Lactose hydrolysis and formation of galactooligosaccharides by a novel immobilized beta-galactosidase from the thermophilic fungus Talaromyces thermophilus.

beta-Galactosidase from the fungus Talaromyces thermophilus CBS 236.58 was immobilized by covalent attachment onto the insoluble carrier Eupergit C with a high binding efficiency of 95%. Immobilization increased both activity and stability at higher pH values and temperature when compared with the free enzyme.

Formation of galacto-oligosaccharides during lactose hydrolysis by a novel beta-galactosidase from the moderately thermophilic fungus Talaromyces thermophilus.

Discontinuous and continuous processes of lactose hydrolysis and concomitant galacto-oligosaccharide (GalOS) formation were studied. To this end a wide experimental range of the main variables was evaluated, including the initial lactose concentration, the degree of lactose conversion, the pH value and the temperature for discontinuous transformations, while the initial lactose concentration and the feed rate were varied for the continuous process. For both processes a high-initial lactose concentration proved to be advantageous for the formation of GalOS.

Purification and characterisation of an intracellular enzyme with beta-glucosidase and beta-galactosidase activity from the thermophilic fungus Talaromyces thermophilus CBS 236.58.

An intracellular beta-glycoside hydrolase with beta-glucosidase and beta-galactosidase activity, designated beta-glucosidase BGL1, was isolated to apparent homogeneity from the thermophilic ascomycete Talaromyces thermophilus CBS 236.58. The monomeric enzyme has a molecular mass of 50 kDa (SDS-PAGE) and an isoelectric point of 4.