Dispersin B is a β-hexosaminidase that specifically hydrolyzes β-1,6-glycosidic linkages of acetylglucosamine polymers found in biofilm. This enzyme is derived from Aggregatibacter actinomycetemcomitans, which secretes adherent cells from mature biofilm colonies by secreting disperse B. The active site of Disperse B contains three highly conserved acidic residues: aspartic acid at residue 183 (D183), glutamic acid at residue 184 (E184), and glutamic acid at residue 332 (E332).
Design:
We hope that Dspb, like siderophore, is regulated by HSL, and when HSL is present, the dspb gene will express. It is also considered that the dspb enzyme activity is low, can be accumulated in the cells first, and then released by the subsequent lysis system.