity of a direct conversion of starch into α,α-trehalose.