The peptide hydrolase system of Lactobacillus reuteri.
Peptide hydrolase system of Lactobacillus reuteri CRL 1098, a lactic acid bacteria of sourdough origin, was investigated. This microorganism has a broad range of peptidases consisting of an active aminopeptidase, X-Prolyl-dipeptidylaminopeptidase, dipeptidase and tripeptidase. Aminopeptidase, iminopeptidase and endopeptidase are most likely located in the cytoplasmic fraction showing no detectable association with the cell membrane, while dipeptidase and tripeptidase are mainly associated with the latter fraction. The peptidases are metalloenzymes activated by Co2+ and inhibited by Cu2+, Hg2+, Cd2+ and by metal-complexing reagents. The aminopeptidase activity inhibited by EDTA can be restored by Mn2+ while that of di- and tripeptidase treated with 1,10-phenantroline can be restored by Zn2+ and Co2+, respectively.
Rollan
G
G
Centro de Referencia para Lactobacilos (CERELA) y Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Tucumán, Argentina. rollan@cerela.org.ar
Font de Valdez
G F
GF
D006863:Hydrogen-Ion Concentration; D007778:Lactobacillus / Q000201:enzymology*; D008666:Metalloendopeptidases / Q000378:metabolism; D010084:Oxidation-Reduction; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors; D013696:Temperature
D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D008666:Metalloendopeptidases