Figure 3.

Thermal denaturation of PlyC. Top: The structural stability of the PlyC holoenzyme was assessed by incubating the endolysin at 1 mg/mL in PBS at temperatures ranging from 37 to 65 °C (left) or 42 to 48 °C (right) for 30 min. After heat treatment, the samples were cooled on ice and visualized via native PAGE. The absence of PlyC in wells corresponds to thermally induced protein unfolding and aggregation. Bottom: Lytic activity was normalized to unheated PlyC. +, ≥90% of unheated PlyC activity; −, ≤10% of unheated PlyC activity.