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- Othman, Nor Zalina, et al.
(författare)
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Aeration rate effect on the growth kinetics, phytase production and plasmid stability of recombinant Escherichia coli BL21 (DE3)
- 2014
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Ingår i: Journal of Pure and Applied Microbiology. - 0973-7510. ; 8:4, s. 2721-2728
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Tidskriftsartikel (refereegranskat)abstract
- Phytase production using Escherichia coli BL21 (DE3), a recombinant strain harboring a plasmid encoding thermostable Bacillus phytase, in semi-industrial scale was studied in this work. Among the factors needed to be considered in order to achieve high enzyme yield, aeration rate plays an important role. Suitable aeration is required to supply cells with sufficient amount of air for cell and phytase production. The effect of different aeration rates, (1.0, 2.0 and 3.0 vv-1min-1), on the kinetics of cell growth and phytase production by the recombinant E. coli BL21 (DE3) in 16-L pilot scale stirred tank bioreactor was investigated. The highest cell concentration of 3.81 gL-1 concomitant with the maximal total phytase production of 15.63 UmL-1 were obtained in a bioreactor of aeration rate 3.0vv-1min-1. At this high aeration rate, a maximal specific growth rate (μmax) and the maximal specific phytase production of 0.33 h-1 and 4102Ug-1, respectively, were achieved.
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2. |
- El Massry, Abdel Moneim, et al.
(författare)
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Synthesis and structure elucidation of novel fused 1,2,4-triazine derivatives as potent inhibitors targeting CYP1A1 activity
- 2012
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Ingår i: Bioorganic and Medicinal Chemistry. - : Elsevier BV. - 0968-0896 .- 1464-3391. ; 20:8, s. 2624-2637
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Tidskriftsartikel (refereegranskat)abstract
- Synthesis and structure elucidation of new series of novel fused 1,2,4-triazine derivatives 3a-3f, 4a-4i and 6a-6b and their inhibitory activities are presented. Molecular structures of the synthesized compounds were confirmed by H-1 NMR, C-13 NMR, MS spectra and elemental analyses. X-ray crystallographic analysis was performed on 2-acetyl-8-(N,N-diacetylamino)-6-(4-methoxybenzyl)-3-(4-methoxy-phenyl)- 7-oxo-2,3-dihydro-7H-[1,2,4]triazolo[4,3-b][1,2,4]triazine 3d and 2-acetyl-8-(N-acetyl- amino)-6-benzyl-3-(4-chlorophenyl)-3-methyl-7-oxo-2,3-dihydro-7H-[1,2,4] triazolo[4,3-b][1,2,4]triazine 4e to secure their structures. The inhibitory effect of these compounds toward the CPY1A1 activity was screened to determine their potential as promising anticancer drugs. Our data showed that compounds 4e, 5a, 5b and 6b possess the highest inhibitory effects among all tested compounds. Furthermore, analysis of triazolotriazine derivatives docking showed that these compounds bind only at the interface of substrate recognition site 2 (SRS2) and (SRS6) at the outer surface of the protein. Amino-acids ASN214, SER216 and ILE462 participate in the binding of these compounds through H-bonds.
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