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Xingwang Zhou,Jun Yao,Ming Yang,Jiangquan Ma,Qingwei Zhou,Ershen Ou,Zhen Zhang,Xueni Sun 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2018 NANO Vol.13 No.4
In this research, a series of novel MoSe2/SrTiO3 heterostructures were successfully prepared by a two-step hydrothermal method. The samples were characterized by XRD, UV-Vis, SEM, TEM, EDS and XPS. Results showed that the degradation of MO under UV is better than that under the visible light. And, MoSe2 loaded on SrTiO3 under UV irradiation demonstrated a higher catalytic activity. The degradation rate of methyl orange was 99.46% for MoSe2/SrTiO3 under the optimum loading weight (0.1 wt.%). This is mainly because the combination of MoSe2 and SrTiO3 prevents electrons and holes recombination in SrTiO3 and · O2 - appears in the system. In general, MoSe2/SrTiO3 heterostructures have good environmental friendliness for photocatalytic degradation.
Xingwang Zhou,Jia Zhou,Yongwei Yu,Jiangquan Ma,Xueni Sun,Lanmei Hu 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2017 NANO Vol.12 No.10
In this research, a series of catalysts based on MoSe2 were synthesized by the hydrothermal method and used for the catalytic hydrogenation of alkali lignin for the first time. For 4 wt.% NiSe2/MoSe2 catalyst, at 290 ℃, under 2MPa H2 pressure for 1.5 h, the conversion of alkali lignin and the yield of bio-oil reached 96.47% and 93.68%, respectively. In addition, the composition of the product (bio-oil) was analyzed via Fourier transform infrared (FTIR) spectrometry, gas chromatography-mass spectrometry (GC-MS) spectra, and proton nuclear magnetic resonance (1HNMR) spectra. Finally, our study demonstrated that those MoSe2-based composite catalysts can effectively degrade the biomass into bio-oil containing valuable chemical products.
Yifan Qian,Xingwang Zhang,Lei Zhou,Shifang Ren,Jianxin Gu 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
Human LOX-1/OLR 1 plays a key role in atherogenesis and endothelial dysfunction. The N-glycosylation of LOX-1 has been shown to affect its biological functions in vivo and modulate the pathogenesis of atherosclerosis. However, the N-glycosylation pattern of LOX-1 has not been described yet. The present study was aimed at elucidating the N-glycosylation of recombinanthuman LOX-1 with regard to N-glycan profile and N-glycosylation sites. Here, an approach using nonspecific protease (Pronase E) digestion followed by MALDI-QIT-TOF MS and multistage MS (MS3) analysis is explored to obtain site-specificN- glycosylation information of recombinanthuman LOX-1, in combination with glycan structure confirmation through characterizing released glycans using tandem MS. The results reveal that N-glycans structures as well as their corresponding attached site of LOX-1 can be identified simultaneously by direct MS analysis of glycopeptides from non-specific protease digestion. With this approach, one potential glycosylation site of recombinanthuman LOX-1 on Asn139 is readily identified and found to carry heterogeneous complex type N-glycans. In addition, manual annotation of multistage MS data utilizing diagnostic ions, which were found to be particularly useful in defining the structure of glycopeptides and glycans was addressed for proper spectra interpretation. The findings described herein will shed new light on further research of the structure-function relationships of LOX-1 N-glycan.