• Journal of Microbiology
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• v.35 no.1
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• pp.15-20
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• 1997

Kinetic studies were done to elucidate the reaction mechanism of purine nucleoside phosphorylase (PNP) in Micrococcus Luteus. PNP catalyzes the reversible phosphorolysis of ribonucleosides to their respective base. The effect of alternative competing substrates suggested that a single enzyme was involved in binding to the active site for all purine nucleosides, inosine, deoxyiosine, guanosine, deoxyguanosine, adenosine and deoxyadenosine. Affinity studies showed that pentose moiety reduced the binding capacity and methylation of ring N-1 of inosine and guanosine had little effect on binding to bacterial enzyme, whereas these compounds did not bind to the mammalian enzymes. The initial velocity and product inhibition studies demonstrated that the predominant mechanism of reaction was an ordered bi, bi reaction. The nucleoside bound to the enzyme first, followed by phosphate. Ribose 1-phosphate was the first product to leave, followed by base.

• Preventive Nutrition and Food Science
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• v.7 no.1
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• pp.33-36
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• 2002

A catalase from Micrococcus sp. isolated from soil was applied to degrade hydrogen Peroxide in wastewater from a semiconductor industry. The degradation rates of hydrogen peroxide increased with increasing reaction time and catalase concentrations in the reaction mixture. However, in the presence of aluminum chloride or chloride oxide used in detergent compounds, the degradation rate of hydrogen peroxide was not affected. Enzyme stabilizers and antifoam did not affect the degradation rates of hydrogen peroxide.

• Journal of the korean veterinary medical association
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• v.7 no.5
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• pp.9-15
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• 1963

Two cases of gangrenous mastitis of goats occured naturally at Feb. 1962 in Taegu area were observed clinically In other hand the strains of micrococcus isolated the animals were examined bacteriologically. The results were summeriged as follows: 1. The c

• Plant Disease and Agriculture
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• v.5 no.1
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• pp.41-45
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• 1999

Bacterial population densities on soybean pods from Chungnam province ranges 105~106 CFU/$\textrm{cm}^2$, whereas those of bacteria causing sprout rot ranged 0~103 CFU/$\textrm{cm}^2$. Erwinia chrysanthemi, Xanthomonas campestris pv. glycines, Staphylococcus sp., and Micrococcus sp. were identified as pathogenic bacteria causing soybean sprout rot. The population density of X. campestris pv. glycines was higher than those of other bacteria.

• Bulletin of the Korean Chemical Society
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• v.28 no.9
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• pp.1591-1594
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• 2007

• Proceedings of the Korean Society of Life Science Conference
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• 2001.09a
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• pp.79-80
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• 2001

• Applied Biological Chemistry
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• v.36 no.6
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• pp.539-546
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• 1993

This paper describes the purification and partial characteristics of aminopeptidase from Microccus sp. LL3 to utilize the microorganism as a potential agent for industrial application for the purpose of shortening ripening period of cheddar cheese. The optimal temperature and pH for enzyme activity were $35^{\circ}C$ and 7.0, respectively for L-leucine-p-nitroanilide as substrate. The enzyme remained stable for 10 minutes up to $50^{\circ}C$. The activity of aminopeptidase was stimulated by $Mg^{++}$ ion but strongly inhibited by $Hg^{++}$, metal complexing reagents, ethylenediaminetetraacetate (EDTA) and 1,10-phenanthroline. The enzyme was thought to be metallopeptidase. This enzyme had a broad substrate specificity, but was inactive on peptide with arginine as N-terminal amino acid. An intracellular aminopeptidase from Micrococcu sp. LL3 was purified by chromatography on DEAE-Sephacel and filtration on Sepacryl S-300. The enzyme has a molecular weight of 43,500.

• Korean Journal of Food Science and Technology
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• v.45 no.2
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• pp.248-251
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• 2013

The purpose of this study was to investigate the inactivation effect of intense pulsed light (IPL) on Micrococcus roseus, an irradiation-resistant bacterium isolated from laver, and the commercial feasibility of this sterilization method on dried laver. The inactivation of M. roseus in cultivated plates increased with increasing light intensity and treatment time. Approximately 6.6 log CFU/mL reduction of the cell viability was achieved with IPL treatment for 3 min at 1,000 V of light intensity, tailing was not shown. In addition, the inactivation rate of M. roseus increased with increasing pulse number at same light intensity and treatment time. The killing efficiency for M. roseus increased with by decreasing the distance between the light source and the sample surface.

• Korean Journal of Microbiology
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• v.45 no.1
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• pp.69-73
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• 2009

Proteases are degradative enzymes which hydrolyze a peptide bond between amino acids and they are abundantly applied to commercial field. In order to investigate optimal medium compositions of carbon and nitrogen source for enzyme production, modified STY medium containing 0.15% yeast extract were used as basal medium. When galactose was used as carbon source, enzyme activity showed 1.3 higher than that of glucose. For nitrogen source addition of casamino acids to basal medium in place of tryptone showed lowest activity, whereas addition of malt extract showed maximal activity. The optimum temperature and pH of extracellular protease were found to be $35^{\circ}C$ an pH 8.5.

• Journal of the Korean Chemical Society
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• v.37 no.7
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• pp.677-682
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• 1993

Polyacryloylcephalexine and polymethacryloylcephalexine were prepared by the reaction of polyacryloylchloride or polymethacryloyl chloride with cephalexine. The antimicrobial activities of these polymeric drugs were investigated by the common twofold dilution technique and the minimum inhibitory concentration (MIC) of polymeric durgs was also examined. Polyacryloylcephalexine revealed an excellent antibacterial activity against Micrococcus luteus ATCC 9341, Escherichia coli ESS, Bacillus subtilis ATCC 6633, Staphylococcus aureus ATCC 25923, Mycobacterium phlei IFO 3158, Klebsiella pueumouiae KCTC 1560, Escherichia coli KCTC 1039, Salmonella typhimurium KCTC 1925. Polymethacryloylcephalexine revealed an excellent antibacterial activity against Micrococcus luteus ATCC 9341, Klebsiella pueumouiae KCTC 1560, Bacillus subtilis ATCC 6633, Staphylococcus aureus ATCC 25923, Mycobacterium phlei IFO 3158, Escherichia coli KCTC 1039, Escherichia coli ESS, Salmonella typhimurium KCTC 1925.