Abstract
Proteolytic activity was determined in the soluble fraction of Lactobacillus bulgaricus cells. Maximum proteolytic activity was at pH 6.0 and 6.5 and at 45 C. Proteolytic activity in the soluble fraction was enhanced by iron ions (Fe^+2) and inhibited by EDTA. Activity toward some synthetic peptides indicated the presence of an exopeptidase, an iminopeptidase and a carboxypeptidase in the soluble fraction. Proteolytic enzymes in the soluble fraction were partially purified by affinity chromatography. The material isolated by affinity chromatography had proteinase activity and carboxypeptidase activity which was enhanced by iron ions (Fe^+2) and inhibited by EDTA. SDS gel electrophoresis of the isolated enzymes revealed three bands with molecular weights of 66,000, 52,000, and 42,000.
Chaparro-Serrano, Mildred (1985). Purification and characterization of proteolytic enzymes from Lactobacillus bulgaricus. Texas A&M University. Texas A&M University. Libraries. Available electronically from
https : / /hdl .handle .net /1969 .1 /DISSERTATIONS -439102.