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Identification of genes required for decolorization of crystal violet in <i>Citrobacter</i> sp. MY-5
Kim, Ji-Youn,Lee, Young-Mi,Jang, Moon-Sun,Kang, Dong-Woo,Kim, Seok-Jo,Kim, Cheorl-Ho,Lee, Young-Choon The Microbiology Research Foundation 2005 The Journal of general and applied microbiology Vol.51 No.3
Kim, Young-Ok,Kim, Han-Woo,Park, In-Suk,Lee, Jeong-Ho,Lee, Sang-Jun,Kim, Kyung-Kil The Microbiology Research Foundation 2009 The Journal of general and applied microbiology Vol.55 No.5
<P><I>Citrobacter braakii </I>produced an intracellular acid glucose phosphatase (AgpC) which was purified 986 fold to homogeneity with the specific activity of 286 units/mg. AgpC hydrolyzed a wide variety of phosphorylated compounds with high activity for glucose-1-phosphate and glucose-6-phosphate. The optimum pH and temperature for the enzyme activity was pH 5.0 and 45°C, respectively. The <I>Km </I>value for glucose-1-phosphate was 5.12 mM with a <I>Vmax </I>27.8 U mg<SUP>-1</SUP>. Its molecular weight was 46 kDa by SDS-PAGE gel and the sequence of N-terminal amino acid residues identified was Gln-Thr-Ala-Pro-Glu-Gly-Tyr-Gln-Leu-Gln. The glucose-1-phosphatase gene (<I>agpC</I>) was cloned from the <I>C. braakii </I>genomic library. This gene comprised 1,242 nucleotides and encoded a polypeptide of 413 amino acids. The result of its BLAST search showed a significant similarity with glucose-1-phosphatase from enterobacteria such as <I>E. coli</I>, <I>Enterobacter</I>, <I>Shigella</I>, and <I>Salmonella</I><I>.</I></P>
Yoon, Won Suck,Choi, Hyuk Jin,Park, Yong Keun The Microbiology Research Foundation 2011 The Journal of general and applied microbiology Vol.57 No.2
<P>IL-12 is known to be an essential cytokine which appears to provide protective immunity against intracellular bacteria, such as <I>Salmonella</I>. In this study, we investigated the possibility of developing a vaccine using IL-12 against virulent <I>Salmonella</I>. We used the host defense system activated by cytokine IL-12. The highly virulent <I>Salmonella </I>strain (<I>Salmonella typhimurium </I>UK-1) was transformed with cytokine-expressing plasmids. These live, wild-type pathogens were used as vaccine strains without undergoing any other biological or genetic attenuating processes. The newly developed strains induced partial protection from infections (30-40%). Of note, the interleukin-12-transformed pathogen was safe upon immunization with low doses (10<SUP>3</SUP> cfu), induced IgG responses, and stimulated protective immune responses against <I>Salmonella typhimurium </I>in mice (80-100%). These results suggest that IL-12 induced attenuation of wild-type <I>Salmonella </I>in the host infection stage and vaccine development using the wild-type strain harboring plasmid-secreting IL-12 may be considered as an alternative process for intracellular bacterial vaccine development without the inconvenience of time-consuming attenuation processes.</P>
Kim, Bong-Hyun,Lee, Ji Yeon,Lee, Peter C. W. The Microbiology Research Foundation 2015 The Journal of general and applied microbiology Vol.61 No.4
<P>A fungal strain producing high levels of phytase was purified to homogeneity from Penicillium oxalicum KCTC6440 (PhyA). The molecular mass of the purified PhyA was 65 kDa and optimal activity occurred at 55°C. The enzyme was stable in a pH range of 4.5-6.5, with an optimum performance at pH 5.5. The Km value for the substrate sodium phytate was 0.48 mM with a Vmax of 672 U/mg. The enzyme was inhibited by Ca(2+), Cu(2+), and Zn(2+), and slightly enhanced by EDTA. The PhyA efficiently released phosphate from feedstuffs such as soybean, rich bran and corn meal. The PhyA gene was cloned in two steps of degenerate PCR and inverse PCR and found to comprise 1501 bp and encode 461 amino acid residues. The enzyme was found to have only 13 amino acids differing to the known PhyA from other Penicillium sp., but has distinct enzyme characteristics. Computational analysis showed that PhyA possessed more positively charged residues in the active sites compared to other PhyA molecules, which may explain the broader pH spectrum.</P>