Publications by authors named "Shaimaa A Nour"

Background: The energy efficiency and environmental friendliness of recombinant chitinase A make it a promising candidate for industrial applications as a sustainable catalyst. For the first time, a very stable and an efficient biocatalyst was developed to decolorize synthetic dyes by immobilizing Serratia marcescens chitinase A (SmChiA) onto beads comprised of sodium alginate (SA) and modified rice husk powder (mRHP). The mRHP was produced by treating rice husk powder with citric acid, which was then combined with SA at three different concentrations (25, 50 and 100% of SA weight) and cross-linked with calcium chloride to form the beads.

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  • Microbial combating, particularly through innovative strategies, is a crucial area of research, leading to the development of a new combined chemo- and photodynamic delivery system using zinc oxide nanoparticles (ZnO NPs) and other agents.
  • The engineered nanoformulation, ZnO@ALG-POR/BER, showcased significantly better loading capacity and antimicrobial effectiveness when paired with laser treatment compared to traditional methods, achieving complete suppression of bacterial and fungal growth.
  • Additionally, the cytotoxicity study indicated that these nanoformulations, especially ZnOBER@ALG-POR, demonstrated moderate biocompatibility with human retinal cells, paving the way for potential applications in medical treatments.
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Carbimazole has disadvantages on different body organs, especially the thyroid gland and, rarely, the adrenal glands. Most studies have not suggested any solution or medication for ameliorating the noxious effects of drugs on the glands. Our study focused on the production of xylooligosaccharide (XOS), which, when coadministered with carbimazole, relieves the toxic effects of the drug on the adrenal glands.

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  • Researchers isolated a cellulase-producing bacterium, Bacillus amyloliquefaciens strain elh, from rice peel and used optimization methods like one-variable-at-a-time (OVAT) and response surface methodology (RSM) to increase cellulase production.* -
  • Initial cellulase activity was 0.141 U/ml, but after optimization, the peak activity reached 14.04 U/ml, and the optimal fermentation time was identified as 72 hours using specific nitrogen and sugar sources.* -
  • The cellulase-encoding gene (egl) was successfully cloned and expressed in E. coli, resulting in an activity of 22.3 U/ml, and in silico analysis showed key interactions between cellulase and
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Microbial proteases have proven their efficiency in various industrial applications; however, their application in accelerating the wound healing process has been inconsistent in previous studies. In this study, heterologous expression was used to obtain an over-yielding of the serine alkaline protease. The serine protease-encoding gene aprE was isolated from Bacillus safensis lab 418 and expressed in E.

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Background: Hydrocarbon pollution stemming from petrochemical activities is a significant global environmental concern. Bioremediation, employing microbial chitinase-based bioproducts to detoxify or remove contaminants, presents an intriguing solution for addressing hydrocarbon pollution. Chitooligosaccharides, a product of chitin degradation by chitinase enzymes, emerge as key components in this process.

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Root-knot nematode is one of the major problems that face the agricultural production of several vegetable crops. Chemical nematicides have been banned because of their healthy and environmental undesirable attributes. So, this study aimed to evaluate the potential use of sweet annie (Artimisia annua) and garden cress (Lepidium sativum) as green routes for the development of effective and eco-friendly alternative nematicides.

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Background: The production of industrial enzymes such as xylanase using sufficient cost-effective substrates from potent microorganisms is considered economically feasible. Studies have reported castor cake (Ricinus communis) as the most potent and inexpensive alternative carbon source for production of xylanase C by using Aspergillus terreus (A. terreus).

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