Characterization of Enterocin 1146, a Bacteriocin from Enterococcus faecium Inhibitory to Listeria monocytogenes

1992 ◽  
Vol 55 (7) ◽  
pp. 497-502 ◽  
Author(s):  
EUGENIO PARENTE ◽  
COLIN HILL

Enterococcus faecium DPC 1146 produces a bacteriocin, enterocin 1146, which is inhibitory to Listeria monocytogenes. Enterocin 1146 was produced in GM17 and in milk. The bacteriocin was partially purified by ammonium sulfate precipitation. Its molecular weight, estimated by SDS-PAGE, was 3.0 kDa. It could be stored at −20°C without loss of activity, but pH had a marked effect on enterocin 1146, which was more stable at both high (up to 120°C) and low temperatures (4°C) at pH 5 than at pH 7 and 9. The sensitivity of 57 strains belonging to 35 different species was studied using a critical dilution assay. L. monocytogenes and L. innocua were most sensitive; enterocin 1146 had a bactericidal effect on Listeria. Starter and nonstarter lactic acid bacteria (except Lactobacillus sake)were insensitive or relatively resistant to the bacteriocin. Genetic determinants for bacteriocin production and immunity do not appear to be plasmid borne.

1992 ◽  
Vol 55 (7) ◽  
pp. 503-508 ◽  
Author(s):  
EUGENIO PARENTE ◽  
COLIN HILL

Enterocin 1146, a bacteriocin produced by Enterococcus faecium. DPC1146, has a rapid bactericidal effect on Listeria in buffer systems, broth, and milk. In trypticase soy broth, increasing the bacteriocin dose and/or decreasing the pH extended the lag phase of Listeria innocua. A logarithmic relationship was found between response (as proportion of survivors or growth compared to a control) and dose. Increasing the inoculum level of the indicator reduced the effectiveness of enterocin 1146. Log-phase cells of L. innocua were more resistant than stationary-phase cells in both broth and buffer systems. In milk treated with 250 arbitrary units of enterocin 1146/ml and inoculated with 103 or 105 CFU/ml of Listeria monocytogenes Scott A, populations reached only 5–14% of the control after 24 h at 30°C, with numbers exceeding 107, while at 6°C a slow decrease in population was found.


LWT ◽  
2021 ◽  
Vol 141 ◽  
pp. 110954
Author(s):  
Roger Junges da Costa ◽  
Andresa Pereira da Silva ◽  
Renata Nobre da Fonseca ◽  
Silvia de Oliveira Hübner ◽  
Elen Silveira Nalério ◽  
...  

Author(s):  
Felipe Miceli Farias ◽  
Lúcia Martins Teixeira ◽  
Deyse Christina Vallim ◽  
Maria do Carmo de Freire Bastos ◽  
Marco Antônio Lemos Miguel ◽  
...  

2020 ◽  
Vol 17 (3) ◽  
pp. 241-254
Author(s):  
Yaqiong Zhang ◽  
Zhiping Jia ◽  
Yunyang Liu ◽  
Xinwen Zhou ◽  
Yi Kong

Background: Deinagkistrodon acutus (D. acutus) and Bungarus multicinctus (B. multicinctus) as traditional medicines have been used for hundreds of years in China. The venoms of these two species have strong toxicity on the victims. Objective: The objective of this study is to reveal the profile of venom proteins and peptides of D. acutus and B. multicinctus. Method: Ultrafiltration, SDS-PAGE coupled with in-gel tryptic digestion and Liquid Chromatography- Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS) were used to characterize proteins and peptides of venoms of D. acutus and B. multicinctus. Results: In the D. acutus venom, 67 proteins (16 protein families) were identified, and snake venom metalloproteinases (SVMPs, 38.0%) and snake venom C-type lectins (snaclecs, 36.7%) were dominated proteins. In the B. multicinctus venom, 47 proteins (15 protein families) were identified, and three-finger toxins (3FTxs, 36.3%) and Kunitz-type Serine Protease Inhibitors (KSPIs, 32.8%) were major components. In addition, both venoms contained small amounts of other proteins, such as Snake Venom Serine Proteinases (SVSPs), Phospholipases A2 (PLA2s), Cysteine-Rich Secreted Proteins (CRISPs), 5'nucleotidases (5'NUCs), Phospholipases B (PLBs), Phosphodiesterases (PDEs), Phospholipase A2 Inhibitors (PLIs), Dipeptidyl Peptidases IV (DPP IVs), L-amino Acid Oxidases (LAAOs) and Angiotensin-Converting Enzymes (ACEs). Each venom also had its unique proteins, Nerve Growth Factors (NGFs) and Hyaluronidases (HYs) in D. acutus, and Cobra Venom Factors (CVFs) in B. multicinctus. In the peptidomics, 1543 and 250 peptides were identified in the venoms of D. acutus and B. multicinctus, respectively. Some peptides showed high similarity with neuropeptides, ACE inhibitory peptides, Bradykinin- Potentiating Peptides (BPPs), LAAOs and movement related peptides. Conclusion: Characterization of venom proteins and peptides of D. acutus and B. multicinctus will be helpful for the treatment of envenomation and drug discovery.


1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.


Gene ◽  
2021 ◽  
Vol 777 ◽  
pp. 145459
Author(s):  
Tawsif Ahmed Kazi ◽  
Suranjita Mitra ◽  
Bidhan Chandra Mukhopadhyay ◽  
Sukhendu Mandal ◽  
Swadesh Ranjan Biswas

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