Characterisation of autolytic enzymes in Lactobacillus pentosus

dc.contributor.authorChartier, Marie Pierre Chapot
dc.contributor.buuauthorÇibik, Recep
dc.contributor.departmentUludağ Üniversitesi/Veteriner Fakültesi/Besi̇n Hi̇jyeni̇ ve Teknoloji̇si̇ Anabi̇li̇m Dalı.tr_TR
dc.contributor.scopusid56010542400tr_TR
dc.date.accessioned2022-04-21T06:23:36Z
dc.date.available2022-04-21T06:23:36Z
dc.date.issued2004
dc.description.abstractAims: To characterize autolysis and autolytic system of the lactic acid bacterium Lactobacillus pentosus. Methods and Results: Autolysis of nine Lact. pentosus strains was evaluated in buffer solution. Their peptidoglycan hydrolase profiles were examined by renaturing SDS-PAGE and revealed two major activity bands at 58 and 112 kDa. Specificity analysis indicated the presence of at least two different types of peptidoglycan hydrolase activities in Lact. pentosus 1091. Conclusions: Autolysis of Lact. pentosus was shown to be strain dependent and involvement of at least two different autolysins was evidenced. Significance and Impact of the Study: The autolytic system of Lact. pentosus was characterized for the first time and the data obtained could be used in the selection of strains of technological interest.en_US
dc.identifier.citationÇibik, R. ve Chartier, M. P. C. (2004). “Characterisation of autolytic enzymes in Lactobacillus pentosus”. Letters in Applied Microbiology, 38(6), 459-463.en_US
dc.identifier.endpage463tr_TR
dc.identifier.issn0266-8254
dc.identifier.issue6tr_TR
dc.identifier.pubmed15130139tr_TR
dc.identifier.scopus2-s2.0-2642540907tr_TR
dc.identifier.startpage459tr_TR
dc.identifier.urihttps://doi.org/10.1111/j.1472-765X.2004.01516.x
dc.identifier.urihttps://sfamjournals.onlinelibrary.wiley.com/doi/full/10.1111/j.1472-765X.2004.01516.x
dc.identifier.urihttp://hdl.handle.net/11452/25922
dc.identifier.volume38tr_TR
dc.identifier.wos000221256600003tr_TR
dc.indexed.pubmedPubMeden_US
dc.indexed.scopusScopusen_US
dc.indexed.wosSCIEen_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.relation.collaborationYurt dışıtr_TR
dc.relation.journalLetters in Applied Microbiologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBiotechnology and applied microbiologyen_US
dc.subjectMicrobiologyen_US
dc.subjectBacteria (microorganisms)en_US
dc.subjectLactobacillusen_US
dc.subjectLactobacillus pentosusen_US
dc.subjectPosibacteriaen_US
dc.subjectAutolysisen_US
dc.subjectNonstarter lactic acid bacteriaen_US
dc.subjectPeptidoglycan hydrolaseen_US
dc.subjectRenaturing SDS-PAGEen_US
dc.subjectLactic-acid bacteriaen_US
dc.subjectLactococcus-lactisen_US
dc.subjectCheeseen_US
dc.subjectStrainsen_US
dc.subjectIdentificationen_US
dc.subjectProteolysisen_US
dc.subjectPhenotypeen_US
dc.subjectProphageen_US
dc.subjectCheddaren_US
dc.subject.emtreeArticleen_US
dc.subject.emtreeAutolysisen_US
dc.subject.emtreeBacterial strainen_US
dc.subject.emtreeControlled studyen_US
dc.subject.emtreeEnzyme activityen_US
dc.subject.emtreeLactobacillusen_US
dc.subject.emtreeLactobacillus pentosusen_US
dc.subject.emtreeNonhumanen_US
dc.subject.emtreePolyacrylamide gel electrophoresisen_US
dc.subject.emtreeAutolysinen_US
dc.subject.emtreeBufferen_US
dc.subject.emtreeEnzymeen_US
dc.subject.emtreeHydrolaseen_US
dc.subject.emtreeLactic aciden_US
dc.subject.emtreePeptidoglycanen_US
dc.subject.meshBacteriolysisen_US
dc.subject.meshCarbohydratesen_US
dc.subject.meshDensitometryen_US
dc.subject.meshElectrophoresis, polyacrylamide gelen_US
dc.subject.meshFood microbiologyen_US
dc.subject.meshLactobacillusen_US
dc.subject.meshMolecular weighten_US
dc.subject.meshN-acetylmuramoyl-l-alanine amidaseen_US
dc.subject.meshSubstrate specificityen_US
dc.subject.scopusCheese Ripening; Cheese; Renneten_US
dc.subject.wosBiotechnology and applied microbiologyen_US
dc.subject.wosMicrobiologyen_US
dc.titleCharacterisation of autolytic enzymes in Lactobacillus pentosusen_US
dc.typeArticle

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