Abstract
Studies were carried out to clarify the biochemical characteristics of purified bacteriocin produced by Serratia marcescens strain K1.
Bacteriocin activity increased 100 to 1, 000 times in the course of purification by DEAF-cellulose column chromatography followed by sucrose density gradient ultracentrifugation.
The pigment of this microbe was separated from the bacteriocin by ultracentrifugation.
Purified bacteriocin was homogeneous on polyacrylamide gel electrophoresis in the presence of 2% sodium dodecyl sulfate.
The bacteriocin molecule was found to be of protein nature with a specific gravity of 1.046.
