Immobilized β-galactosidase BgaC from Bifidobacterium adolescentis retains stability and activity during repeated cycles of use.

ABSTRACT: β-Galactosidase enzymes catalyze the hydrolysis of terminal non-reducing β-D-galactose residues in β-galactosides. These enzymes are important in producing lactose-free dairy products, reducing the lactose content of whey in dairy products, and for production of galactooligosaccharides (GOS) as prebiotic additives to infant formula. To use β-galactosidases in industrial settings, enzyme immobilization procedures are used to enhance their activity and stability and to minimize enzyme quantities and cost. In this study, recombinant Bifidobacterium adolescentis β-galactosidase BgaC was immobilized in calcium alginate and gelatin cross-linked with glutaraldehyde. The kinetic parameters and stability properties of immobilized BgaC were characterized in comparison with free soluble enzyme. The K

SUBMITTER: Mulualem DM 

PROVIDER: S-EPMC12310786 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature