Driss Mountassif

Antibacterial activities of the crude ethanol extracts of medicinal plants against Listeria monocytogenes and some other pathogenic strains

Searches for substances with antimicrobial activity are frequent and medicinal plants have been considered interesting by some researchers since they are frequently used in popular medicine as remedies for many infectious diseases. The aim of this study was to verify the antibacterial effect of ethanol extracts of 13 plants (Artemisia Herba Alba, Lavandula officinalis L., Matricaria Chamomilla, Eugenia caryophylata , Cistus salvifolius, Mentha suaveolens subsp. Timija, Thymus serpyllum L., Lippia citriodora, Cinnamomum Zeylanicum, Rosa centifolia, Thymus vulgaris L, Rosmarinus officinalis and Pelargonium graveolens) against Listeria monocytogenes and other pathogenic strains. These plants are used more for their therapeutic effects in the aromatization of the traditionally fermented dairy products. For this purpose, the agar well diffusion method was the antimicrobial susceptibility performed test. The major components of extracts tested were identified by gas chromatography coupled with mass spectrometry (GC/MS) analysis. The obtained results revealed in vitro anti-Listeria monocytogenes activities of all the extracts. Also, the extracts of clove, mint timija, cinnamon, cistus, rose, thyme, wild thyme, artemisia, rosemary, geranium and camomile presented in this order promises inhibitory capacity with MIC value between 0.25 mg/mL for clove extract and 6.75 mg/mL for camomile extract. On the other hand, the antimicrobial activity was mainly a function of their chemical composition, in particular in the nature of their major volatile compounds. This study thus confirmed the possibility of using these plants or some of their components in food systems to prevent the growth of foodborne bacteria and to extend the shelf-life of processed foods.

Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis.

BackgroundThe interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions.ResultsPurifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the enzyme. This new procedure is based on the use of polyclonal antibodies raised against BDH from bacterial Pseudomonas aeruginosa. This study improves the procedure for purification of both soluble microbial and mammalian membrane-bound BDH. Even though the Jaculus orientalis genome has not yet been sequenced, for the first time a D-3-hydroxybutyrate dehydrogenase cDNA from jerboa was cloned and sequenced.ConclusionThis study applies immunoaffinity chromatography to purify BDH, the membrane-bound and lipid-dependent enzyme, as a 31 kDa single polypeptide chain. In addition, bacterial BDH isolation was achieved in a two-step purification procedure, improving the knowledge of an enzyme involved in the lipid metabolism of a unique hibernating mammal. Sequence alignment revealed conserved putative amino acids for possible NAD+ interaction.

Sensitivity of liver metabolism in jerboa (Jaculus orientalis) to ciprofibrate, a peroxisome proliferator

Ciprofibrate is a well-known drug used to normalize lipid parameters and fibrinogen in atherosclerosis patients. In laboratory rodents such as rats or mice, ciprofibrate exhibits peroxisome proliferator activity. However, to date, no clear alterations or side effects caused by ciprofibrate have been noted in humans. In order to further investigate such possible relationships, we studied the effects of sustained ciprofibrate treatment in jerboas (Jaculus orientalis). In these rodents, ciprofibrate does not induce hepatomegaly or promote liver cell DNA replication, confirming that this species more closely resembles humans than do rats or mice. The jerboas were treated daily with ciprofibrate at 3 mg/kg body weight for 4 weeks. Subcellular markers, clinical enzymes and enzymatic antioxidant defenses were then assessed. The results showed a strong decrease in peroxisomal catalase activity and an increase in the level of malondialdehyde (a stress biomarker). Moreover, ciprofibrate in vivo and in vitro inhibited D-3-hydroxybutyrate dehydrogenase, a mitochondrial enzyme of the ketone body interconversion that is important in redox balance (NAD+/NADH+H+ ratio). In conclusion, under these conditions, ciprofibrate induced alterations in the liver oxidative metabolism.