Mohamed Ali Borgi

Faculty of Science of Gafsa, Capsa, Gafsa, Tunisia

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Publications (8)16.43 Total impact

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    ABSTRACT: Phytases catalyze the hydrolysis of phytic acid in a stepwise manner to lower inositol phosphates, myo-inositol (having important role in metabolism and signal transduction pathways), and inorganic phosphate. These enzymes have been widely used in animal feed in order to improve phosphorus nutrition and to decrease pollution in animal waste. Compared to previously described phytases, the phytase (PhyL) from Bacillus licheniformis ATCC 14580 has attractive biochemical properties which can increase the profitability of several biotechnological procedures (animal nutrition, humain health…etc). Due to its amino acid sequence with critical substitutions, the PhyL could be a model to enhance other phytases features, in terms of thermal stability and high activity. Otherwise, an engineered PhyL, with low pH optimum, will represent a challenge within the class of β- propeller phytases.
    No preview · Article · May 2015
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    ABSTRACT: The phyL gene encoding phytase from the industrial strain Bacillus licheniformis ATCC 14580 (PhyL) was cloned, sequenced, and overexpressed in Escherichia coli. Biochemical characterization demonstrated that the recombinant enzyme has an apparent molecular weight of nearly 42 kDa. Interestingly, this enzyme was optimally active at 70-75 °C and pH 6.5-7.0. This enzyme is distinguishable by the fact that it preserved more than 40 % of its activity at wide range of temperatures from 4 to 85 °C. This new phytase displayed also a high specific activity of 316 U/mg. For its maximal activity and thermostability, this biocatalyst required only 0.6 mM of Ca(2+) ion and exhibited high catalytic efficiency of 8.3 s(-1) μM(-1) towards phytic acid.
    Full-text · Article · Dec 2013 · Applied Microbiology and Biotechnology
  • Mohamed A Borgi · Moez Rhimi · Adel Kadri
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    ABSTRACT: The crystallization behaviour of the highly thermostable glucose isomerase from the Streptomyces sp. strain isolated from Tunisian soil was investigated using ammonium sulfate as a precipitating agent. We established phase diagrams at different temperatures and protein concentrations. It was found that the solubility increased with increasing temperature and decreased with increasing salt concentration. The temperature-dependent solubility was used to characterize the thermodynamic parameters of crystallization such as enthalpy, entropy and free energy.
    No preview · Article · Oct 2013 · General Physiology and Biophysics
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    ABSTRACT: The implication of the original alanine 63 (Ala63) and the unique cysteine 306 (Cys306) residues in the thermostability of the Streptomyces sp. SK glucose isomerase (SKGI) were investigated by site-directed mutagenesis and homology modelling. The Cys306 to Ala mutation within SKGI dramatically affected its thermal stability by decreasing the half-life from 80 to 15 min at 90°C while the Ala63 to Ser replacement shifted this half-life to 65 min. The electrophoretic analysis proves that the residue Cys306 participates in oligomerization of the SKGI. Its stabilizing role is materialized by hydrogen bonds established with arginines at positions 284 and 259, as deduced from the constructed three-dimensional model. We have also shown that the presence of an Ala63 instead of Ser63 seems to be more suitable for enzyme thermostability by maintaining hydrophobic pocket that contributes to the protection of the enzyme active site.
    No preview · Article · Oct 2009 · Biologia
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    ABSTRACT: To develop a feasible enzymatic process for the concomitant d-tagatose and d-fructose production, the thermostable l-arabinose isomerase of Bacillus stearothermophilus US100 (l-AI US100) and the mutant d-glucose isomerase obtained from that of Streptomyces SK (SKGI-A103G) were successfully co-expressed in Escherichia coli HB101 strain. The recombinant cells were immobilized in alginate beads and showed, similarly to the free cells, optimal temperatures for d-galactose and d-glucose isomerisation of 80 and 85 °C, respectively. The two isomerases were optimally active at pH 7.5. Cell entrapment significantly enhanced the acidotolerance of the two isomerases, as well as their stability at high temperatures. To perform simultaneous isomerisation of d-galactose and d-glucose at 65 °C and pH 7.5 in packed-bed bioreactor, cells concentration, dilution rate, productivity and bioconversion rate were optimized to be 32 g/l, 2.6 h−1, 3 g/l h and 30%, respectively.
    No preview · Article · May 2007 · Enzyme and Microbial Technology
  • Mohamed Ali Borgi · Moez Rhimi · Samir Bejar
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    ABSTRACT: The Ala103 to Gly mutation, introduced within the glucose isomerase from Streptomyces sp. SK (SKGI) decreased its catalytic efficiency (k(cat)/K(m)) toward D-glucose from 7.1 to 3 mM(-1) min(-1). The reverse counterpart replacement Gly103Ala introduced into the glucose isomerase of Streptomyces olivochromogenes (SOGI) considerably improved its catalytic efficiency to be 6.7 instead of 3.2 mM(-1) min(-1). This later mutation also increased the half-life time of the enzyme from 70 to 95 min at 80 degrees C and mainly modified its pH profile. These results provide evidence that the residue Ala103 plays an essential role in the kinetic and physicochemical properties of glucose isomerases from Streptomyces species.
    No preview · Article · Feb 2007 · Biotechnology Journal
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    ABSTRACT: In order to over express the xylA gene of Streptomyces sp. SK strain, it was cloned under the control of the constitutive ermE-up promoter. This construct was integrated through site-specific recombination process into the chromosome of a Streptomyces violaceoniger glucose isomerase deficient strain using the non-replicative vector pTS55. The resulting CBS4 strain shows a perfect stability in the absence of selection pressure. Its glucose isomerase activity was about four and nine-fold greater, than that obtained from Streptomyces sp. SK, respectively fully induced or not by xylose.
    No preview · Article · Dec 2005 · Enzyme and Microbial Technology
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    ABSTRACT: The glucose isomerase gene (xylA) from the Streptomyces sp. SK strain encodes a 386-amino-acid protein (42.7 kDa) showing extensive identities with many other bacterial glucose isomerases. We have shown by gel filtration chromatography and SDS-PAGE analysis that the purified recombinant glucose isomerase (SKGI) is a 180 kDa tetramer of four 43 kDa subunits. Sequence inspection revealed that this protein, present some special characteristics like the abundance of hydrophobic residues and some original amino-acid substitutions, which distinguish SKGI from the other GIs previously reported. The presence of an Ala residue at position 103 in SKGI is especially remarkable, since the same amino-acid was found at the equivalent position in the extremely thermostable GIs from Thermus thermophilus and Thermotoga neapolitana; whereas a Gly was found in the majority of less thermostable GIs from Streptomyces. The Ala103Gly mutation, introduced in SKGI, significantly decreases the half-life time at 90 degrees C from 80 to 50 min and also shifts the optimum pH from 6.5 to 7.5. This confirms the implication of the Ala103 residue on SKGI thermostability and activity at low pH. A homology model of SKGI based on the SOGI (that of Streptomyces olivochromogenes) crystal structure has been constructed in order to understand the mutational effects on a molecular scale. Hence, the Ala103Gly mutation, affecting enzyme properties, is presumed to increase molecular flexibility and to destabilize, in particular at elevated temperature, the 91-109 loop that includes the important catalytic residue, Phe94.
    No preview · Article · Sep 2004 · Biochimie