A novel bacteriocin with a broad inhibitory spectrum produced by Lactobacillus sake C2, isolated from traditional Chinese fermented cabbage

Food Control ◽  
2010 ◽  
Vol 21 (1) ◽  
pp. 76-81 ◽  
Author(s):  
Yurong Gao ◽  
Shiru Jia ◽  
Qiang Gao ◽  
Zhilei Tan
2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Sarah Wigley ◽  
George M Garrity
Keyword(s):  

2021 ◽  
Vol 22 (6) ◽  
pp. 3051
Author(s):  
Silvia López-Argüello ◽  
María Montaner ◽  
Antonio Oliver ◽  
Bartolome Moya

Avibactam belongs to the new class of diazabicyclooctane β-lactamase inhibitors. Its inhibitory spectrum includes class A, C and D enzymes, including P. aeruginosa AmpC. Nonetheless, recent reports have revealed strain-dependent avibactam AmpC induction. In the present work, we wanted to assess the mechanistic basis underlying AmpC induction and determine if derepressed PDC-X mutated enzymes from ceftazidime/avibactam-resistant clinical isolates were further inducible. We determined avibactam concentrations that half-maximally inhibited (IC50) bocillin FL binding. Inducer β-lactams were also studied as comparators. Live cells’ time-course penicillin-binding proteins (PBPs) occupancy of avibactam was studied. To assess the ampC induction capacity of avibactam and comparators, qRT-PCR was performed in wild-type PAO1, PBP4, triple PBP4, 5/6 and 7 knockout derivatives and two ceftazidime/avibactam-susceptible/resistant XDR clinical isolates belonging to the epidemic high-risk clone ST175. PBP4 inhibition was observed for avibactam and β-lactam comparators. Induction capacity was consistently correlated with PBP4 binding affinity. Outer membrane permeability-limited PBP4 binding was observed in the live cells’ assay. As expected, imipenem and cefoxitin showed strong induction in PAO1, especially for carbapenem; avibactam induction was conversely weaker. Overall, the inducer effect was less remarkable in ampC-derepressed mutants and nonetheless absent upon avibactam exposure in the clinical isolates harboring mutated AmpC variants and their parental strains.


1992 ◽  
Vol 16 (3) ◽  
pp. 215-225 ◽  
Author(s):  
Odón J. Sobrino ◽  
Juan M. Rodríguez ◽  
Wagner L. Moreira ◽  
Luis M. Cintas ◽  
María F. Fernández ◽  
...  
Keyword(s):  

1999 ◽  
Vol 62 (7) ◽  
pp. 773-777 ◽  
Author(s):  
GIANLUIGI MAURIELLO ◽  
MARIA APONTE ◽  
ROSAMARIA ANDOLFI ◽  
GIANCARLO MOSCHETTI ◽  
FRANCESCO VILLANI

Cell survival, cellular damage, and antagonistic activity were investigated after spray-drying of four bacteriocin-producing strains of lactic acid bacteria: Lactococcus lactis subsp. lactis 140, isolated from natural whey culture and producing a narrow-inhibitory spectrum bacteriocin); L. lactis subsp. lactis G35, isolated from pizza dough and producing nisin; Lactobacillus curvatus 32Y and Lactobacillus sp. 8Z, isolated from dry sausages. Trials were performed with bacteria suspended in skimmed milk or directly grown in whey. Three air temperatures at the inlet of the drier (160, 180, and 200°C) and three flow rates (10, 13, and 17 ml/min) were assayed. Cell viability and bacteriocin activity of the dried materials were determined immediately after the process and after 5, 15, 30, and 60 days of storage at 4°C. There was no significant difference between the two feeding suspensions in cell survival, always decreasing with the increase of inlet-air temperature. No loss of bacteriocin activity was detected in reconstituted powders, nor was any loss of ability to produce bacteriocin found after drying. Investigations of sensitivity to NaCl revealed only temporary damage to dried bacteria. During storage for 2 months at 4°C, all samples, but mainly the lactococcal strains, displayed a gradual decrease in cell survival. Bacteriocin activity remained at the same level, allowing powders to be considered as effective biopreservatives.


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