Cell Wall, Membrane, and Intracellular Peptidase Activities of Propionibacterium shermanii

作者: Stefan Sahlström , Cruz Espinosa , Thor Langsrud , Terje Sørhaug

DOI: 10.3168/JDS.S0022-0302(89)79115-3

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摘要: Abstract A procedure has been developed for the production of spheroplasts from Propionibacterium shermanii α and P. ATCC 9614. Thus, it was also possible to produce clean cell wall, membrane, intracellular fractions. The solubilized wall preparation nearly free markers; leakage aldolase malate dehydrogenase below .5% after 90min in lysozyme. purity homogeneity membrane fraction were visualized with electron micrographs. Polyacrylamide gel electrophoresis a zymogram technique used compare peptidases pure Fifteen dipeptides 2 tripeptides as substrates. Peptidases 9614 found (one band one band), (three bands two bands), fractions (six seven bands). contain reflectance values 0 57, respectively. 57 peptidase broad substrate specificity, that is slightly narrower. Among five appear be unique membranes, those 28 75. An specificity value 55 both strains. enzymes hydrolyzed most 15 enzyme tripeptides. 24/25 strains same, limited specificity. each strain all L-leucine-L-leucine-L-leucine, plus L-alanine-L-leucine-glycine

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