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- 저자 : Fuping Lu (검색결과 3 건)
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Hengda Yuan,Yu Zhang,Guoqiang Lu,Fuping Chen,Tanlong Xue,Xin Shu,Yingying Zhao,Jun Nie,Xiaoqun Zhu 한국공업화학회 2022 Journal of Industrial and Engineering Chemistry Vol.109 No.-
The application of conventional absorbing materials is limited due to complex preparation process andpoor transparency caused by fillers. In this study, a highly transparent ionic organogel was preparedby photocuring a dimethyl sulfoxide (DMSO) solution of a polymerizable magnetic cationic monomer[DAC]5[Dy(NCS)8]. Both components of organogel, which are the photopolymerizable magnetic cationicmonomer and polar solvent DMSO, have an important effect on the magnetic losses and dielectric lossesproperties of the organogel respectively. By tuning the mass ratio of DMSO to the monomer and the contentof the cross-linker, the complex permittivity of the gel could be effectively adjusted to improve theimpedance matching, and finally a gel with excellent wave absorption properties and good tensile propertieswas obtained. The optimum organogel was fabricated with a minimum reflection loss of 45.9 dBand a broadest effective absorption bandwidth (EAB) of up to 5.2 GHz, and effective absorption in the millimeterband (26.5–40 GHz) which is within the fifth generation (5G) mobile networks. With the advantagesof simple preparation method, arbitrary shape and good adhesion to a variety of substrates andcomplex surfaces, this multifunctional gel provides a new solution for complex scenarios requiring opticaltransparency and simultaneous absorption of electromagnetic waves.
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Jun Wang,Wei Li,Dandan Niu,Suren Singh,Fuping Lu,Xiaoguang Liu 한국식품과학회 2017 Food Science and Biotechnology Vol.26 No.3
a-Glucosidase was immobilized onto an epoxyactivated resin (Eupergit C) to catalyze maltose into isomaltooligosaccharides (IMO), and then the effects of organic–aqueous media on the enzymatic properties of immobilized a-glucosidase were examined. An immobilization efficiency of 79.61% was obtained under the condition of pH 6.0, ionic strength of 2.0 M, and 30 mg of protein/g of resin. The butyl acetate-aqueous biphasic system was found to significantly improve the catalytic activity of the immobilized enzyme and the yield of IMO. The highest yield of IMO (50.83%, w/w) was obtained at pH 4.5 and 55 C in a butyl acetate/buffer system (25:75, v/v). In addition, the immobilized enzyme particles were distributed into the organic phase after the completion of transglycosylation, which facilitates the separation and recycling use of the immobilized enzyme. Immobilized aglucosidase retains a robust reusability in this continuous operation model. The present findings are of potential in improving the IMO manufacturing process.
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( Sanyuan Shi ),( Liu Yang ),( Chen Yang ),( Shanshan Li ),( Hong Zhao ),( Lu Ren ),( Xiaokang Wang ),( Fuping Lu ),( Ying Li ),( Huabing Zhao ) 한국미생물생명공학회(구 한국산업미생물학회) 2021 Journal of microbiology and biotechnology Vol.31 No.2
Many bacteria metabolize aromatic compounds via catechol as a catabolic intermediate, and possess multiple genes or clusters encoding catechol-cleavage enzymes. The presence of multiple isozyme-encoding genes is a widespread phenomenon that seems to give the carrying strains a selective advantage in the natural environment over those with only a single copy. In the naphthalene-degrading strain Pseudomonas putida ND6, catechol can be converted into intermediates of the tricarboxylic acid cycle via either the ortho- or meta-cleavage pathways. In this study, we demonstrated that the catechol ortho-cleavage pathway genes (catB<sub>I</sub>C<sub>I</sub>A<sub>I</sub> and catB<sub>II</sub>C<sub>II</sub>A<sub>II</sub>) on the chromosome play an important role. The cat<sub>I</sub> and cat<sub>II</sub> operons are co-transcribed, whereas catA<sub>I</sub> and catA<sub>II</sub> are under independent transcriptional regulation. We examined the binding of regulatory proteins to promoters. In the presence of cis-cis-muconate, a well-studied inducer of the cat gene cluster, CatR<sub>I</sub> and CatR<sub>II</sub> occupy an additional downstream site, designated as the activation binding site. Notably, CatR<sub>I</sub> binds to both the cat<sub>I</sub> and cat<sub>II</sub> promoters with high affinity, while CatR<sub>II</sub> binds weakly. This is likely caused by a T to G mutation in the G/T-N11-A motif. Specifically, we found that CatR<sub>I</sub> and CatR<sub>II</sub> regulate catB<sub>I</sub>C<sub>I</sub>A<sub>I</sub> and catB<sub>II</sub>C<sub>II</sub>A<sub>II</sub> in a cooperative manner, which provides new insights into naphthalene degradation.
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