Immobilization of β-galactosidase from <i style="mso-bidi-font-style:normal">Enterobacter cloacae</i>:<i style="mso-bidi-font-style:normal"> </i>Characterization and its use in the continuous production of low lactose milk

Abstract

Immobilization of β-galactosidase from <i style="mso-bidi-font-style:normal">Enterobacter cloacae</i> was carried out using barium alginate gel (2%). Maximum activity (39.33 IU/mg) of the immobilized enzyme was observed at pH 9.0 and temperature 50^oC. The immobilized enzyme was found to be stable in pH range 8.5-9.5 and temperature range 4-50^oC. The enzyme activity was stimulated by only Ca²⁺_, Mn²⁺and EDTA at 0.5 mM concentration. Immobilized enzyme was used for the preparation of low lactose milk in a jacketed packed bed column reactor (height 150 mm, internal diam 22 mm). At 89 mm bed height and dilution rate 4.30 h^-1, 61.25 and 46.67% conversion of lactose were observed using lactose (4%) solution and milk (lactose content 4.2%) as substrate, respectively.