Immobilization of a recombinant Escherichia coli producing a thermostable alpha-L-rhamnosidase: Creation of a bioreactor for hydrolyses of naringin
An U-L-rhamnosidase (E.C. 3.2.1.40) from a newly discovered thermophilic bacterium was expressed in Escherichia coli BL21 DE3 pRIL cells. The cells were immobilized in Ca2+-alginate beads. The temperature of 50 degrees C used in reactions, appeared to be sufficient for making the mesophilic strain porous enough for the substrate to access the cloned thermostable enzyme. Pretreatment of cells with
