title: Autolytic phenotype of Lactococcus lactis strains isolated from traditional Tunisian dairy products.
abstract: OBJECTIVE
  To evaluate the autolytic properties of Lactococcus lactis strains isolated from artisan Tunisian dairy products, their peptidoglycan hydrolase content and their activity spectrum.
  
  
  RESULTS
  The autolytic phenotype of Lactococcus strains was evaluated under starvation conditions in potassium phosphate buffer. The results obtained highlighted a high degree of diversity among the strains analysed, allowing the identification of high and low autolytic Lactococcus lactis strains. Peptidoglycan hydrolase content was evaluated by renaturing SDS-PAGE using cells of Micrococcus lysodeikticus as a target for the enzymatic activity. A major activity band migrating at about 45 kDa was observed. The lytic activity, evaluated in the presence of different chemicals, was retained in 8% NaCl, 15 mmol l(-1) CaCl2, and in a pH range between 5 and 9.5. The substrate specificity of peptidoglycan hydrolase from Lactococcus strains was evaluated in renaturing SDS-PAGE incorporating cells of different bacterial species. The major autolysin of Lactococcus lactis was active against cells of Lactococcus lactis subsp. lactis, Streptococcus thermophilus, Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus helveticus and Listeria monocytogenes.
  
  
  CONCLUSIONS
  Autolytic activity is widely distributed in Lactococcus lactis and the rate of autolysis is strain-dependent. The major peptidoglycan hydrolase showed a wide spectrum of activity against several lactic acid bacteria and bacterial species involved in food-related infection.
  
  
  CONCLUSIONS
  The autolytic phenotype of Lactococcus lactis strains isolated from Tunisian artisan dairy products has been determined, and the data obtained should allow the selection of strains of technological interest in the cheese-ripening process.
authors.affiliation: Department of Food Science and Microbiology, University of Milano, Italy.
authors.forename: H
authors.initials: H
authors.lastname: Ouzari
authors.forename: A
authors.initials: A
authors.lastname: Cherif
authors.forename: D
authors.initials: D
authors.lastname: Mora
mesh_terms: D001433:Bacteriolysis; D003611:Dairy Products / Q000382:microbiology*; D010450:Endopeptidases / Q000378:metabolism; D013294:Lactococcus lactis / Q000145:classification* / Q000201:enzymology / Q000254:growth & development / Q000302:isolation & purification; D009113:Muramidase / Q000235:genetics; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D014416:Tunisia
chemical_list: C092497:AcmA protein, Lactococcus lactis; D009113:Muramidase; D010450:Endopeptidases; C021816:mutanolysin; D009238:N-Acetylmuramoyl-L-alanine Amidase