• Natural Product Sciences
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• 제3권1호
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• pp.71-74
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• 1997

Cell suspension cultures of Solanum mammosum transformed inoculated salicyl alcohol into salicin $(salicyl\;alcohol\;2-0-{\beta}-D-glucopyranoside)$. The highest level of salicin (59.3 mg/flask) in the cells was formed within 3 days after inoculating with salicyl alcohol (50 mg /flask containing 50 ml medium). The glucosylation capability of salicyl alcohol by cell suspension cultures of S. mammosum was relatively higher than that reported previously.

• Journal of Ginseng Research
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• 제20권3호
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• pp.284-290
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• 1996

To Identify phenolic components known to exist in Korean ginseng (Panax ginseng C.A. Meyer) by GC/MS, three derivatization methods were employed for their analyses. First, phenolic components in ether soluble acidic fraction prepared from Korean red ginseng powder were taimethylsilylated. Secondly, phenolic acids in the same fraction were esterified with diazomethane followed by trlmethylsilylation. Thirdly, acidic components in ginseng powder were extracted and esterified concurrently by methanolic sulfuric acid, followed by fractionation of phenolic components with Silica Sep-Paka and trimethylsilylatlon. All phenolic components found in ginseng except gen tisic acid were identified by retention times and mass spectrums of standards. Besides, 5 phenolic components including salicyl alcohol and 1-H-indole-2-carboxylic acid were first identified from Korea an red ginseng by GC/MS.

• KSBB Journal
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• 제19권5호
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• pp.363-367
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• 2004

Leuconostoc mesenteroides NRRL B-1149 produces various glucoseyltransferases for the synthesis of dextran, levan and glucose-1-phosphate using sucrose as a substrate. A sucrose phosphorylase (1149SPase) was purified from L. mesenteroides NRRL B-1149 culture by using hollow fiber filtration (30 kDa cut off), Toyopearl DEAE 650 M column chromatography and following two times of DEAE-Sepharose column chromatographies. The specific activity of the purified 1149SPase was 25.7 (U/mg) with $16\%$ yield. The 1149SPase showed a molecular size of 56 kDa on denatured $10\%$ SDS-PAGE. The N-terminal amino acid sequence of the enzyme was MEIQNKAM. The optimum pH and temperature of this enzyme were 6.2~6.5 and 37^{circ}C, respectively. It had an apparent K_{m} of 6.0 mM and K_{cat} of 1.62/s for sucrose. 1149SPase crystal was formed by hanging drop diffusion technique using 20 mM calcium chloride dihydrate, 100 mM sodium acetate trihydrate pH 4.6 and $30\%$ 2-methyl-2,4-pentanediol as vaporizing and reservation solution. The 1149SPase catalyzes transferring of glucose from isomaltose or sucrose to salicin and salicyl alcohol by disproportionation reaction or acceptor reaction and synthesized two acceptor products, respectively.