Isoprene is an aviation fuel of high quality and an important polymer building block in the synthetic chemistry industry. In light of high oil prices, sustained availability, and environmental concerns, isoprene from renewable materials is contemplated as a substitute for petroleum-based product. Escherichia coli with advantages over other wild microorganisms, is considered as a powerful host for biofuels and chemicals. Here, we constructed a synthetic pathway of isoprene in E. coli by introducing an isoprene synthase (ispS) gene from Populus nigra, which catalyzes the conversion of dimethylallyl diphosphate (DMAPP) to isoprene. To improve the isoprene production, we overexpressed the native 1-deoxy-D: -xylulose-5-phosphate (DXP) synthase gene (dxs) and DXP reductoisomerase gene (dxr) in E. coli, which catalyzed the first step and the second step of MEP pathway, respectively. The fed-batch fermentation results showed that overexpression of DXS is helpful for the improvement of isoprene production. Surprisingly, heterologous expression of dxs and dxr from Bacillus subtilis in the E. coli expressing ispS resulted in a 2.3-fold enhancement of isoprene production (from 94 to 314 mg/L). The promising results showed that dxs and dxr from B. subtilis functioned more efficiently on the enhancement of isoprene production than native ones. This could be caused by the consequence of great difference in protein structures of the two original DXSs. It could be practical to produce isoprene in E. coli via MEP pathway through metabolic engineering. This work provides an alternative way for production of isoprene by engineered E. coli via MEP pathway through metabolic engineering.
Common human plasma proteins (CHPP), also called blood proteins, are proteins found in blood plasma. The molecular structure/property-affinity relationships of dietary polyphenols noncovalently binding to CHPP were investigated by comparing the binding constants obtained from the fluorescence titration method. An additional methoxy group in flavonoids increased their binding affinities for CHPP by 1.05 to 72.27 times. The hydroxylation on the 4' position (ring B) of flavones and flavonols and the 5 position (ring A) of isoflavones weakened the binding affinities; however, the hydroxylation on other positions of flavonoids slightly enhanced or little affected the binding affinities for CHPP. The glycosylation of flavonoids weakened or slightly affected the affinities for CHPP by 1 order of magnitude. The hydrogenation of the C2═C3 double bond of flavone, 6-hydroxyflavone, 6-methoxyflavone and myricetin decreased the binding affinities about 10.02 to 17.82 times. The galloylation of catechins significantly improved the binding affinities with CHPP about 10 to 1000 times. The esterification of gallic acid increased its binding affinity. The binding affinities with CHPP were strongly influenced by the structural differences of dietary polyphenols. Polyphenols with higher affinities for purified HSA also showed stronger affinities with CHPP. The hydrophobic force played an important role in binding interaction between polyphenols and CHPP.
The molecular structure/property-affinity relationships of dietary polyphenols non-covalently binding to total plasma proteins of type II diabetes (IIDTPP) were investigated by comparing the binding constants obtained from the fluorescence titration method. An additional methoxy group in flavonoids increased their binding affinities for IIDTPP by 1.38 to 15.85 times. The hydroxylation at the 4' position (Ring B) of flavonols and the 5 position (Ring A) of isoflavones weakened the binding affinities; however, hydroxylation at other positions on flavonoids slightly enhanced or little affected the binding affinities for IIDTPP. The glycosylation of flavonoids slightly decreased or little affected the affinities for IIDTPP by less than 1 order of magnitude. The hydrogenation of the C2[double bond, length as m-dash]C3 double bond of flavone, 6-hydroxyflavone, 6-methoxyflavone and myricetin decreased the binding affinities. The galloylation of catechins significantly improved the binding affinities with IIDTPP approximately 10 to 1000 times. The esterification of gallic acid increased its binding affinity. The hydrophobic force played an important role in the binding interaction between polyphenols and IIDTPP.
Ligninolytic bacteria degrading lignin were isolates and identified, and their biodegradation mechanism of alkaline-lignin was investigated. Four strains with lignin degradation capability were screened and identified from the soil, straw, and silage based on their decolorizing capacity of aniline blue and colony size on alkaline-lignin medium. The degradation ratio of Bacillus aryabhattai BY5, Acinetobacter johnsonii LN2, Acinetobacter lwoffii LN4, and Micrococcus yunnanensis CL32 have been assayed using alkaline-lignin as the unique carbon source. Further, the Lip (lignin peroxidase) and Mnp (manganese peroxidase) activities of strains were investigated. Lip activity of A. lwoffii LN4 was highest after 72 h of incubation and reached 7151.7 U · l–1. Mnp activity of M. yunnanensis CL32 was highest after 48 h and reached 12533 U · l–1. The analysis of alkaline-lignin degradation products by GC-MS revealed that the strains screened could utilize aromatic esters compounds such as dibutyl phthalate (DBP), and decomposite monocyclic aromatic compounds through the DBP aerobic metabolic pathway. The results indicate that B. aryabhattai BY5, A. johnsonii LN2, A. lwoffii LN4, and M. yunnanensis CL32 have high potential to degrade alkaline-lignin, and might utilize aromatic compounds by DBP aerobic metabolic pathway in the process of lignin degradation.
The molecular property-affinity relationship of dietary flavonoids for bovine gamma-globulin (γ-globulin) was investigated by fluorescence titration analysis. The quenching effects of flavonoids on γ-globulin fluorescence depended on the structures of flavonoids. The magnitudes of binding constants between flavonoids and γ-globulin were within the range of 10(3)-10(5) L mol(-1). These data were much smaller than the affinities between flavonoids and purified bovine and human serum albumins. The affinities of flavonoids for γ-globulin were strongly influenced by the structural differences of the compounds under study. The affinities for γ-globulin decreased with increasing partition coefficients and increased with increasing hydrogen bond acceptor numbers of flavonoids, which suggested that the binding interaction was mainly caused by hydrogen bond forces.
The effect of a ZnO#ZnS QDs heterojunction (O#SQDs) on the binding affinities of flavonoid glycosides for bovine serum albumin (BSA) was investigated. The fluorescence intensities of BSA decreased remarkably with increasing concentration of O#SQDs. The magnitudes of the binding constants of flavonoid glycosides for BSA in the presence of O#SQDs were in the range of 10(5)-10(7) L mol(-1), and the number of binding sites per BSA (n) was determined as 1.24 ± 0.17. O#SQDs increased the affinities of flavonoid glycosides for BSA by about 2.96% to 114.68% depending on their structures. O#SQDs in blood will enhance the transportation of flavonoid glycosidegs in blood and improve their pharmacology effects. From this point, O#SQDs are a perfect candidate for flavonoid glycosides delivery applications.
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