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Countryside Administration and Programming Management System
Lin, Xiao Quan,Zhang, Dong Hong,Zhang, Hai Ming,Liu, Yu Zeng 대한원격탐사학회 2000 International Symposium on Remote Sensing Vol.16 No.1
In accordance with the practical need to China countryside agricultural planting, land utilizing programming and countryside administrative information management, adopting MIS/GIS and large scaled map, the $quot;Countryside Administration and Programming Management System$quot; realizes the management functions to land resource, planting, land utilizing programming, household and population, family plan, administrative documents, developing programing, statistics analysis, lays goad ground work far using GIS and information Internet technology in countryside administration and producing management.
Review : Perspective on Peroral Endoscopic Myotomy for Achalasia: Zhongshan Experience
( Quan Lin Li ),( Ping Hong Zhou ) The Editorial Office of Gut and Liver 2015 Gut and Liver Vol.9 No.2
Worldwide, peroral endoscopic myotomy (POEM) has achieved remarkable initial outcomes in the treatment of achalasia. In China, POEM has developed very quickly since the first case was performed in our center in August 2010. With experience, we have successfully performed POEM for special cases (such as pediatric patients, patients with sigmoid-type esophagus, and patients with recurrent symptoms after previous surgery) and have altered our technique to achieve long-term symptom remission and simplify the POEM procedure. These changes include posterior wall incision, full-thickness myotomy, a “push-and-pull” technique for myotomy, and water-jet assisted POEM. In this article, our experiences in POEM are summarized, including changes in technique, applications of the procedure, and the management of possible complications. (Gut Liver, 2015;9:152-158)
Lin-Hu Quan,Jin-Ying Piao,Jin-Woo Min,Ho-Bin Kim,Sang-Rae Kim,Dong-Uk Yang,Deok Chun Yang 고려인삼학회 2011 Journal of Ginseng Research Vol.35 No.3
Ginsenoside Rb_1is the main component in ginsenosides. It is a protopanaxadiol-type ginsenoside that has a dammarane-type triterpenoid as an aglycone. In this study, ginsenoside Rb_1 was transformed into gypenoside XVII, ginsenoside Rd, ginsenoside F_2 and compound K by glycosidase from Leuconostoc mesenteroides DC102. The optimum time for the conversion was about 72 h at a constant pH of 6.0 to 8.0 and the optimum temperature was about 30°C. Under optimal conditions, ginsenoside Rb_1was decomposed and converted into compound K by 72 h post-reaction (99%). The enzymatic reaction was analyzed by highperformance liquid chromatography, suggesting the transformation pathway: ginsenoside Rb_1→ gypenoside XVII and ginsenoside Rd→ginsenoside F_2→compound K.
Lin-Hu Quan,Jin-Ying Piao,Jin-Woo Min,Ho-Bin Kim,Sang-Rae Kim,Dong-Uk Yang,Deok Chun Yang 고려인삼학회 2011 Journal of Ginseng Research Vol.35 No.3
Ginsenoside Rb<sub>1</sub>is the main component in ginsenosides. It is a protopanaxadiol-type ginsenoside that has a dammarane-type triterpenoid as an aglycone. In this study, ginsenoside Rb<sub>1</sub> was transformed into gypenoside XVII, ginsenoside Rd, ginsenoside F<sub>2</sub> and compound K by glycosidase from Leuconostoc mesenteroides DC102. The optimum time for the conversion was about 72 h at a constant pH of 6.0 to 8.0 and the optimum temperature was about 30℃. Under optimal conditions, ginsenoside Rb<sub>1</sub> was decomposed and converted into compound K by 72 h post-reaction (99%). The enzymatic reaction was analyzed by high-performance liquid chromatography, suggesting the transformation pathway: ginsenoside Rb<sub>1</sub>→gypenoside XVII and ginsenoside Rd→ginsenoside F<sub>2</sub>→compound K.
LIN XU,QUAN LIN,HAO CHENG,CHUANXI WANG 성균관대학교(자연과학캠퍼스) 성균나노과학기술원 2014 NANO Vol.9 No.3
The heterostructure EuSe/Ag nanoparticles (NPs) were prepared through one-step colloidchemical method. Blue °uorescent EuSe NPs were prepared by amine reducing method witholeylamine (OLA) as surface stabilizer. The colloid microemulsion was formed through themixture of AgNO 3 aqueous solution and the EuSe n-Hexane solution. On the interface, Agþionscould be reduced to Ag NPs by OLA. Finally heterogeneous EuSe/Ag NPs were obtained. Thestructure and properties of EuSe NPs and EuSe/Ag NPs were characterized by photo-luminescence (PL), transmission electron microscopy (TEM) and X-ray photoelectron spec-troscopy (XPS). The results showed that the luminescence resonance energy transfer (LRET)occurred on the interface of EuSe NPs and Ag NPs. Also it demonstrated that the linear enhancedLRET e®ect happened with increasing the concentration of Agþ. All these properties make ourheterostructural EuSe/Ag NPs to have interesting potential applications for ions detection andbiosensors.
Quan, Lin-Hu,Min, Jin-Woo,Yang, Dong-Uk,Kim, Yeon-Ju,Yang, Deok-Chun Springer International 2012 Applied microbiology and biotechnology Vol.94 No.2
<P>Microbacterium esteraromaticum was isolated from ginseng field. The beta-glucosidase gene (bgp1) from M. esteraromaticum was cloned and expressed in Escherichia coli BL21 (DE3). The bgp1 gene consists of 2,496 bp encoding 831 amino acids which have homology to the glycosyl hydrolase family 3 protein domain. The recombinant beta-glucosidase enzyme (Bgp1) was purified and characterized. The molecular mass of purified Bgp1 was 87.5 kDa, as determined by SDS-PAGE. Using 0.1 mg ml(-1) enzyme in 20 mM sodium phosphate buffer at 37A degrees C and pH 7.0, 1.0 mg ml(-1) ginsenoside Rb1 was transformed into 0.444 mg ml(-1) ginsenoside Rg3 within 6 h. The Bgp1 sequentially hydrolyzed the outer and inner glucose attached to the C-20 position of ginsenosides Rb1. Bgp1 hydrolyzed the ginsenoside Rb1 along the following pathway: Rb1 -> aEuro parts per thousand Rd -> aEuro parts per thousand 20(S)-Rg3. This is the first report of the biotransformation of ginsenoside Rb1 to ginsenoside 20(S)-Rg3 using the recombinant beta-glucosidase.</P>
Quan, Lin-Hu,Piao, Jin-Ying,Min, Jin-Woo,Yang, Dong-Uk,Lee, Hee Nyeong,Yang, Deok Chun Sociedade Brasileira de Microbiologia 2011 Brazilian journal of microbiology Vol.42 No.3
<P>About 40 different types of ginsenoside (ginseng saponin), a major pharmacological component of ginseng, have been identified along with their physiological activities. Among these, compound K has been reported to prevent the development of and the metastasis of cancer by blocking the formation of tumors and suppressing the invasion of cancerous cells. In this study, ginsenoside Rb1 was converted into compound K via interaction with the enzyme secreted by β-glucosidase active bacteria, <I>Leuconostoc citreum</I> LH1, extracted from kimchi. The optimum time for the conversion of Rb1 to compound K was about 72 hrs at a constant pH of 6.0 and an optimum temperature of about 30°C. Under optimal conditions, ginsenoside Rb1 was decomposed and converted into compound K by 72 hrs post-reaction (99%). Both TLC and HPLC were used to analyze the enzymatic reaction. Ginsenoside Rb1 was consecutively converted to ginsenoside Rd, F2, and compound K via the hydrolyses of 20-C β-(1 → 6)-glucoside, 3-C β-(1 → 2)-glucoside, and 3-C β-glucose of ginsenoside Rb1.</P>
Microbial transformation of ginsenoside Rb1 to compound K by Lactobacillus paralimentarius.
Quan, Lin-Hu,Kim, Yeon-Ju,Li, Guan Hao,Choi, Kwang-Tea,Yang, Deok-Chun Springer 2013 World journal of microbiology biotechnology Vol.29 No.6
<P>In this study, the major ginsenoside Rb1 was transformed into the more pharmacologically active minor compound K by food grade Lactobacillus paralimentarius LH4, which was isolated from kimchi, a traditional Korean fermented food. The enzymatic reaction was analyzed by TLC, HPLC, and NMR. Using the cell-free enzyme of Lactobacillus paralimentarius LH4 at optimal conditions for 30?C at pH 6.0, 1.0?mg?ml(-1) ginsenoside Rb1 was transformed into 0.52?mg?ml(-1) compound K within 72?h, with a corresponding molar conversion yield of 88?%. The cell-free enzyme hydrolyzed the two glucose moieties attached to the C-3 position and the outer glucose moiety attached to the C-20 position of the ginsenoside Rb1. The cell-free enzyme hydrolyzed the ginsenoside Rb1 along the following pathway: ginsenoside Rb1??gypenoside XVII and ginsenoside Rd??ginsenoside F2??compound K. Our results indicate that Lactobacillus paralimentarius LH4 has the potential to be applied for the preparation of compound K in the food industry.</P>
Quan, Lin-Hu,Min, Jin-Woo,Sathiyamoorthy, Subramaniyam,Yang, Dong-Uk,Kim, Yeon-Ju,Yang, Deok-Chun Kluwer Academic Publishers 2012 Biotechnology letters. Vol.34 No.5
<P>Ginsenosides Re and Rg1 were transformed by recombinant 관-glucosidase (Bgp1) to ginsenosides Rg2 and Rh1, respectively. The bgp1 gene consists of 2,496??bp encoding 831 amino acids which have homology to the glycosyl hydrolase families 3 protein domain. Using 0.1??mg enzyme ml(-1) in 20??mM sodium phosphate buffer at 37°C and pH 7.0, the glucose moiety attached to the C-20 position of ginsenosides Re and Rg1, was removed: 1??mg ginsenoside Re ml(-1) was transformed into 0.83??mg Rg2??ml(-1) (100% molar conversion) after 2.5??h and 1??mg ginsenoside Rg1??ml(-1) was transformed into 0.6??mg ginsenoside Rh1??ml(-1) (78% molar conversion) in 15??min. Using Bgp1 enzyme, almost all initial ginsenosides Re and Rg1 were converted completely to ginsenosides Rg2 and Rh1. This is the first report of the conversion of ginsenoside Re to ginsenoside Rg2 and ginsenoside Rg1 to ginsenoside Rh1 using the recombinant 관-glucosidase.</P>