HIGH-LEVEL EXPRESSION OF BACILLUS-THURINGIENSIS PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C BY THE BACILLUS-BREVIS HOST-VECTOR SYSTEM

We succeeded in hyperproduction of Bacillus thuringiensis phosphatidyl inositol-specific phospholipase C (PIPLC), using a Bacillus brevis 47 expression system. The recombinant B. thuringiensis PIPLC was expresse d under the control of the middle wall protein gene promoter in B. bre vis expression vector pNU211. A large amount of recombinant PIPLC (0.4 g per liter culture) was secreted into the medium as a mature enzyme, and the enzymatic properties of purified recombinant PIPLC were simil ar to those of the enzyme from wild-type B. thuringiensis. This system provides a useful approach to the three-dimensional structure-functio n relationship of PIPLC.