e when yeasts on cheese surface had reached high counts of 6 5 ±

e. when yeasts on cheese BIIB057 manufacturer surface had reached high counts of 6.5 ± 0.2 × 106 CFU cm-2. From the amount added to the smear brine (5 × 103 CFU ml-1), Listeria counts of 1.4 ± 0.9 × 101 CFU cm-2 (first trial) and of 1.0 ± 0.6 × 102 CFU cm-2 (repetition) were recovered from the surface immediately after contamination. Listeria development was strongly affected by the surface flora applied for ripening. A decrease of Listeria counts below the detection limit of the method (< 3 CFU cm-2) was observed

for cheeses treated with complex consortia F or M supplemented with Debaryomyces hansenii selleck chemicals llc FAM14334 (Figure 4). Listeria could be recovered from cheese surface (~2000 cm2) with an enrichment procedure at the end of ripening (60 to 80 days), for both consortia. In contrast,

Listeria counts on control cheeses treated with the commercial culture OMK 704 increased to ca. 105 CFU cm-2 after one month (Figure 4). Figure 4 In situ inhibition of Listeria on cheese surface by complex consortia. Cheese surfaces were treated with smear brines (3.3% (w/v) NaCl), inoculated with either consortium F, consortium M or the defined commercial culture OMK 704 (control cheese). Two independent experiments were carried out for each treatment. Different symbols indicate different commercial cheese production. Smear brines were inoculated with Listeria innocua on day 7 and 8, at 5 × 103 CFU ml-1. Stars indicate times where Listeria counts were below the detection limit of the enumeration method (< 3 CFU cm-2;

dashed line). Discussion AZD9291 clinical trial To our knowledge, this work describes the first dynamic study of naturally developing anti-listerial cheese surface consortia. The monitoring of two complex consortia obtained from industrial productions was carried out with TTGE, a culture independent fingerprinting technique which enabled species-level detection of high-GC and low-GC bacteria in separate runs. Previous studies reported a broad range of biodiversity in smear consortia, with 2 to 15 bacterial species detected [2, 5, 22, 23]. High bacterial diversity was observed in consortium F, with 13 species detected at dominant level by culture independent analysis. The cultivation approach detected only 9 of the 13 species present at dominant level in consortium F, but enabled detection of 6 additional species present CYTH4 at subdominant level. TTGE is a semiquantitative approach with limited sensitivity compared to the cultivation approach. However, as fingerprinting technique, TTGE enabled to overcome the arbitrary selection exercised on the flora by the cultivation step, giving a more complete view of biodiversity at dominant level. The combined use of both approaches led to a detailed knowledge of biodiversity in cheese smear flora, as already observed by Feurer et al. and Mounier et al. [5, 24]. The identification strategy used in the present study for the cultivation approach, i.e.

Recently mutations in the phospholipid biosynthesis genes cardiol

Recently mutations in the phospholipid biosynthesis genes cardiolipin synthase (cls2) and CDP-diacylglycerol-glycerol-3-phosphate 3 phosphatidyltransferase (pgsA) have been found in clinical DNS strains [17]. Another altered

protein sometimes found in DNS strains is YycG, which is one of two components of a response regulator system involved in the metabolism of the cytoplasmic membrane and cell wall [11]. The proteins RpoB and RpoC, which comprise the β and β′ subunit of RNA polymerase, have also been found with amino acid substitutions in DNS S. aureus strains Cytoskeletal Signaling inhibitor [11]. Recently, a single nucleotide polymorphism in rpoB from a laboratory derived DNS S. aureus was associated with decreased negative surface charge, increased cell wall Bcr-Abl inhibitor thickness, and both vancomycin and daptomycin heteroresistance [18]. Additionally, increased expression of the dltABCD operon increases d-alanylation of cell wall teichoic acids contributing to an increase in positive surface charge [13]. CH5183284 clinical trial Recent work has also suggested membrane proteins may augment the bactericidal effects of daptomycin, and alteration or loss of these proteins may contribute to DNS [15]. It has also been proposed that changes in carotenoid biosynthesis in S. aureus can increase membrane rigidity and

contribute to increases in daptomycin MIC values [19]. Overall, DNS S. aureus strains show altered membrane potential, changes in membrane fluidity, increased positive membrane surface charge, and decreased membrane depolarization [10–15]. It is hypothesized that the increase Morin Hydrate in cytoplasmic membrane surface charge repels the active daptomycin-Ca2+ complex and therefore impedes interaction of daptomycin with the membrane [10, 20]. There are likely other genetic changes that contribute to DNS in S. aureus as strains exhibiting elevated MICs often have only some of the changes mentioned above [21–24].

There is still much room for discovery of novel cell membrane and genetic changes in DNS strains of S. aureus. We have observed that some of the S. aureus strains identified as DNS by the clinical microbiology laboratory at our institution using Microscan® (Dade Behring, Deerfield, IL, USA) were actually susceptible via broth microdilution following passage on antibiotic free agar or time being stored at −80 °C. This observation led us to question the stability of these isolates. Additionally, previous in vitro work we have done with DNS strains has demonstrated variable activity of daptomycin [25, 26]. In some cases, daptomycin regimens of 10 mg/kg per day maintain antibacterial activity and led us to hypothesize that some S.

25 μg/23 75 μg) PFGE-RFLP (Pulsed-Field Gel Electrophoresis – RF

25 μg/23.75 μg). PFGE-RFLP (Pulsed-Field Gel Electrophoresis – RFLP) Genomic DNA was prepared in agarose plugs as previously described [28] and digested at 37°C with 40 U of SpeI (New England Biolabs). SpeI fragments were

separated by PFGE using www.selleckchem.com/products/4egi-1.html a CHEF-DRII apparatus (Bio-Rad, Laboratories) in a 1% agarose gel in 0.5× Tris-Borate-EDTA buffer (TBE) at 150 V and at 10°C. Pulse ramps were 5 to 35 s for 35 h followed by 2 to 10 s for 10 h. Molecular weight marker was a concatemer of phage l (New England Biolabs). The strains were randomly distributed among the SRT2104 nmr different gels. SpeI-digested DNAs from strains ADV48 and ADV90 were respectively loaded in the first and the last well on each gel in order to standardize the migration patterns. Fingerprinting profiles generated by PFGE were standardized with PhotoCapt® software (Vilbert Lourmat). The automated band detection was visually checked. The profiles were scored for the AZD8931 supplier presence or absence of DNA

bands. Restriction fragment variability was determined by the Nei and Li distance method modified by using the RESTDIST program in the Phylip package v.3.66 [29]. Clustering was predicated by the unweighted pair group average method (UPGMA) using the SplitsTree v4.0 [30, 31]. Gene amplification and sequencing Genomic DNA was obtained using the Aquapure DNA extraction kit (EpiCentre). Seven genes (dnaK, recA, rpoB, trpE, aroC, omp25 and gap) were amplified using the PI-1840 primers shown in Table 3. PCR was carried out in 50 μL of reaction mixture containing 200 nM (each) primer (Sigma Genosys), 200 μM (each) desoxy-nucleoside triphosphates (dNTP) (Euromedex), 2.5 U of Taq DNA polymerase (Promega) in the appropriate reaction buffer and 50 ng of genomic DNA as the template. Amplification conditions were as follows: initial denaturation of 3 min at 95°C followed by 35-cycles with 1 min at

94°C, 1 min at 60°C (for dnaK, rpoB recA and gap fragments) or 1 min at 65°C (for trpE, aroC and omp25 fragments) and 2 min 30 s at 72°C. The final extension was carried out at 72°C during 10 min. PCR products and molecular weight marker (phage phiX DNA digested with HaeIII, New England Biolabs) were separated in 1.5% (w/v) agarose gel in 0.5× TBE buffer. Amplification products were sequenced in both direction using forward and reverse sequencing primers (Table 3) on an ABI 3730xl automatic sequencer (Cogenics, France). The sequences were deposited to GenBank database with accession numbers: GQ429327 to GQ429816. Table 3 Primers used for genes amplification and sequencing.

Additional bands of different intensity, not detected in the S m

Additional bands of different intensity, not detected in the S. meliloti total RNA, corresponding to RNA species smaller than the full-length transcripts PND-1186 mouse were also visible when CoIP RNA was hybridized to SmrC9, SmrC16 and SmrC45 probes. A recent report addressing the stability of the seemingly homologous SmrC15 and SmrC16 sRNAs in a S. meliloti 2011 Δhfq mutant suggested that Hfq protects both full-length transcripts from degradation and stabilises degradation products corresponding

Sotrastaurin supplier specifically to the 3′-half of SmrC16 [29]. Our results corroborate that both, SmrC15 and SmrC16 sRNAs do bind Hfq and also suggest that the major band detected by the SmrC16 probe could correspond to a degradation product of this transcript interacting with a particular high efficiency with the protein. Nonetheless, the identity of this SmrC16-derived product remains controversial since the probe used in our study hybridizes to the 5′-half JAK inhibitor rather than to the 3′-end of the full-length transcript. Thus, further verifications should be carried out to elucidate this apparent contradiction. Similarly, the additional

faint hybridization bands detected with SmrC9 and SmrC45 probes could be interpreted as corresponding to degradation products of these sRNAs retaining a less efficient binding capacity to Hfq than the full-length transcripts. Figure 7 Binding of S. meliloti sRNAs to a FLAG-epitope

tagged Hfq protein. Western-blot showing the specific recognition of the chromosomally encoded 3 × FLAG tagged Hfq protein by ANTI-FLAG M2® monoclonal antibodies in total protein extracts of two independent 1021hfq FLAG strains (i.e. two different clones arising from the second cross-over event) (left panel); and Northern analysis of CoIP RNA from the 1021hfq FLAG and wild-type strains for the detection of the Smr sRNAs (right panel). Lane 1 shows the expression pattern of the corresponding sRNAs in the wild-type strain. Discussion There is increasing evidence that the ubiquitous RNA chaperone Hfq acts as a global post-transcriptional regulator controlling gene networks underlying key steps in the interactions of pathogenic bacteria with their eukaryotic hosts [41]. However, why its role in beneficial host-microbe interactions had not been investigated in detail. Here, we have genetically addressed the function of Hfq in the nitrogen-fixing endosymbiont S. meliloti, both as free-living bacterium and during the symbiotic interaction with its legume host alfalfa. As summarized in the model shown in Fig. 8, our results suggest the involvement of Hfq in bacterial pathways affecting central metabolism, rhizospheric competence, survival within the nodule cells and symbiotic nitrogen fixation.

The MICs of purified native EntA from E faecium T136 against Lis

The MICs of purified native EntA from E. faecium T136 against Listerias ranged from 40 to 120 ng/ml [34]. Similarly, rEntA also showed a narrow antibacterial spectrum (Table 1) including L. ivanovii ATCC19119, and with a low MIC value of 20 ng/ml, it is approximately 20-fold lower than that of ampicillin (390 ng/ml). The re-growth after MVL achievement was a common phenomenon

when the Listeria was treated with bacteriocins such as EntA, pediocin, sakacin A and enterococcin EFS2 in relatively low concentrations (1× or 2 × MIC) [3], but we found no re-growth after MVL within 10 h learn more when 4 × MIC rEnA was used with the Listeria (Figure 3), indicating that higher concentrations of rEnA are essential to inhibit the multiplication of Listeria. The bactericidal activity and overall structure of Pediocin PA-1 and piscicolin 126

were well maintained at higher temperatures [35,36]. The native EntA was stable at 100°C and acidic pH conditions [37]. We found that rEntA also exhibited high stability under a wide range of temperatures (37–80°C) and pH levels (2–8) (Figure 4). These properties were potentially due to the higher cysteine content of the antimicrobial peptides [38], similar to the EntA containing four cysteine residues. In addition, the antimicrobial activity of some bacteriocins (nisin, sakacin P and curvacin A) was significantly enhanced with the addition of NaCl from 0 to 1.17 M [39]. However, the activity of rEntA against Listeria was enhanced only at low NaCl concentrations (25 and 50 mM). Despite the unknown mechanisms PI3K inhibitor of the above differential Selleckchem Compound C effects, the high stability of rEntA over wide ranges of temperature, pH, and NaCl concentration supports its use as a food preservative and drug candidate. Due to the high content of basic and aromatic amino acids in class IIa bacteriocins, pediocin PA-1, enterocin B, plantaricin 423

and native EntA were very sensitive to the digestive proteases trypsin and pepsin [11,40,41]. Similarly, the purified rEntA, with 12.76% basic amino acids and 10.63% aromatic amino acids, was inactivated with trypsin and pepsin (Figure 4C). This high sensitivity to digestive proteases of rEntA contributes to its safety in foods and drugs, DOK2 during and after oral administration. Conclusion In conclusion, rEntA, as an antimicrobial agent with merit, could selectively kill important and pathogenic Listeria and retain bio-activity over a wide range of pH values, temperature and NaCl concentrations. These excellent antibacterial properties make it a potential candidate as a food preservative and therapeutic antimicrobial agent. rEntA was successfully expressed in P. pastoris X-33 at the highest level of 51,200 AU/ml and was purified through a gel filtration column. This yeast system may be a feasible technological approach to produce rEntA as a potent anti-Listeria agent after further optimization.

Moreover, induced Akt activity (p-AKT) (due to overexpression) is

Moreover, induced Akt activity (p-AKT) (due to overexpression) is sufficient to block apoptosis triggered by many death stimuli Crenolanib in vitro [5]. p53 has an important protective role against undesired cell proliferation. As such, p53 has been described as the “guardian of the genome”. The p53 protein is a transcription

factor that normally inhibits cell growth and stimulates cell death in response to myriad stressors, including DNA damage (induced by either UV or chemical agents such as hydrogen peroxide), oxidative stress, and deregulated oncogene expression [6–10]. p53 activation is characterized by a drastic increase and its rapid accumulation in stressed cells [11]. p53 is a master gene regulator controlling diverse cellular pathways, by either activating or repressing downstream genes. Among such genes, there is also the selleck compound proto-oncogene c-myc, which is negatively regulated by p53 [12]. The c-myc proto-oncogene encodes the c-myc transcription factor, BAY 73-4506 and was originally identified as the cellular homologue to the viral oncogene (v-myc) of the avian myelocytomatosis retrovirus [13, 14]. More recently, elevated or deregulated expression of c-myc has been detected in a wide range of human cancers, and is often associated with aggressive, poorly differentiated tumours [15, 16]. One of

the key biological functions of c- myc is its ability to promote cell-cycle progression [17–19] by repressing genes as the cyclin-dependent kinase inhibitors p21/WAF1 (p21) and p27Kip1 (p27), which are involved in cell-cycle arrest [20–22]. Cell division relies on the activation of cyclins, which bind to cyclin-dependent kinases to induce

cell-cycle progression towards mitosis. Following anti-mitogenic signals, p21 and p27 bind to cyclin-dependent kinase complexes to inhibit their catalytic activity and induce cell-cycle arrest [23]. Acceleration of tumorigenesis is observed when apoptosis is suppressed by overexpression of anti-apoptotic proteins such as Bcl2 [24]. When anti-apoptotic Bcl-2 family members are overexpressed, the ratio of FAD pro- and anti-apoptotic Bcl-2 family members is disturbed and apoptotic cell death can be prevented. Targeting the anti-apoptotic Bcl-2 family of proteins can improve apoptosis [25–27]. Apoptosis induction is arguably the most potent defence against cancer growth. Evidence suggests that certain chemopreventive agents can trigger apoptosis in transformed cells in vivo and in vitro, which appears to be associated with their effectiveness in modulating the process of carcinogenesis. In this study, we analyzed the effect of CF on 12 different cell lines showing that the nutraceutical has anti-cancer activity.

85 (0 81–0 90)  rs4122238 [13] 0 86 (0 81–0 91)  rs8192935 [13] 0

85 (0.81–0.90)  rs4122238 [13] 0.86 (0.81–0.91)  rs8192935 [13] 0.89 (0.85–0.93) Renal impairment [16]  Mild 1.50 (0.78–2.90)  Moderate 3.15 (1.63–6.08)

 Severe 6.31 (3.54–11.25) AUC 0–∞ area under the concentration-time curve from zero to infinity, CES1 carboxylesterase-1, NA not available, P-gp P-glycoprotein aThis represents the mean ratio of the AUC0–∞ of individuals with the covariate to healthy controls without the covariate, or, for genetic polymorphisms, the mean ratio 4SC-202 molecular weight (95 % CI) of either peak (P-gp) or trough (CES1) concentrations of single allele carriers to wildtype bSteady-state dosing of clopidogrel has not been shown to significantly alter dabigatran AUC0–∞ [7] cMay be associated with decreased dabigatran AUC0–∞ [10] As dabigatran is mainly cleared by the kidneys (fraction excreted unchanged in urine of 0.8), renal function is a major determinant of dabigatran concentrations [15, 16]. Glucuronidation is responsible for the remaining 20 % of dabigatran

clearance [15, 17]. The dabigatran glucuronides are equipotent to dabigatran Fosbretabulin solubility dmso against thrombin, and appear to be primarily renally cleared [15, 17]. Hence, it has been recommended that maintenance dose rates of dabigatran etexilate should be adjusted to take renal function into account [5, 18]. The standard representation of renal function is the glomerular filtration rate (GFR) [19, 20]. The gold standard methods for determining GFR are based on the clearance of renally eliminated exogenous compounds Salubrinal solubility dmso [21]. However, as these are inconvenient for routine clinical use, several equations for estimating GFR based on the measurement of endogenous compounds are currently recommended [19, 20]. The Cockcroft–Gault (CG) equation [22], which uses the endogenous renal biomarker, creatinine, has been used for many years to gauge renal function in relation to drug dosing [23].

More recently, the Chronic Kidney Disease Epidemiology Collaboration (CKD-EPI) 2009 equation [24] was developed to using creatinine assays standardised against the isotope dilution mass spectrometry (IDMS) method, and has become one of the most commonly used GFR equations [25, 26]. Cystatin C is an alternative renal function biomarker that has received considerable attention [27]. Whereas creatinine assay standardisation was introduced in 2006, the first certified reference material (ERM-DA471/IFCC) for standardising cystatin C assays has only been available since 2010 [28]. Hence, while a multitude of cystatin C-based GFR equations have been developed over the years [29], only a few have employed assays that are traceable to ERM-DA471/IFCC [30, 31]. These include the CKD-EPI equations that feature cystatin C [30]. All GFR equations are expected to explain some of the variance in dabigatran concentrations.

Through the 12-μm pore membrane, the number of migratory si-SW199

Through the 12-μm pore membrane, the number of migratory si-SW1990 cells significantly decreased by 85% compared with SW1990 (Fig. 4A, B). si-BxPC3 showed similar reduction of invasion to ECMs (Fig. 4B). Figure 3 Effect of MUC5AC suppression on cell adhesion. (A) Cancer cells were seeded in 96-well plates coated with Matrigel, laminin and fibronectin. After 30 min incubation, adherent cells were quantified by MTT assay. A phase contrast photograph of SW-1990 shows the representative adhering cells to the well coated in finbonectin. Scale bar, 50 μm. (B) Quantitication of the effect of

MUC5AC downregulation on cell adhesion to Matrigel, laminin and fibronectin. Cell adhesion of si-SW1990 and si-BxPC3 learn more to ECM declined significantly compared with parental cells. Shown data are means ± SD. *; P < 0.05; **; P < 0.01; ***; P < 0.001. Figure 4 Effect of MUC5AC suppression on cell invasion. (A) Cell invasion through membrane filter coated with Matrigel was examined. 72

h later, invading cancer cells were stained by hematoxylin and counted under a microscope. A phase contrast photograph of SW-1990 shows the representative adhering cells to the well coated in finbonectin (arrows). Scale bar, 50 μm. (B) The number of invading si-SW1990 and si-BxPC3 was significantly Luminespib molecular weight lower compared to parental cells. Data shown are means ± SD. ***; P < 0.001. Suppression of MUC5AC reduced expression of integrins and production of MMP-3 and VEGF In order to clarify the underlying mechanisms of these properties, we examined the mRNA expression of molecules associated with cell adhesion and invasion by RT-PCR. No differences were seen between SW1990 and si-SW1990 with regard to mRNA expression of E-Cadherin, Snail, ZO-1, ZO-2, MMPs and integrins, whereas

mRNA expression levels of α3, α9, and β3 integrin, MMP-3 and VEGF had decreased in both of si-SW1990 as compared with SW1990. si-BxPC3 also exhibited lower mRNA expression of α3 integrin, Adenosine triphosphate MMP-3 and VEGF. No expression of VEGFR-2 and twist were detected (Fig. 5A). Next, we investigated production of MMP-3 and alpha 3-integrin proteins by cancer cells, resulting in higher expression level of these proteins by parental cells compared with MUC5AC suppressed cells (Fig. 5B). In addition, production of VEGF was significantly lower in the culture supernatant of si-SW1990 and si-BxPC3 (Fig. 5C). Having demonstrated that SW1990 and si-SW1990 cell express VEGFR-1 mRNA and produce VEGF, we finally examined phosphorylation of VEGFR-1 (p-VEGFR-1) and Erk1/2 on both cell lines by Nutlin-3a manufacturer western blot analysis. Fig. 5B showed that VEGF induced VEGFR-1 phosphorylation were higher in both of SW1990 and BxPC3 compared with si-SW1990 and si-BxPC3. Moreover, Erk 1/2 phosphorylation was strongly reduced in MUC5AC reducing cells.

GenBank accession numbers are provided as additional file 1 Table

GenBank accession numbers are provided as additional file 1 Tables S1 and S2. Table 4 Leptospira www.selleckchem.com/products/BAY-73-4506.html clusters identified using lfb1 sequence polymorphism. Clusters Serovars Reference Strains Collection isolates Clinical Samples (number of amplicons) % of PCR-diagnosed human cases (January 2008-February 2010) L.interrogans 1 Copenhageni/Pyrogenes 5 isolates Human GSK1210151A solubility dmso (60) and deer (2) 68.2% L.interrogans 2 Autumnalis/Australis/Lai no isolate Human (6) 6.8% L.interrogans 3 Bataviae no isolate Human (3) 3.4% L.interrogans 4 Canicola/Pomona 5 isolates Human

(2) and deer (3) 2.3% L.interrogans 5 Unidentified serovar 5 isolates Human (10) 11.4% L.borgpetersenii 1 Castellonis/Sejroe 4 isolates Human (7) and deer (1) 7.9% L.borgpetersenii 2 Hardjo-bovis 1 isolate Deer (6) 0% We also evaluated if the direct

sequencing of the secY diagnostic product [9] could confirm the existence of the different clusters identified using lfb1 polymorphism (Figure 2). The 202 bp PCR product could successfully be amplified and sequenced from DNA extracted from all isolates. Using DNA from clinical specimens, samples from both lfb1-deduced clusters of L. borgpetersenii were successfully amplified and sequenced, but only samples from 3 out of the 5 lfb1-deduced clusters of L. interrogans could be amplified (clusters L. interrogans 1, 4 and 5). However, samples from the two remaining clusters (clusters L. interrogans 2 and 3) were scarce (see Table 4) and had low Leptospira concentrations (see Table 2). secY products using DNA Epothilone B (EPO906, Patupilone) from these clinical specimens could not be generated, even using combinations of primers used for BIX 1294 mouse the MLST study [18] and for diagnosis [9]. However, the phylogeny deduced from a 174 bp alignment of the diagnostic secY product confirmed the clusters identified by both the MLST and lfb1 typing schemes. Strains from cluster L. interrogans 5 had sequences 100% identical to L. interrogans Hardjo-prajitno (strain Hardjoprajitno) and to L. meyeri serovar Perameles strain Bandicoot, a strain recently re-assigned to the species L. interrogans [25]. GenBank

accession numbers of the sequences generated and used in this study are provided as additional file 1 Tables S1 and S2. Figure 2 secY -derived phylogeny of New Caledonian isolates, clinical specimens and reference strains based on a 174 bp sequence polymorphism. Blue legends indicate reference strains, red legends indicate the putative unknown serovar. GenBank accession numbers are provided as additional file 1 Tables S1 and S2. MLST-deduced phylogeny DNA sequences retrieved from databases or sequenced from products successfully amplified were concatenated and allowed drawing a phylogeny of the New Caledonian isolates, together with reference strains (Figure 3). GenBank accession numbers of the sequences generated and used in this study are provided as additional file 1 Tables S1 and S2.

Int J Food Microbiol 2007, 114:342–351 PubMedCrossRef 11 Obodai

Int J Food BMN 673 chemical structure Microbiol 2007, 114:342–351.PubMedCrossRef 11. Obodai M, Dodd CER: Characterization of dorminant microbiota of a Ghanaian feremented milk product, nyarmie, by culture-and https://www.selleckchem.com/products/lcz696.html nonculture-based methods. J Appl Microbiol 2006, 100:1355–1363.PubMedCrossRef

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of starter cultures of Bacillus subtilis and Bacillus pumilus for fermentation of African locust bean (Parkia biglobosa) to produce Soumbala. Int J Food Microbiol 2004, 90:197–205.PubMedCrossRef 18. Glover RL, Abaidoo RC, Jakobsen M, Jespersen L: Biodiversity of Saccharomyces cerevisiae isolated

from a survey of pito production sites in various parts of Ghana. Syst Appl Microbiol 2005,28(8):755–761.PubMedCrossRef 19. Papalexandratou Z, Camu N, Falony G, De Vuyst L: Comparison of the bacterial species diversity of spontaneous cocoa bean fermentations carried out at selected Oxalosuccinic acid farms in Ivory Coast and Brazil. Food Microbiol 2011, 5:964–973.CrossRef 20. Adams MR: Safety of industrial lactic acid bacteria. J Biotechnol 1999, 68:171–178.PubMedCrossRef 21. Adams MR, Marteau P: On the safety of lactic acid bacteria from food. Int J Food Microbiol 1995, 27:263–264.PubMedCrossRef 22. FEEDAP Panel: opinion of the scientific panel on additives and products or substances used in animal feed on the updating of the criteria used in assessment of bacterial resistance to antibiotics of human and veterinary importance. EFSA J 2008, 732:1–15. 23. Mathur S, Singh R: Antibiotic resistance in food lactic acid bacteria: a review. Int J Food Microbiol 2005, 105:281–295.PubMedCrossRef 24. Temmermana R, Pot B, Huys G, Swings J: Identification and antibiotic susceptibility of bacterial isolates from probiotic products. Int J Food Microbiol 2003, 81:1–10.CrossRef 25. Kastner S, Perreten V, Bleuler H, Hugenschmidt G, Lacroix C, Meile L: Antibiotic susceptibility patterns and resistance genes of starter cultures and probiotic bacteria used in food. Syst Appl Microbiol 2006, 29:145–155.PubMedCrossRef 26.