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See detailCharacterization of a novel chitinase from a moderately halophilic bacterium, Virgibacillus marismortui strain M3-23
Essghaier, Badiaa; Hedi, Abdeljabbar; Bajji, Mohammed et al

in Annals of Microbiology (2012), 62(2), 835-841

A new chitinase produced by the moderately halophilic bacterium Virgibacillus marismortui strain M3- 23 was identified and characterized. Distinguishable characteristics of high activity and stability at ... [more ▼]

A new chitinase produced by the moderately halophilic bacterium Virgibacillus marismortui strain M3- 23 was identified and characterized. Distinguishable characteristics of high activity and stability at different pH, temperatures and salinity of M3-23 chitinase are reported. Analysis of the catalytic domain sequence from the enzyme highlighted its relationship to glycosyl hydrolase family 18. Comparison of the deduced chitinase sequence from strain M3-23 to known chitinases from Bacillus species showed low similarity (82%), suggested its novelty. This is the first report of the characterization of chitinase from the species V. marismortui. The halo- and thermo-tolerant nature of the chitinolytic enzyme allows its potential use in agricultural and industrial applications. [less ▲]

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See detailThe influence of growth conditions on enterocin-like production by Enterococcus faecium CWBI-B1430 and Enterococcus mundtii CWBI-B1431 isolates from artisanal Peruvian cheeses
Aguilar Galvez, Ana Consuelo ULg; Guillermo Arciniegas, Sandra Denisse; Dubois Dauphin, Robin ULg et al

in Annals of Microbiology (2011), 61

Strains of Enterococcus faecium CWBI-B1430 and Enterococcus mundtii CWBI-B1431, isolated from artisanal-produced Peruvian cheeses, offer a broad potential application as food biopreservatives for heat ... [more ▼]

Strains of Enterococcus faecium CWBI-B1430 and Enterococcus mundtii CWBI-B1431, isolated from artisanal-produced Peruvian cheeses, offer a broad potential application as food biopreservatives for heat-processing treatments. The aim of this work was to optimize the production conditions and medium composition for the production of bacteriocin-like substances (BLIS). The kinetics of the BLIS production for both strains is a growth-associated process, and the maximum inhibitory activity for E. faecium CWBI-B1430 and E. mundtii CWBI-B1431 was achieved after 9 and 8 h of fermentation, respectively. Temperature, initial pH, oxygen level, and their interactions all influence BLIS production for both strains; this influence was specific for each strain. The bacteriocin gene expression in a 20.0-L fermentor confirms previous work carried out by fermentation in the flask; the first reports of expression revealed mundticin KS from E. faecium and enterocin P from E. mundtii. Both strains demonstrated antilisteria activity and were multi-producers of enterocin. Furthermore, the study with whey milk as an inexpensive source of fermentable carbohydrates indicated lower BLIS production than that obtained with M17LG broth. The short chain fatty acid (SCFA) analyses offer a new alternative use for both strains, as strains probiotic, for propionic acid production. [less ▲]

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See detailHigh salt-tolerant protease from a potential biocontrol agent bacillus pumilus M3-16
Essghaier, Badiaa; Bajji, Mohammed; Jijakli, Haissam ULg et al

in Annals of Microbiology (2009), 59(3), 553-558

In this paper, we investigate the characterization and evaluation of the antifungal protease activity from a halotolerant strain M3-16 of Bacillus pumilus, earlier isolated from a shallow salt lake in ... [more ▼]

In this paper, we investigate the characterization and evaluation of the antifungal protease activity from a halotolerant strain M3-16 of Bacillus pumilus, earlier isolated from a shallow salt lake in Tunisia. Protease enzyme was highly induced by the pathogen tested in vitro (27.4 U/ml). This is the first report on high salt-tolerant protease from B. pumilus, since it was active at high salinity (from 5 to 30% NaCl, w/v) as well as in the absence of salinity. This enzyme showed optimal activity at 60 °C and pH 8. At 80 °C and 30 min, the enzyme retained up to 91% and it showed stability over a wide pH range (from pH 5 to 11). The enzyme was found to be monomer with an estimated molecular mass of 31 kDa. The amino acid sequence showed high similarity (94%) to ATP-dependent protease from B. pumilus strain ATCC 7061. Thus, our alkaline thermostable and high salt-tolerant protease induced by a phytopathogenic fungus, could be useful for application in diverse areas such as biotechnology alimentary and agronomy industries. [less ▲]

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