Publications by authors named "Amira A El-Fallal"

4 Publications

  • Page 1 of 1

Effect of Biologically Treated Wheat Straw with White-Rot Fungi on Performance, Digestibility and Oxidative Status of Rabbits.

Pak J Biol Sci 2020 Jan;23(12):1551-1562

Background And Objective: Raising growing rabbits is an ideal solution to confront animal protein deficiency, especially in developing countries. The presence of lignin in wheat straw causes limitation of the digestion overall process. The biological delignification is a practical and promising alternative due to improving the digestibility of wheat straw. This study aimed to enhance wheat straw digestibility and enriching it with protein and use it as a growing rabbit feedstuff.

Materials And Methods: Enzymes production of white-rot fungi was assayed in myco-straw and the mean value was recorded. Wheat straw has been treated with the three most effective fungal species with Biological Treated Wheat Straw (BTWS). After that, the myco-straw was grounded and included in diet to evaluate the growth performance, digestibility and blood parameters of a growing V-line rabbit.

Results: The best three species for enzyme productions were P. sajor-caju, P. columbinus and P. floridanus. The optimum incubation period was 16 days. The fungal treatments showed significant enzymes activity of laccase, Mn-peroxidase, cellulase and xylanase. Body weight, body weight gain and feed conversion ratio of growing V-line rabbits had improved than those of the control. But, nutrients digestibility of the diet containing BTWS and Carcass traits of growing V-line rabbits were non-significant compared with the control one. In comparison with control, the lipid profile had no differences but the total protein was improved.

Conclusion: White-rot fungal conversion of wheat straw is maybe one potential alternative providing a more practical, environmental-friendly and nutritionally enhancing as rabbits feedstuff. Rabbits fed BTWS-diets had significantly improved growth performance.
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http://dx.doi.org/10.3923/pjbs.2020.1551.1562DOI Listing
January 2020

Ergosterol Peroxide from the Egyptian Red Lingzhi or Reishi Mushroom, Ganoderma resinaceum (Agaricomycetes), Showed Preferred Inhibition of MCF-7 over MDA-MB-231 Breast Cancer Cell Lines.

Int J Med Mushrooms 2020 ;22(4):389-396

Chemistry Department, Faculty of Science, Damietta University, New Damietta City, Egypt; Department of Neurosurgery, Robert Wood Johnson Medical School, Rutgers University, Piscataway, NJ 08854, USA.

Ergosterol peroxide and ganoderic acid AMI were isolated for the first time from the mycelium of the Egyptian Ganoderma resinaceum mushroom. The structure of these two metabolites was established by detailed analysis of 1D and 2D NMR. The isolated compounds were tested for their antitumor in vitro activities in MCF-7 and MDA-MB-231 breast cancer cell lines. Ergosterol peroxide showed preferred inhibition of MCF-7 (ER +ve) cell lines relative to MDA-MB-231 (ER -ve) cell lines with an IC50 of 1.18 μM and 12.82 μM respectively. Our data suggest that ergosterol peroxide targets estrogen receptors.
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http://dx.doi.org/10.1615/IntJMedMushrooms.2020034223DOI Listing
February 2021

Heterologous expression, purification, immobilization and characterization of recombinant α-amylase AmyLa from Laceyella sp. DS3.

Int J Biol Macromol 2019 Jul 3;132:1274-1281. Epub 2019 Apr 3.

Botany and Microbiology Department, Faculty of Science, Damietta University, Egypt. Electronic address:

AmyLa α-amylase gene from Laceyella sp. DS3 was heterologously expressed in E. coli BL21. E. coli BL21 maximally expressed AmyLa after 4 h of adding 0.02 mM IPTG at 37 °C. The recombinant AmyLa α-amylase was purified 2.19-fold through gel filtration and ion exchange chromatography. We immobilized the purified recombinant AmyLa α-amylase on four carriers; chitosan had the best efficiency. The recombinant free and the immobilized AmyLa α-amylase showed optimum activity in the pH ranges of 6.0-7.0 and 4.0-7.0, respectively and possessed an optimum temperature of 55 °C. The free enzyme had activation energy, Km, and Vmax of 291.5 kJ, 1.5 mg/ml, and 6.06 mg/min, respectively. The immobilized enzyme had activation energy, Km, and Vmax of 309.74 kJ, 6.67 mg/ml, and 50 mg/min, respectively. The immobilized enzyme was calcium-independent and insensitive (relative to the free enzyme) to metals. It could also be reused for seven cycles.
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http://dx.doi.org/10.1016/j.ijbiomac.2019.04.010DOI Listing
July 2019

Purification, sequencing, and biochemical characterization of a novel calcium-independent α-amylase AmyTVE from Thermoactinomyces vulgaris.

Appl Biochem Biotechnol 2013 Jun 4;170(3):483-97. Epub 2013 Apr 4.

Botany Department, Faculty of Science, Damietta University, P.O. Box 34517, New Damietta, Egypt.

α-Amylase from Thermoactinomyces vulgaris was highly purified 48.9-fold by ammonium sulfate precipitation, gel filtration on Sephadex G-50 column, and ion exchange chromatography column of DEAE-cellulose. The molecular weight of the enzyme was estimated to be 135 and 145 kDa by SDS-PAGE. Its high molecular weight is due to high glycosylation. The purified amylase exhibited maximal activity at pH 6.0 to 7.0 and was stable in the range of pH 4.0 to 9.0. The optimum temperature for its activity was 50 °C. The enzyme half-life time was 120 min at 50 °C, suggesting intermediate temperature stable α-amylase. The enzyme was sensitive to different metal ions, including NaCl, CoCl(2), and CaCl(2), and to different concentrations of EDTA. The enzyme activity was inhibited in the presence of 1 mM CaCl(2), suggesting that it is a calcium-independent α-amylase. The TLC showed that the amylase hydrolyzed starch to produce large maltooligosaccharides as the main products. A 1.1-kb DNA fragment of the putative α-amylase gene (amy TVE) from T. vulgaris was amplified by using two specific newly designed primers. Sequencing analysis showed 56.2 % similarity to other Thermoactinomyces α-amylases with two conserved active sites confirming its function.
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http://dx.doi.org/10.1007/s12010-013-0201-7DOI Listing
June 2013
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