CREATING A BIFUNCTIONAL PROTEIN BY INSERTION OF BETA-LACTAMASE INTO THE MALTODEXTRIN-BINDING PROTEIN

Hybrid proteins were generated by inserting the penicillin-hydrolyzing enzyme, TEM beta-lactamase (Bla), into the maltodextrin-binding prote in (MalE). The inserted Bla was functionally accommodated by MalE when it was placed within permissive sites. The maltose binding and penici llinase activities of purified hybrids were indistinguishable from tho se of the wild-type MalE and Bla proteins. Moreover, these hybrids dis played an additional unexpected property: maltose stabilized the activ e site of inserted Bla.