Catalytic properties of immobilized tannase produced from Aspergillus aculeatus compared with the free enzyme

El-Tanash, A. B.; Sherief, A.A.; Nour, Alshaymaa

doi:10.1590/s0104-66322011000300004

Cited by 34 publications

(21 citation statements)

References 30 publications

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“…The presence of chelator EDTA and surfactants also inhibited the tannase from Paecilomyces variotii and Aspergillus aculeatus (11,48). Considering that the use of certain compounds can be advantageous in various industrial enzymatic processes, the resistance of enzymes to this kind of compounds is desirable (37).…”

Section: Eff Ect Of Metal Ions and Other Chemicalsmentioning

confidence: 99%

Production, Characterization and Application of a Thermostable Tannase from Pestalotiopsis guepinii URM 7114

Sena¹,

Santos

Gouveia

et al. 2014

Food. Technol. Biotechnol.

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SummaryTannase (EC 3.1.1.20) is an enzyme that hydrolyzes the ester and depside bonds of tannic acid to gallic acid and glucose. In the production of foods and beverages, it contributes to the removal of the undesirable eff ects of tannins. The aim of this study is to investigate the potential of endophytic fungi isolated from jamun (Syzygium cumini (L.) Skeels) leaves, and identifi ed as Pestalotiopsis guepinii, in the production of tannase. Tannase was produced extracellularly by P. guepinii under submerged, slurry-state and solid-state fermentations. The submerged fermentation was found to be the most promising (98.6 U/mL). Response surface methodology was employed to evaluate the eff ect of variables (pH and temperature), and the results showed that the best conditions for tannase activity were pH=6.9 and 30 °C. K m was found to be 7.18·10 -4 mol/L and v max =250.00 U/mL. The tannase activity was the highest in the presence of Ca 2+ at a concentration of 5·10 -3 mol/L. Moreover, the enzyme was not inhibited by the tested chelators and detergents. The stability of the enzyme was also studied, and crude enzyme was evaluated in simulation of gastrointestinal digestion of monogastric animals. The crude enzyme was highly stable under simulated conditions; it retained 87.3 % of its original activity a er 6 h. The study contributes to the identifi cation of microbial species that produce tannase, with potential application in biotechnology.

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Section: Eff Ect Of Metal Ions and Other Chemicalsmentioning

confidence: 99%

Production, Characterization and Application of a Thermostable Tannase from Pestalotiopsis guepinii URM 7114

Sena¹,

Santos

Gouveia

et al. 2014

Food. Technol. Biotechnol.

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“…From the slope of the straight lines produced in the Arrhenius plots, activation energies of 4.55 and 3.34 kcal/mol were deduced for free and immobilized β-glucosidase, respectively. A lower activation energy for the immobilized enzyme has been reported to be an indication of diffusional limitations (Allenza, 1986;EL-Tanash et al, 2011). The activation energy of an enzyme reaction may or may not change as a consequence of the immobilization process.…”

Section: Enzyme Properties Temperature Profilementioning

confidence: 99%

“…The cost of β-glucosidase-based technology can be reduced by increasing the enzyme reusability and its stability (AbdEl-Ghaffar and Hashem, 2010). Immobilization of enzymes on a carrier offers significant cost benefits for industrial processes, because it facilitates enzyme recycling, enables improvements in thermo-stability (thereby reducing enzyme inactivation), and allows for greater control of enzyme activity (El-Tanash et al, 2011;Alkhatib et al, 2012). In addition, immobilization eliminates the need to separate an enzyme from the product solution and allow these expensive compounds to be reused (Mazzuce et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Biochemical studies on immobilized fungal β-glucosidase

Ahmed

El-Shayeb

Hashem

et al. 2013

Braz. J. Chem. Eng.

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-β-Glucosidase from Aspergillus niger was immobilized on sponge by covalent binding through a spacer group (glutaraldehyde). Sponge-immobilized enzyme had the highest immobilization yield (95.67%) and retained 63.66% of the original activity exhibited by the free enzyme. The optimum pH of the immobilized enzyme remains almost the same as for the free enzyme (pH 4.0). The optimum temperature for β-glucosidase activity was increased by 10 ºC after immobilization. The activation energy (E a ) of the immobilized β-glucosidase was lower than the free enzyme (3.34 and 4.55 kcal/mol), respectively. Immobilized β-glucosidase exhibited great thermal stability and retained all the initial activity after incubation at 55 ºC for 2 h; however, the free enzyme retained 89.25% under the same condition. The calculated half-life (t ½ ) value of heat inactivation of immobilized enzyme at 60, 65 and 70 ºC was 213.62, 72.95 and 56.80 min, respectively, whereas at these temperatures the free enzyme was less stable (half-life of 200.0, 55.31 and 49.5 min, respectively). The deactivation rate constant at 65 ºC for the immobilized β-glucosidase is 9.5x10 -3 / min, which was lower than that of the free form (12.53x10 -3 / min). The immobilization process improved the pH stability of the enzyme (immobilized and free enzyme retained 69.35 and 39.86%, respectively, of their initial activity after 45 min at pH 7.5). The effect of some chemical substances on the activity of the immobilized and free β-glucosidase has been investigated. In the presence of sodium dodecyl sulfate (SDS) and p-chloromercuri benzoate (p-CMB) the immobilized enzyme retained 36.13 and 45.34%, respectively, of the initial activity, which is higher than that of free enzyme (13.71 and 1.61%, respectively). The Michaelis constant (K m ) value of the free enzyme was 40.0 mM, while the apparent K m value for the immobilized enzyme was 46.51 mM. The maximum reaction rate (v max ) of immobilized β-glucosidase was smaller than that of the free enzyme by 7.69%. Sponge-immobilized β-glucosidase was repeatedly used to hydrolyze cellobiose (5 and 8 cycles with retained activity of 67.32 and 51.04%, respectively).

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“…However, entrapment into semi-permeable membrane capsule using sodium alginate is a cost effective common method that shows good performance in industrial applications (El-Tanash et al, 2011). Recently Yao et al (2014) studied different supports for tannase immobilization and found that entrapment in calcium alginate beads was the best method.…”

Section: Introductionmentioning

confidence: 99%

“…They reported that immobilized enzyme prepared by covalent binding to chitosan showed highest activity and Yield. Previous supports for tannase immobilization includes chitosan beads(Abdel-Naby et al, 1999), polyacrylamide, calcium alginate(Yao et al, 2014), concanavalin ASepharose(Sharma et al, 2002), Amberlite IR 1204(Sharma et al, 2008), sodium alginate(El- Tanash et al, 2011) and calcium alginate…”

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confidence: 99%