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Biofilm  is  an  aggregate  of  consortium  bacteria  that adhere  to  each  other  on  a  surface.  It  is  usually  protected  by  the exopolysaccharide layer. Various invasive  medical procedures, such as catheterization, endotracheal tube installation, and contact lens utilization, are vulnerable to biofilm infection. The National Institute of Health (NIH) estimates 65% of all  microbial  infections  are  caused  by  biofilm.  Periplasmic  α-amylase  (MalS)  is  an  enzyme  that  hydrolyzes  α-1,  4-glicosidic  bond  in  glycogen,  starch,  and  others  related  polysaccharides  in periplasmic  space.  Another  protein  called hemolysin-α (HlyA)  is  a  secretion  signal  protein  on  C  terminal of  particular  peptide  in  gram  negative  bacteria.  We proposed a novel recombinant plasmid expressing  α-amylase and hemolysin-αfusion in pSB1C3 which is cloned into E.colito enable  α-amylase excretion to extracellular for degrading biofilm polysaccharides content, as in starch agar. Microtiter  assay  was  performed  to  analyze  the  reduction  percentage  of  biofilm  by  adding  recombinant  E.coli into media. This system is more effective in degrading biofilm from gram positive bacteria i.e.:  Bacillus substilis(30.21%) and  Staphylococcus  aureus  (24.20%),  and  less  effective  degrading  biofilm  of  gram  negative  i.e.:  Vibrio  cholera (5.30%), Pseudomonas aeruginosa (8.50%), Klebsiella pneumonia (6.75%) andE. coli (-0.6%). Gram positive bacteria \udhave a thick layer of peptidoglycan, causing the enzyme to work more effectively in degrading polysaccharides

Expression and the Functional Study of Fusion Proteins α-Amylase and Hemolysin- αas an Application in Biofilm Polysaccharide Degradation