Solubilization of wall-bound peroxidases by limited proteolysis

Abstract

The cell wall residue, enriched in lignin, which was obtained from non-xylem tissues of flax stems after extensive digestion with the glycanase mixture, Driselase, had appreciable peroxidase activity which was tightly bound to the wall fragments. A portion of this residual activity was solubilized by limited proteolysis using trypsin. Non-denaturing gel electrophoresis of the trypsin-solubilized extracts revealed the presence of at least one highly mobile anionic peroxidase isozyme.