Figures index

From

A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design

Catalina Kotlar, Sara Inés Roura, Alejandra Graciela Ponce

Journal of Polymer and Biopolymer Physics Chemistry. 2016, 4(1), 28-39 doi:10.12691/jpbpc-4-1-4
  • Figure 1. (A) Observed proteolytic activity versus predicted proteolytic activity from the empirical model (Y= x + 2E-15; R2 = 0.9935); (B) Plot of internally studentized residual versus predicted response
  • Figure 2. Pareto chart showing the effects of observed factors and their combined impact on the response (n=3)
  • Figure 3. Response surface plot (A) and its contour plot (B) of proteolytic activity by peptidase immobilized in cross-linked chitosan beads showing interaction between bead diameter and beads/ enzyme ratio. Other variables were held at zero level
  • Figure 4. Response surface plot and its contour plot of proteolytic activity by peptidase immobilized in cross-linked chitosan beads showing interaction between bead diameter and glutaraldehyde concentration. Other variables were held at zero level
  • Figure 5. Response surface plot and its contour plot of proteolytic activity by peptidase immobilized in cross-linked chitosan beads showing interaction between bead diameter and temperature. Other variables were held at zero level
  • Figure 6. Response surface plot and its contour plot of proteolytic activity by peptidase immobilized in cross-linked chitosan beads showing interaction between glutaraldehyde concentration and temperature. Other variables were held at zero level
  • Figure 7. Repeated use of immobilized peptidase showing the number of times the immobilized enzyme can be used (Y= -0.2435x + 1.2607; R2= 0.9891)