Immobilization of Kluyveromyces lactis β-Galactosidase on Meso-macroporous Silica: Use of Infrared Spectroscopy to Rationalize the Catalytic Efficiency.

Enzyme immobilization on adequate carriers is a challenging strategy. Understanding the enzyme-carrier interactions and their effects on enzyme conformation and bioactivity is critical. In this study, a meso-macropores silica (MMS) was used to immobilize β-galactosidase from the yeast Kluyveromyces lactis (β-gal-KL) by physical adsorption.

Gelatin/Maltodextrin Water-in-Water (W/W) Emulsions for the Preparation of Cross-Linked Enzyme-Loaded Microgels.

Cross-linked gelatin microgels were formed in gelatin-in-maltodextrin water-in-water (W/W) emulsions and evaluated as carriers of the enzyme β-galactosidase (β-Gal). The phase behavior of aqueous gelatin/maltodextrin mixtures was studied in detail, focusing on the multiphase region of the phase diagram that is constituted by three equilibrium phases: two immiscible aqueous phases plus one solid phase. The solid phase was analyzed by Raman spectroscopy, and water-in-water emulsions were formed within the multiphase region.

Effect of Meso vs Macro Size of Hierarchical Porous Silica on the Adsorption and Activity of Immobilized β-Galactosidase.

β-Galactosidase (β-Gal) is one of the most important enzymes used in milk processing for improving their nutritional quality and digestibility. Herein, β-Gal has been entrapped into a meso-macroporous material (average pore size 9 and 200 nm, respectively) prepared by a sol-gel method from a silica precursor and a dispersion of solid lipid nanoparticles in a micelle phase. The physisorption of the enzyme depends on the concentration of the feed solution and on the pore size of the support.