Fakher Frikha

Publications (38) View all

• Article: Surface behavior of α-synuclein and its interaction with phospholipids using the Langmuir monolayer technique: A comparison between monomeric and fibrillar α-synuclein.

  Ali Chaari, Habib Horchani, Fakher Frikha, Robert Verger, Youssef Gargouri, Moncef Ladjimi
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  ABSTRACT: Due to the involvement of α-Synuclein (α-Syn) in lipid transport and its role in the normal function and in the pathology of Parkinson disease, it is important to study first the surface properties of the protein at the air/water interface and second its behavior related to biological membranes. For this purpose, the monomolecular film technique was used as membrane model to compare the interactions with various phospholipids of monomeric and fibrillar forms of α-Syn. We have determined the apparent equilibrium surface pressure of the two forms of α-Syn (monomeric and fibrillar form) at the air/water interface. The surface pressures reached by monomeric α-Syn were shown to be higher than the ones of fibrillar α-Syn and similar to the value obtained by mellitin, a lytic peptide of bee venom, which has been described as "protein detergent". The monomeric α-Syn adsorbed more rapidly at the air/water interface with a maximal adsorption rate at least 60-times higher than the fibrillar form. In the presence of a phospholipid monolayer, the surface activities of two α-Syn forms are much greater than observed at the air/water interface. Also we can show that the fibrillar form of α-Syn have a higher value of critical pressure than the monomeric form for the cow brain extract and the Phospatidyl Glycerol (an anionic phospholipid) which confirm its higher affinity for the anionic phospholipid than the monomeric form. According these results, we can suggest that this aggregate form have important implications for the pathological activity and, therefore, for the associated neurotoxicity which can results in layer disruption and cell leakage.
  International journal of biological macromolecules 04/2013; · 2.37 Impact Factor
• Article: Decolorization and detoxification of two textile industry effluents by the laccase/1-hydroxybenzotriazole system.

  Ouafa Benzina, Dalel Daâssi, Héla Zouari-Mechichi, Fakher Frikha, Steve Woodward, Lassaad Belbahri, Susana Rodriguez-Couto, Tahar Mechichi
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  ABSTRACT: The aim of this work was to determine the optimal conditions for the decolorization and the detoxification of two effluents from a textile industry-effluent A (the reactive dye bath Bezactive) and effluent B (the direct dye bath Tubantin)-using a laccase mediator system. Response surface methodology (RSM) was applied to optimize textile effluents decolorization. A Box-Behnken design using RSM with the four variables pH, effluent concentration, 1-hydroxybenzotriazole (HBT) concentration, and enzyme (laccase) concentration was used to determine correlations between the effects of these variables on the decolorization of the two effluents. The optimum conditions for pH and concentrations of HBT, effluent and laccase were 5, 1 mM, 50 % and 0.6 U/ml, respectively, for maximum decolorization of effluent A (68 %). For effluent B, optima were 4, 1 mM, 75 %, and 0.6 U/ml, respectively, for maximum decolorization of approximately 88 %. Both effluents were treated at 30 °C for 20 h. A quadratic model was obtained for each decolorization through this design. The experimental and predicted values were in good agreement and both models were highly significant. In addition, the toxicity of the two effluents was determined before and after laccase treatment using Saccharomyces cerevisiae, Bacillus cereus, and germination of tomato seeds.
  Environmental Science and Pollution Research 01/2013; · 2.65 Impact Factor
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  Article: Heterologous expression and secretion of an antifungal Bacillus subtilis chitosanase (CSNV26) in Escherichia coli.

  Olfa Kilani-Feki, Fakher Frikha, Imen Zouari, Samir Jaoua
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  ABSTRACT: The aims of the study were the production improvement, the purification, the characterization and the activity investigation of chitosanase CSNV26 of Bacillus subtilis (V26). The gene csnV26 encoding for this protein was amplified and cloned in the pBAD vector then expressed in Escherichia coli (Top10). The SDS-PAGE and zymogram analysis of the recombinant protein showed that it has two active forms sized 27 and 31 kDa, corresponding to the protein with and without signal peptide. This protein has the particularity of being secreted by Top10-pBAD-csnV26 with a high yield of 6.2 g/l. The HPLC purification of CSNV26 from supernatant confirmed the presence of the two sizes. The investigation of the CSNV26 thermostability showed that the pure protein is highly stable keeping 68 % of its activity after 30-min treatment at 100 °C, contrarily to the protein present within the supernatant of E. coli and B. subtilis (V26). The molecular dynamics study of the predicted structure of protein in both forms showed that the presence of the peptide signal in the form of 31 kDa gave it a remarkable thermal stability. The antifungal activity of CSNV26 was evidenced on Rhizopus nigricans and Rhizopus oryzae. Indeed, it has provoked an alteration and embrittlement of their hyphae with onset of protoplast.
  Bioprocess and Biosystems Engineering 10/2012; · 1.81 Impact Factor
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  Article: Enzymatic transesterification of palm stearin and olein blends to produce zero-trans margarine fat.

  Mohamed Sellami, Hanen Ghamgui, Fakher Frikha, Youssef Gargouri, Nabil Miled
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  ABSTRACT: Food industries aim to replace trans fat in their products by formulations having equivalent functionality and economic viability. Enzymatic transesterification can be a technological option to produce trans free fats targeting commercial applications. Palm stearin and palm olein blends in different ratios were enzymatically transesterified in a solvent free system using a Rhizopus oryzae lipase immobilised onto CaCO3 to produce a suitable fat for margarine formulation. Slip melting points and triacylglycerols profiles were evaluated upon transesterification. Results indicated that all transesterified blends had lower slip melting points than their non transesterified counterparts. Furthermore, the triacylglycerols profile showed a decrease in the concentration of the high melting point triacylglycerols. The rheological analysis showed that margarine prepared with the transesterified blend showed a better spreadability than that of a control margarine prepared with non transesterified fat. Adding powder of dry bark orange to margarine preparation improved its colour and fairly affected its spreadability and rheological behaviour. The margarine prepared with transesterified fat displayed a rheological behaviour that was comparable to that of commercial sample. This study is an ecofriendly approach to the utilization of relatively low value bioresources like palm stearin and palm olein for making margarine free of trans fatty acids that are now implicated as risk factor for heart diseases.
  BMC Biotechnology 08/2012; 12:48. · 2.35 Impact Factor
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  Article: Alkaline xylanases from Bacillus mojavensis A21: production and generation of xylooligosaccharides.

  Anissa Haddar, Dorra Driss, Fakher Frikha, Semia Ellouz-Chaabouni, Moncef Nasri
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  ABSTRACT: Medium composition and culture conditions for the xylanases production by Bacillus mojavensis A21 were optimized using two statistical methods: Plackett-Burman design applied to find the key ingredients and conditions for the best yield of enzyme production and Box-Behnken design used to optimize the value of the four significant variables: barley bran, NaCl, agitation, and cultivation time. The optimal conditions for higher production of xylanases were barley bran 18.66 g/l, NaCl 1.04 g/l, speed of agitation 176 rpm and cultivation time 34.08 h. Under these conditions, the xylanase experimental yield (7.45 U/ml) closely matched the yield predicted by the statistical model (7.23 U/ml) with R² = 0.98. The medium optimization resulted in a 6.83-fold increase in xylanase production compared to that of the initial medium. Best xylanase activity was observed at the temperature of 50 °C and at pH 8.0. The enzyme retained more 96% of its activity after 24 h at pH ranges from 7.0 to 90.0. The enzyme preserved more 80% of its initial activity after 60 min of pre-incubation from 30 °C to 60 °C. The main hydrolysis products yielded from corncob extracted xylan were xylobiose and xylotriose, suggesting the good potential of strain A21 in xylooligosaccharides production.
  International journal of biological macromolecules 07/2012; 51(4):647-56. · 2.37 Impact Factor