In-vitro biodegradation of Glyphosate using genetically improved bacterial isolates from ‎highly polluted wastewater

Serih, Nivien Abo; salim, rasha; Fikry, Ahmed; Hammad, M. A.; El-Sayed, Ghada M.

doi:10.21608/ejchem.2022.141571.6194

Cited by 2 publications

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“…They used 16s rDNA sequencing to analyze a strain of Lysinibacillus sphaericus that produces ß -glucosidase isolated from an Egyptian environment. Also, Abosereh et al (2022) used 16s rDNA barcoding for molecular identification of a Bacillus sp. isolated from the Egyptian soil and identified it as B. cereus .…”

Section: Discussionmentioning

confidence: 99%

Recombinant production, purification, and biochemical characterization of a novel L-lactate dehydrogenase from Bacillus cereus NRC1 and inhibition study of mangiferin

Esa

El-Sayed

El-Khonezy

et al. 2023

Front. Bioeng. Biotechnol.

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Lactate dehydrogenase (LDH, EC 1.1.1.27) is one of the vital glycolytic conditions, especially during anaerobic conditions. It is a significant diagnostic, prognostic, and monitoring biomarker parameter. A 950-bp DNA fragment containing the gene (LDH) encoding LDH was amplified from Bacillus cereus NRC1. The deduced amino acid sequence reveals that B. cereus LDH (Bc-LDH) is highly homologous to the LDHs of Bacillus organisms. All LDH enzymes have a significant degree of conservation in their active site and several additional domains with unidentified functions. The gene for LDH, which catalyzes lactate synthesis, was cloned, sequenced (accession number: LC706200.1), and expressed in Escherichia coli BL21 (DE3). In this investigation, Bc-LDH was purified to homogeneity with a specific activity of 22.7 units/mg protein and a molecular weight of 35 kDa. It works optimally at pH 8.0. The purified enzyme was inhibited by FeCl2, CuCl2, ZnCl2, and NiCl, whereas CoCl2 was found to boost the activity of Bc-LDH. The molecular docking of the 3D model of the Bc-LDH structure with a natural inhibitor, mangiferin, demonstrated excellent LDH inhibition, with a free binding energy of −10.2 kcal/mol. Moreover, mangiferin is a potent Bc-LDH inhibitor that inhibits Bc-LDH competitively and has one binding site with a Ki value of 0.075 mM. The LDH-mangiferin interaction exhibits a low RMSF value (>1.5 Å), indicating a stable contact at the residues. This study will pave the way for more studies to improve the understanding of mangiferin, which could be considered an intriguing candidate for creating novel and improved LDH inhibitors.

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Section: Discussionmentioning

confidence: 99%

Recombinant production, purification, and biochemical characterization of a novel L-lactate dehydrogenase from Bacillus cereus NRC1 and inhibition study of mangiferin

Esa

El-Sayed

El-Khonezy

et al. 2023

Front. Bioeng. Biotechnol.

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“…The biological approach to soil remediation is considered more ecologically friendly and less expensive than physical-chemical techniques (Zhan et al, 2018). Glyphosate is a widely used herbicide efficiently eliminated by microorganisms (Bhatt et al, 2021a), Over time, various studies have confirmed the ability of different microorganisms to degrade glyphosate (Abosereha et al, 2022;Elarabi et al, 2020;Ermakova et al, 2017). However, studies on the biodegradation of glyphosate by the genus Streptomyces are rare (Singh et al, 2019;Lipok et al, 2009;Obojska et al, 1999), although this particular genus of actinomycetales being the most dominant in soil, accounting for more than 95% of the identified bacteria (Barka et al, 2016).…”

Section: Discussionmentioning

confidence: 99%

Streptomyces sp. Strain SRH22: A Potential Bioremediation Agent for Glyphosate-Contaminated Agricultural Soils

Rebai,

Sholkamy,

Alharbi

et al. 2023

Environ. Nat. Resour. J.

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Glyphosate, also known as N-phosphonomethylglycine, is the herbicide that is widely used across the globe. As there are concerns over its potential toxicity to non-target soil species, there is a growing interest in identifying glyphosate-degrading microorganisms in soil. Biodegradation, by actinobacteria, is a very promising approach to eliminate this pesticide from contaminated environments. The present work isolated and identified actinobacteria capable of degrading glyphosate from Saharan agriculture, as well as determined how the application of this herbicide affects the abundance of actinobacteria present in soil. It was observed that the use of glyphosate led to an increased abundance of actinobacteria in the soil compared to the untreated soil. Among this population, an actinobacterial strain was isolated from glyphosate contaminated soil by the enrichment method, and was identified to possess the greatest capability to degrade glyphosate at 50 mg/L. The identification of this strain was achieved through a combination of cultural, morphological, biochemical, and molecular techniques. This included the use of 16S rDNA sequencing, leading to its successful classification as Streptomyces sp. strain SRH22. This strain was assigned the accession number OQ302556 by the National Center for Biotechnology Information (NCBI). A rapid, sensitive, and straightforward spectrophotometric technique was employed for the quantification of glyphosate. Results showed that the optimal biodegradation (90.2%) was obtained under a temperature of 30 degrees, a PH of 7.2, and an inoculum volume of 4% timed over six days. This work shows that the Streptomyces SRH22 presents good potentiality to be used as a bioremediation agent for agricultural soils in the Algerian Sahara.

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In-vitro biodegradation of Glyphosate using genetically improved bacterial isolates from ‎highly polluted wastewater

Cited by 2 publications

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Recombinant production, purification, and biochemical characterization of a novel L-lactate dehydrogenase from Bacillus cereus NRC1 and inhibition study of mangiferin

Recombinant production, purification, and biochemical characterization of a novel L-lactate dehydrogenase from Bacillus cereus NRC1 and inhibition study of mangiferin

Streptomyces sp. Strain SRH22: A Potential Bioremediation Agent for Glyphosate-Contaminated Agricultural Soils

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