Creating a bifunctional protein by insertion of β-lactamase into the maltodextrin-binding protein
- 1 November 1997
- journal article
- Published by Springer Nature in Nature Biotechnology
- Vol. 15 (12) , 1276-1279
- https://doi.org/10.1038/nbt1197-1276
Abstract
Hybrid proteins were generated by inserting the penicillin-hydrolyzing enzyme, TEM beta-lactamase (Bla), into the maltodextrin-binding protein (MalE). The inserted Bla was functionally accommodated by MalE when it was placed within permissive sites. The maltose binding and penicillinase activities of purified hybrids were indistinguishable from those of the wild-type MalE and Bla proteins. Moreover, these hybrids displayed an additional unexpected property: maltose stabilized the active site of inserted Bla.Keywords
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