Both bifidobacteria and clostridia are part of the natural gut microflora and while clostridia may be responsible for severe intestinal infections, bifidobacteria are probiotic microorganisms belonging to the most important prospective bacteria in the bowel. The antimicrobial activity of biochanin A was tested in vitro against six Bifidobacterium spp., and eight Clostridium spp. using the broth microdilution method. Biochanin A showed an inhibition against all clostridia in the range of minimum inhibitory concentrations (MIC) from 64 μg/mL (for Cl. clostridioforme, strains DSM 933 and I3) to 1,024 μg/mL (for Cl. perfringens, DSM 11778). No bifidobacteria were suppressed at four-fold higher concentration (MICs > 4,096) than MIC of Cl. perfringens. These results indicate selective growth inhibition of biochanin A and its potential use in antimicrobial prevention and/or protection.
2-Hydroxyphenazine (2-OH-PHZ) is an effective biocontrol
antibiotic
secreted by Pseudomonas chlororaphis GP72AN and is transformed from phenazine-1-carboxylic acid (PCA).
PCA is the main component of the recently registered biopesticide
“Shenqinmycin”. Previous research showed that 2-OH-PHZ
was better in controlling wheat take-all disease than PCA; however,
2-OH-PHZ production was low under natural conditions. Herein, we confirmed
that PCA induced reactive oxygen species in its host P. chlororaphis GP72AN and that the addition of DTT
improved PCA production by 1.8-fold, whereas the supplementation of
K3[Fe(CN)6] and H2O2 increased
the conversion rate of PCA to 2-OH-PHZ. Finally, a two-stage fermentation
strategy combining the addition of DTT at 12 h and H2O2 at 24 h enhanced 2-OH-PHZ production. Taken together, the
two-stage fermentation strategy was designed to enhance 2-OH-PHZ production
for the first time, and it provided a valuable reference for the fermentation
of other antibiotics.
In this study, ten anthra-, nine naphtho-, and five benzoquinone compounds of natural origin and five synthetic naphthoquinones were assessed, using an enzymatic in vitro assay, for their potential to inhibit cyclooxygenase-1 and -2 (COX-1 and COX-2), the key enzymes of the arachidonic acid cascade. IC₅₀ values comparable with COX reference inhibitor indomethacin were recorded for several quinones (primin, alkannin, diospyrin, juglone, 7-methyljuglone, and shikonin). For some of the compounds, we suggest the redox potential of quinones as the mechanism responsible for in vitro COX inhibition because of the quantitative correlation with their pro-oxidant effect. Structure-relationship activity studies revealed that the substitutions at positions 2 and 5 play the key roles in the COX inhibitory and pro-oxidant actions of naphthoquinones. In contrast, the redox mechanism alone could not explain the activity of primin, embelin, alkannin, and diospyrin. For these four quinones, molecular modeling suggested similar binding modes as for conventional nonsteroidal anti-inflammatory drugs (NSAIDs).
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