Purification and Characterization of an Endopeptidase from Propionibacterium freudenreichii
نویسندگان
چکیده
منابع مشابه
Purification and characterization of an endopeptidase from Lactococcus lactis
1 Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand * New Zealand Dairy Research Institute, Palmerston North, New Zealand An endopeptidase has been purified from Lactococcus lactis subsp. crernoris SK11. The enzyme is a 70 kDa monomer, strongly inhibited by the metalloproteinase inhibitors 1,l O-phenanthroline and phosphoramidon but relatively insensitiv...
متن کاملLipase and Esterase Activities of Propionibacterium freudenreichii subsp. freudenreichii.
The lipase and esterase activities of eight strains of dairy Propionibacterium freudenreichii subsp. freudenreichii were studied. A lipase activity was detected on whole cells and in the culture supernatant. The highest activity was expressed at 45 degrees C and pH 6.8. An esterase activity was also detected in the culture medium. The electrophoresis of the intracellular fractions of the cells ...
متن کاملMolecular and genetic characterization of propionicin F, a bacteriocin from Propionibacterium freudenreichii.
This work describes the purification and characterization of propionicin F, the first bacteriocin isolated from Propionibacterium freudenreichii. The bacteriocin has a bactericidal activity and is only active against strains of P. freudenreichii. Propionicin F appears to be formed through a processing pathway new to bacteriocins. The mass of the purified bacteriocin was determined by mass spect...
متن کاملAminopeptidase activities of Propionibacterium freudenreichii dairy isolates
This study was undertaken to achieve more information on the aminopeptidase activities expressed in Propionibacterium freudenreichii strains naturally occurring in milk and dairy products. Fifty four strains belonging to both subspecies freudenreichii and shermanii were analyzed for activity towards different amino acyl β-naphthylamide (βNA) derivatives. The ability to efficiently hydrolyze ami...
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ژورنال
عنوان ژورنال: Journal of Dairy Science
سال: 1996
ISSN: 0022-0302
DOI: 10.3168/jds.s0022-0302(96)76587-6