Untersuchungen zum Enzymspektrum von Erysipelothrix rhusiopathiae

Abstract

The enzyme spectrum of non proliferating cells of Erysipelothrix rhusiopathiae was investigated by means of different low molecular synthetic substrates. Activities of aminopeptidases were found directed against compounds of L-alanine, L-arginine, L-aspartic acid, glycine, L-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-proline, L-tryptophane, and L-tyrosine, but not against compounds of L-cystine, L-glutaminic acid, L-histidine, L-hydroxyproline, and L-valine (Table 1). The pH optimum of the investigated aminopeptidases ranges from neutral to alcaline reaction (Table 2). Trypsine, chymotrypsine, or chymotrypsine-like proteases were not detected. E. rhusiopathiae possess esterase activity splitting esters of lower carboxylic acids, i. e. acetic acid, propionic acid, butyric acid, caproic acid, and caprylic acid, but no lipase activity. Under the proved glycosidases only α- and β-D-galactosidase and glucosaminidase were positive. Weak activities of phosphatases and arylsulfatase were found also (Table 3).