• Korean Chemical Engineering Research
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• v.46 no.3
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• pp.581-584
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• 2008

The catalyst carriers of the mesoporous layer compounds were prepared to carry out the partial oxidation of methane(POM) to hydrogen. The catalytic activities of POM to hydrogen were investigated over Ru(3)/SPK and Ru(3)/SPM catalyst in a fixed bed flow reactor under atmosphere. In addition, the catalysts and carriers were characterized by BET, TEM, TPR. The BET surface areas of the silica-pillared $H^+-kenyaite$(SPK) and the silica-pillared $H^+-magadite$(SPM) were $760m^2/g$ and $810m^2/g$, repectively, and the average pore sizes were 3.0 nm and 2.6 nm, repectively. The nitrogen adsorption isotherms were type IV with developed hysteresis. The TEM showed that the mesoporous layer compounds were formed well. The Ru(3)/SPK and the Ru(3)/SPM catalyst were obtained high hydrogen yields(90%, 87%), and were kept constant high hydrogen yields even about 60 hours at 973 K, $CH_4/O_2=2$, $1.25{\times}10^{-5}g-Cat.hr/ml$. The TPR peaks of Ru(3)/SPK and the Ru(3)/SPM catalyst showed the similar reducibilities around 453 K and 413 K. It could be suggested that SPK and SPM had the physicochemical properties as oxidation catalyst carries from these analysis data.

• The Korean Journal of Mycology
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• v.12 no.4
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• pp.133-140
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• 1984

Some properties of cellulolytic enzymes produced by Pleurotus sajor-caju JAFM 1017 during its growth in synthetic medium were investigated. The optimum pH of avicelase, CMCase, and ${\beta}-glucosidase$ was pH 5.5, pH 4.5 and pH 6.0, respectively. Avicelase and CMCase were stable within pH 5.0 to 6.0 and 4.0 to 6.0, respectively, and ,${\beta}-glucosidase$ was within pH 5.5 to 6.5. The optimum temperature of avicelase, CMCase and ${\beta}-glucosidase$ was the same of $40^{\circ}C$. The enzymes were stable below the optimum temperature, but the enzymes were unstable over the temperature of $50^{\circ}C$, and avicelase was losing about 91.7% of activity at $70^{\circ}C$ for 10 min. The enzyme activity of avicelase and CMCase was increased in proportion to the substrate concentration within 1% and 0.7%, respectively, and ${\beta}-glucosidase$ was within 0.1%. The Michaelis constants (Km) of avicelase and CMCase were 30.77mg avicel/ml and 14.64m Na-CMC/ml, respectively and ${\beta}-glucosidase$ was 5. 13mg salicin/ml. The reducing sugar production of avicelase was proportionaly increased until 120 min. and CMCase and ${\beta}-glucosidase$ were until 60min. The activity of three cellulolytic enzymes were increased by $Ca^{2+}$ at the concentration of $10^{-2}M$, but were inhibited by $Hg^{2+}$, $Ag^+$.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.26 no.3
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• pp.214-220
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• 1993

Browning of ascidian, Halocynthia roretzi, meat occurres very rapidly when skinned off or cut during processing and it resulted the quality loss of fresh frozen, dehydrated or fermented products. In this study, the causes of color development and prevention of browning were experimented. The browning of ascidian meat may be occurred enzymatically by a tyrosinase contained in meat and viscera which acted specifically on L-tyrosine as a substrate rather than on catechol. Activity of the enzyme in viscera was three times higher than in meat. The optimum pH and temperature on the tyrosinase activity of crude enzyme obtained from ascidian was 6.0 and $30{\sim}35^{\circ}C$, respectively. The enzyme was inactivated heating at $80^{\circ}C$ for 3 minutes or $90{\sim}100^{\circ}C$ for 1 minute and it was inhibited by $0.1{\sim}0.5mM$ solutions at ascorbic acid, sodium hydrogen sulfite, cystein, citric acid, cyanide but only sodium hydrogen sulfite treatment was effective to retard such a high content of enzyme as in case of viscera. In practical use for processing of ascidian meat browning was retarded by dipping the viscera removed ascidian meat in 0.2M citric acid for 5 minutes or $0.2\%$ sodium hydrogen sulfite solution for 1 minute resulting in sulfur dioxide residue less than 100 ppm.