Isolation and partial characterization of a novel bacteriocin produced by Lactococcus lactis ssp lactis MC38

Date

2007-02-01

Author

Tukel, Cagla
Avsaroglu, M. Dilek
Simsek, Omer
Akcelik, Mustafa

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

69
views

0
downloads

This work presents the isolation and partial characterization of a new lactococcal bacteriocin produced by Lactococcus lactis ssp. lactis MC38. The bacteriocin demonstrated broad spectrum of inhibition activity against both pathogenic and food spoilage organisms, and various lactic acid bacteria. This antimicrobial substance appeared to be proteinaceous because its activity was completely inactivated by proteinase K and alpha-chymotrypsin. It was heat and pH stable. The apparent molecular mass of the purified bacteriocin, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was 8.0 kDa. The amino acid composition of the studied bacteriocin was found to be quite different from known lactococcal bacteriocins. The calculation of the number of amino acid residues in the bacteriocin molecule revealed that it contained 62 amino acids.

Subject Keywords

Food Science, Microbiology, Parasitology

URI

https://hdl.handle.net/11511/67689

Journal

JOURNAL OF FOOD SAFETY

DOI

https://doi.org/10.1111/j.1745-4565.2007.00056.x

Collections

Department of Food Engineering, Article

Suggestions

OpenMETU
Core

Analysis of the genetic determinant for production of the pediocin P of Pediococcus pentosaecus Pep 1 Osmanagaoglu, O; Beyatli, Y; Gündüz, Ufuk; Sacilik, SC (2000-01-01) Pediococcus pentosaceus Pep1 is a vacuum-packaged Turkish sausage isolate which produces a potentially novel bacteriocin of the pediocin (anti-Listeria) family of peptides designated as pediocin P. Curing experiments and plasmid profile analysis indicated that both bacteriocin immunity and production determinants were linked and encoded by 9.0 MDa plasmid, pHD1.0. Attempts to transform purified plasmid pHD1.0 into recipient Escherichia coli JM109 cells by electroporation were successful but none of the E. c...
Characterization of extracellular beta-lactamases from penicillin G-resistant cells of Streptococcus thermophilus Chirica, LC; Güray, Nülüfer Tülün; Gültekin, Güzin Candan; Bozoglu, F (International Association for Food Protection, 1998-07-01) In this study, biochemical properties of two extracellular beta-lactamases produced by penicillin-resistant Streptococcus thermophilus cells were investigated. Both beta-lactamases showed specificity for penicillins but not for cephaloridins. The p-lactamases exhibited different affinities for penicillin G. The one with the higher molecular weight (F1) had a K(m) value of 3.44 mu M and a V(max), value of 8.33, mu mol/min/mg of protein, whereas the beta-lactamase with the lower molecular weight (FII) had a K...
Evaluation of high hydrostatic pressure sensitivity of Staphylococcus aureus and Escherichia coli O157 : H7 by differential scanning calorimetry Alpas, Hami; BOZOGLU, F; KALETUNC, G (Elsevier BV, 2003-11-01) Differential scanning calorimetry (DSC) was used to evaluate the relative high hydrostatic pressure (HHP) resistances of bacterial strains from Staphylococcus aureus and Escherichia coli O157:H7 in vivo. The total apparent enthalpy change and thermal stability were two DSC parameters used to compare bacterial strains of untreated control and pressure-treated bacteria. DSC thermograms indicated that ribosomal denaturation appears to be a major factor in cell death by both thermal and high pressure treatments...
Purification and characterization of an intracellular chymotrypsin-like serine protease from Thermoplasma volcanium Kocabıyık, Semra (2006-01-01) An intracellular serine protease produced by Thermoplasma (Tp.) voleanium was purified using a combination of ammonium sulfate fractionation, ion exchange, and et-casein agarose affinity chromatography. This enzyme exhibited the highest activity and stability at pH 7.0, and at 50 degrees C. The purifed enzyme hydrolyzed synthetic peptides preferentially at the carboxy terminus of phenylalanine or leucine and was almost completely inhibited by PMSF, TPCK, and chymostatin, similarly to a chymotrypsin-like ser...
IDENTIFICATION AND CHARACTERIZATION OF AN INTRONIC TRANSCRIPT FOR IGFBP4 Yılmaz, Utku Cem; Erson Bensan, Ayşe Elif; Department of Molecular Biology and Genetics (2023-1-20) Alternative polyadenylation is a widespread mRNA processing event affecting the length of the 3’UTR of mRNAs. Alternative use of polyadenylation sites sometimes occurs in terminal exons, proximal exons, or proximal introns, affecting the coding 3’UTR length and even the coding sequence of the mRNA. To identify estrogen (E2) related polyadenylation changes by a 3’-seq experiment, we detected an early intronic polyadenylation site for IGFBP4 (insulin-like growth factor binding protein 4). In this thesis, I pr...

Citation Formats

C. Tukel, M. D. Avsaroglu, O. Simsek, and M. Akcelik, “Isolation and partial characterization of a novel bacteriocin produced by Lactococcus lactis ssp lactis MC38,” JOURNAL OF FOOD SAFETY, pp. 17–29, 2007, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/67689.