Please use this identifier to cite or link to this item:
http://hdl.handle.net/11452/25922
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chartier, Marie Pierre Chapot | - |
dc.date.accessioned | 2022-04-21T06:23:36Z | - |
dc.date.available | 2022-04-21T06:23:36Z | - |
dc.date.issued | 2004 | - |
dc.identifier.citation | Çibik, 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.issn | 0266-8254 | - |
dc.identifier.uri | https://doi.org/10.1111/j.1472-765X.2004.01516.x | - |
dc.identifier.uri | https://sfamjournals.onlinelibrary.wiley.com/doi/full/10.1111/j.1472-765X.2004.01516.x | - |
dc.identifier.uri | http://hdl.handle.net/11452/25922 | - |
dc.description.abstract | Aims: 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.language.iso | en | en_US |
dc.publisher | Wiley | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.rights | Atıf Gayri Ticari Türetilemez 4.0 Uluslararası | tr_TR |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Biotechnology and applied microbiology | en_US |
dc.subject | Microbiology | en_US |
dc.subject | Bacteria (microorganisms) | en_US |
dc.subject | Lactobacillus | en_US |
dc.subject | Lactobacillus pentosus | en_US |
dc.subject | Posibacteria | en_US |
dc.subject | Autolysis | en_US |
dc.subject | Nonstarter lactic acid bacteria | en_US |
dc.subject | Peptidoglycan hydrolase | en_US |
dc.subject | Renaturing SDS-PAGE | en_US |
dc.subject | Lactic-acid bacteria | en_US |
dc.subject | Lactococcus-lactis | en_US |
dc.subject | Cheese | en_US |
dc.subject | Strains | en_US |
dc.subject | Identification | en_US |
dc.subject | Proteolysis | en_US |
dc.subject | Phenotype | en_US |
dc.subject | Prophage | en_US |
dc.subject | Cheddar | en_US |
dc.subject.mesh | Bacteriolysis | en_US |
dc.subject.mesh | Carbohydrates | en_US |
dc.subject.mesh | Densitometry | en_US |
dc.subject.mesh | Electrophoresis, polyacrylamide gel | en_US |
dc.subject.mesh | Food microbiology | en_US |
dc.subject.mesh | Lactobacillus | en_US |
dc.subject.mesh | Molecular weight | en_US |
dc.subject.mesh | N-acetylmuramoyl-l-alanine amidase | en_US |
dc.subject.mesh | Substrate specificity | en_US |
dc.title | Characterisation of autolytic enzymes in Lactobacillus pentosus | en_US |
dc.type | Article | en_US |
dc.identifier.wos | 000221256600003 | tr_TR |
dc.identifier.scopus | 2-s2.0-2642540907 | tr_TR |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi | tr_TR |
dc.contributor.department | Uludağ Üniversitesi/Veteriner Fakültesi/Besi̇n Hi̇jyeni̇ ve Teknoloji̇si̇ Anabi̇li̇m Dalı. | tr_TR |
dc.identifier.startpage | 459 | tr_TR |
dc.identifier.endpage | 463 | tr_TR |
dc.identifier.volume | 38 | tr_TR |
dc.identifier.issue | 6 | tr_TR |
dc.relation.journal | Letters in Applied Microbiology | en_US |
dc.contributor.buuauthor | Çibik, Recep | - |
dc.relation.collaboration | Yurt dışı | tr_TR |
dc.identifier.pubmed | 15130139 | tr_TR |
dc.subject.wos | Biotechnology and applied microbiology | en_US |
dc.subject.wos | Microbiology | en_US |
dc.indexed.wos | SCIE | en_US |
dc.indexed.scopus | Scopus | en_US |
dc.indexed.pubmed | PubMed | en_US |
dc.contributor.scopusid | 56010542400 | tr_TR |
dc.subject.scopus | Cheese Ripening; Cheese; Rennet | en_US |
dc.subject.emtree | Article | en_US |
dc.subject.emtree | Autolysis | en_US |
dc.subject.emtree | Bacterial strain | en_US |
dc.subject.emtree | Controlled study | en_US |
dc.subject.emtree | Enzyme activity | en_US |
dc.subject.emtree | Lactobacillus | en_US |
dc.subject.emtree | Lactobacillus pentosus | en_US |
dc.subject.emtree | Nonhuman | en_US |
dc.subject.emtree | Polyacrylamide gel electrophoresis | en_US |
dc.subject.emtree | Autolysin | en_US |
dc.subject.emtree | Buffer | en_US |
dc.subject.emtree | Enzyme | en_US |
dc.subject.emtree | Hydrolase | en_US |
dc.subject.emtree | Lactic acid | en_US |
dc.subject.emtree | Peptidoglycan | en_US |
Appears in Collections: | Scopus Web of Science |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Çıbık_Chapot_2004.pdf | 74.24 kB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License