“…1 a demonstrate that as the temperature was raised to 65 °C, the relative enzymatic activity increased up to 152.7% (22.57 U/mg of specific activity), then gradually decreased to 143.0% (21.14 U/mg of specific activity), and finally reached 21.2% (3.14 U/mg of specific activity) at 80 °C. As mentioned by Wan, et al 24 , The optimal temperature of tannase from K. pneumoniae MTCC 7162 and A. niger NL112 was found to be 40 °C and 45 °C, respectively. Figure 1 Temperature profile of partially purified tannase from A. niger A8 + T. viride utilizing pomegranate peels with SSF technique.…”
“…In addition, Ma et al 40 found that A. ficuum Gim 3.6 tannase-specific activity after purification was 2.74-fold, with an enzyme activity recovery of 77.1%. In addition, Wan et al 24 mentioned that A. niger NL112 tannase specific activity of 57.96 U/mg proteins with a purification of 5.1-Fold. While tannase-specific activity was found to be 9.55 U/mg protein of the pure tannase from A. awamori 41 and 10.22 U/mg protein of the pure tannase from A. niger 42 .…”
Section: Resultsmentioning
confidence: 99%
“…The optimum temperature for tannase activity and stability: The enzyme was characterized by the following of Wan, et al 24 . The optimal temperature was found by assessing activity at optimum pH with varying temperature degrees (25, 37, 40, 45, 50, 55, 60, 70, 75, and 80 °C) for 10 min.…”
Bioconversion using fungi, as natural factory of many applicable bioactive compounds, as enzymes utilizing agro-residue substrates as a solid, abundant, low-cost growth and enzyme production media. This study characterized and applied a tannase enzyme (308 U/mg) from Aspergillus niger A8 + Trichoderma viride co-cultures utilizing pomegranate peels. The partially purified enzyme showed maximal relative activity at 37–65 °C for 10 min and kinetics of thermal inactivation energy at a high point at 60 °C for 0.040/min. The half-life was 37 °C for 58.6 min, temperature coefficient Q10 of tannase was maximal for 1.38 between 40 and 50 °C, and the activation energy was 17.42 kJ/mol. The enzyme activity peaked in the pH range of 4–8, and the maximum relative activity (100.6%) for tannase was achieved at pH 6. The Km and Vmax values for purified enzymes using tannic acid were 7.3 mg/mL and 3333.33 U/mL, respectively. The enzyme reduced the total tannin content in all tannin-rich substrates after 12h. The gallic acid (GA) had total phenols of 77.75 ppm and antioxidant activity of 82.91%. It was observed that the GA as antimicrobial influencer exhibited the largest inhibitory zone diameter (IZD) of 31 ± 1.0 mm against Pseudomonas aeruginosa ATCC27853. The GA minimum inhibitory concentration value was ranged from 7770.0–121.41 µg/mL. The obtained GA showed a bactericidal effect against all bacterial strains except Shigella sonnei DSM5570 and Salmonella typhi DSM17058, which showed bacteriostatic behavior.
“…1 a demonstrate that as the temperature was raised to 65 °C, the relative enzymatic activity increased up to 152.7% (22.57 U/mg of specific activity), then gradually decreased to 143.0% (21.14 U/mg of specific activity), and finally reached 21.2% (3.14 U/mg of specific activity) at 80 °C. As mentioned by Wan, et al 24 , The optimal temperature of tannase from K. pneumoniae MTCC 7162 and A. niger NL112 was found to be 40 °C and 45 °C, respectively. Figure 1 Temperature profile of partially purified tannase from A. niger A8 + T. viride utilizing pomegranate peels with SSF technique.…”
“…In addition, Ma et al 40 found that A. ficuum Gim 3.6 tannase-specific activity after purification was 2.74-fold, with an enzyme activity recovery of 77.1%. In addition, Wan et al 24 mentioned that A. niger NL112 tannase specific activity of 57.96 U/mg proteins with a purification of 5.1-Fold. While tannase-specific activity was found to be 9.55 U/mg protein of the pure tannase from A. awamori 41 and 10.22 U/mg protein of the pure tannase from A. niger 42 .…”
Section: Resultsmentioning
confidence: 99%
“…The optimum temperature for tannase activity and stability: The enzyme was characterized by the following of Wan, et al 24 . The optimal temperature was found by assessing activity at optimum pH with varying temperature degrees (25, 37, 40, 45, 50, 55, 60, 70, 75, and 80 °C) for 10 min.…”
Bioconversion using fungi, as natural factory of many applicable bioactive compounds, as enzymes utilizing agro-residue substrates as a solid, abundant, low-cost growth and enzyme production media. This study characterized and applied a tannase enzyme (308 U/mg) from Aspergillus niger A8 + Trichoderma viride co-cultures utilizing pomegranate peels. The partially purified enzyme showed maximal relative activity at 37–65 °C for 10 min and kinetics of thermal inactivation energy at a high point at 60 °C for 0.040/min. The half-life was 37 °C for 58.6 min, temperature coefficient Q10 of tannase was maximal for 1.38 between 40 and 50 °C, and the activation energy was 17.42 kJ/mol. The enzyme activity peaked in the pH range of 4–8, and the maximum relative activity (100.6%) for tannase was achieved at pH 6. The Km and Vmax values for purified enzymes using tannic acid were 7.3 mg/mL and 3333.33 U/mL, respectively. The enzyme reduced the total tannin content in all tannin-rich substrates after 12h. The gallic acid (GA) had total phenols of 77.75 ppm and antioxidant activity of 82.91%. It was observed that the GA as antimicrobial influencer exhibited the largest inhibitory zone diameter (IZD) of 31 ± 1.0 mm against Pseudomonas aeruginosa ATCC27853. The GA minimum inhibitory concentration value was ranged from 7770.0–121.41 µg/mL. The obtained GA showed a bactericidal effect against all bacterial strains except Shigella sonnei DSM5570 and Salmonella typhi DSM17058, which showed bacteriostatic behavior.
“…In the three purification steps, DEAE-IEC played a critical role in obtaining highly purified tannase. 30 The purity of the two tannases obtained after purification was analyzed by SDS-PAGE (Fig. 1).…”
Section: Resultsmentioning
confidence: 99%
“…The results showed that the activity of tannase from NCUF M8 after purification was 1230.37 U mg −1 , and the purification factor was 17.52, with 35.95% recovery of yield (Supporting Information, Table S2); activity of tannase from NCUF FCYN212 after purification was 864.53 U mg −1 , and the purification factor was 22.83, with 35.37% recovery of yield (Supporting Information, Table S2). In the three purification steps, DEAE‐IEC played a critical role in obtaining highly purified tannase 30 …”
Background
The presence of inorganic pollutants and heavy metals in industrial effluents has become a serious threat and environmental issues. Fungi have a remarkable ability to exclude heavy metals from wastewater through biosorption in eco-friendly way. Tannase plays an important role in bioconversion of tannin, a major constituent of tannery effluent, to gallic acid which has great pharmaceutical applications. Therefore, the aim of the current study was to exploit the potential of tannase from Aspergillus glaucus and fungal biomass waste for the bioremediation of heavy metals and tannin.
Results
Tannase from A. glaucus was partially purified 4.8-fold by ammonium sulfate precipitation (80%). The enzyme was optimally active at pH 5.0 and 40 °C and stable at this temperature for 1 h. Tannase showed high stability at different physiological conditions, displayed about 50% of its activity at 60 °C and pH range 5.0–6.0. Immobilization of tannase was carried out using methods such. as entrapment in Na-alginate and covalent binding to chitosan. The effects of Na-alginate concentrations on the beads formation and enzyme immobilization revealed that maximum immobilization efficiency (75%) was obtained with 3% Na-alginate. A potential reusability of the immobilized enzyme was showed through keeping 70% of its relative activity up to the fourth cycle. The best bioconversion efficiency of tannic acid to gallic acid by immobilized tannase was at 40 °C with tannic acid concentration up to 50 g/l. Moreover, bioremediation of heavy metal (Cr3+, Pb2+, Cu2+, Fe3+, and Mn2+) from aqueous solution using A. glaucus biomass waste was achieved with uptake percentage of (37.20, 60.30, 55.27, 79.03 and 21.13 respectively). The biomass was successfully used repeatedly for removing Cr3+ after using desorbing agent (0.1 N HCl) for three cycles.
Conclusion
These results shed the light on the potential use of tannase from locally isolated A. glaucus in the bioremediation of industrial tanneries contained heavy metals and tannin.
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