Enzymatic Formulation Capable of Degrading Scrapie Prion under Mild Digestion Conditions

摘要: The prion agent is notoriously resistant to common proteases and conventional sterilisation procedures. current methods known destroy infectivity such as incineration, alkaline thermal hydrolysis are harsh, destructive, environmentally polluting potentially hazardous, thus limit their applications for decontamination of delicate medical laboratory devices, remediation contaminated environment processing animal by-products including specified risk materials carcases. Therefore, an friendly, non-destructive enzymatic degradation approach highly desirable. A feather-degrading Bacillus licheniformis N22 keratinase has been isolated which degraded scrapie undetectable level PrPSc signals determined by Western Blot analysis. Prion was verified ex vivo cell-based assay. An formulation combining biosurfactant derived from Pseudomonas aeruginosa at 65°C in 10 min -. time-course analysis carried out 50°C over 2 h revealed the progressive attenuation intensity. Test residual standard cell culture assay confirmed that reduced levels compared cells challenged with untreated sheep (SSBP/1) (p-value = 0.008 95% confidence interval). This novel significant potential application various friendly systems under mild treatment conditions.