Formulation of organic and inorganic hydrogel matrices for immobilization of β-glucosidase in microfluidic platform.

The aim of this study was to formulate silica and alginate hydrogels for immobilization of β-glucosidase. For this purpose, enzyme kinetics in hydrogels were determined, activity of immobilized enzymes was compared with that of free enzyme, and structures of silica and alginate hydrogels were characterized in terms of surface area and pore size. The addition of polyethylene oxide improved the mechanical strength of the silica gels and 68% of the initial activity of the enzyme was preserved after immobilizing into tetraethyl orthosilicate-polyethylene oxide matrix where the relative activity in alginate beads was 87%.

An injectable alginate-based hydrogel for microfluidic applications.

The objective of this study was to develop an injectable alginate based formulation for immobilizing enzymes into microfluidic systems. The gelation was induced upon lowering the pH by addition of d-glucono-δ-lactone (GDL) and release of Ca ions from solid CaCO. The effects of GDL concentration on enzymatic activity and gelation time were investigated.

Determining sites of interaction between prenisin and its modification enzymes NisB and NisC.

Although nisin is a model lantibiotic, our knowledge of the specific interactions of prenisin with its modification enzymes remains fragmentary. Here, we demonstrate that the nisin modification enzymes NisB and NisC can be pulled down in vitro from Lactococcus lactis by an engineered His-tagged prenisin. This approach enables us to determine important intermolecular interactions of prenisin with its modification machinery within L.