Figures & data
Figure 4. Purification of PUMB02 lipase. The dialyzed solution was purified with a fast-performance liquid chromatography (FPLC) system (BioRad) equipped with an anionic exchange (DEAESepharose) which was previously equilibrated with 50mM tris-HCl buffer (pH 7.4). The column was washed with 50 ml of the buffer and then eluted with a linear gradient of 0 to 1.0 M sodium chloride (NaCl) in the same buffer. Linear flow rate was 0.5 ml/min and fractions were collected every 2.0 min. The lipase activity and protein concentration (A280) in each fraction were measured. (A) Butyl-sepharose anion exchange chromatography. (B) DEAEsephadex gel
Figure 5. MALDI-TOF analysis of the tryptic digest fingerprint of PUMB02 lipase predicting the peptide mass to be 31kDa. Lane a: zymogram of PUMB02 lipase; Lane b: crude protein; Lane c: purified protein after size-exclusion chromatography; Lane d: molecular weight markers
Figure 8. Phase contrast microscopic images showing antibiofilm effect of lipases against biofilm forming pathogens at their BIC
Figure 9. Confocal microscope images showing biofilm inhibition effect of lipases against biofilm forming pathogens
