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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>
Sathiyaraj, Gayathri,Srinivasan, Sathiyaraj,Kim, Ho-Bin,Subramaniyam, Sathiyamoorthy,Lee, Ok Ran,Kim, Yeon-Ju,Yang, Deok Chun Sociedade Brasileira de Microbiologia 2011 Brazilian journal of microbiology Vol.42 No.2
<P><I>Cylindrocarpon destructans</I> isolated from ginseng field was found to produce pectinolytic enzymes. A Taguchi’s orthogonal array experimental design was applied to optimize the preliminary production of polygalacturonase (PG) and pectin lyase (PL) using submerged culture condition. This method was applied to evaluate the significant parameters for the production of enzymes. The process variables were pH, pectin concentration, incubation time and temperature. Optimization of process parameters resulted in high levels of enzyme (PG and PL) production after ten days of incubation at a pH of 5.0 at 25°C in the presence of 1.5% pectin. Among different nitrogen sources, urea and peptone showed high production of PG and PL, respectively. The enzyme production and mycelial growth seems to have direct influence on the culture conditions; therefore, at stationary state high enzyme production and mycelial growth were obtained than agitation state. Along with this, optimization of enzyme activity was also determined using various physiological parameters like, temperature, incubation time and pH. Taguchi’s data was also analyzed using one step ANOVA statistical method.</P>
Song, Ok-Ryul,Lee, Seung-Jin,Lee, Yong-Seok,Lee, Sang-Cheol,Kim, Keun-Ki,Choi, Yong-Lark Sociedade Brasileira de Microbiologia 2008 Brazilian journal of microbiology Vol.39 No.1
<P>A mineral phosphate solubilizing bacterium, <I>Burkholderia cepacia</I> DA23 has been isolated from cultivated soils. Phosphate-solubilizing activities of the strain against three types of insoluble phosphate were quantitatively determined. When 3% of glucose concentration was used for carbon source, the strain had a marked mineral phosphate-solubilizing activity. Mineral phosphate solubilization was directly related to the pH drop by the strain. Analysis of the culture medium by high pressure liquid chromatography identified gluconic acid as the main organic acid released by <I>Burkholderia cepacia</I> DA23. Gluconic acid production was apparently the result of the glucose dehydrogenase activity and glucose dehydrogenase was affected by phosphate regulation.</P>
Oh, Chulhong,Nikapitiya, Chamilani,Lee, Youngdeuk,Whang, Ilson,Kang, Do-Hyung,Heo, Soo-Jin,Choi, Young-Ung,Lee, Jehee Sociedade Brasileira de Microbiologia 2010 Brazilian journal of microbiology Vol.41 No.4
<P>An agar-degrading <I>Pseudoalteromonas</I> sp. AG52 bacterial strain was identified from the red seaweed <I>Gelidium amansii</I> collected from Jeju Island, Korea. A β-agarase gene which has 96.8% nucleotide identity to <I>Aeromonas</I> β-agarase was cloned from this strain, and was designated as a<I>ga</I>A. The coding region is 870 bp, encoding 290 amino acids and possesses characteristic features of the glycoside hydrolase family (GHF)-16. The predicted molecular mass of the mature protein was 32 kDa. The recombinant β-agarase (rAgaA) was overexpressed in <I>Escherichia coli</I> and purified as a fusion protein. The optimal temperature and pH for activity were 55 °C and 5.5, respectively. The enzyme had a specific activity of 105.1 and 79.5 unit/mg toward agar and agarose, respectively. The pattern of agar hydrolysis demonstrated that the enzyme is an endo-type β-agarase, producing neoagarohexaose and neoagarotetraose as the final main products.</P><P>Since, <I>Pseudoalteromonas</I> sp. AG52 encodes an a<I>ga</I>A gene, which has greater identity to <I>Aeromonas</I> β-agarase, the enzyme could be considered as novel, with its unique bio chemical characteristics. Altogether, the purified rAgaA has potential for use in industrial applications such as development of cosmetics and pharmaceuticals.</P>