• Journal of the Korean Chemical Society
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• v.17 no.2
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• pp.130-135
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• 1973

The rate-constants of hydrolysis of 3, 4-methylenedioxyphenylmethylenemalononitrile are determined by ultraviolet spectrophotometry at various pH and a rate equation which can be applied over wide pH range is obtained. The rate equation reveals that below pH 5.0 and above pH 9.0, the hydrolysis is initiated by the addition of water and hydroxide ion respectively. However, at pH 6.0-8.0 the competitive addition of water and hydroxide ion occurs. The catalytic contribution of hydroxide ion and water can be fully explained by the rate equation obtained.

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.485-489
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• 2003

Enzymatic hydrolysis of egg yolk Protein was carried out in continuous packed column reactor Five supports for enzyme immobilization were evaluated in this study. We investigated the optimum operation variables - pH, temperature, and flow rate in continuous reactor operation.

• YAKHAK HOEJI
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• v.8 no.1
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• pp.1-5
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• 1964

Present experiment in vivo shows that some conversions of active groups in chloramphenicol residue of ester, that is hydrolytic cleavage of dichloracetamide and glucuronide formation, seem to take place prior to hydrolysis. This result suggest that the enzymatic hydrolysis rate in vitro, is not available as an index for the evaluation of the chlorampherical ester potency.

• Bulletin of the Korean Chemical Society
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• v.29 no.12
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• pp.2477-2481
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• 2008

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.459-462
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• 2000

The pretreatment of used newspaper for the enzymatic digestion preprocess was performed on a percolation reactor and a batch reactor. The test condition of percolation process was $170^{circ}C$, 60min, 1 mL/min, and 400psi, that of batch was $40^{circ}C$, 3hr. and latm Reaction solutions used in pretreatment process were aqueous ammonia, sulfuric acid, water, and hydrogen-peroxide as an oxidizing agent. As a result, the effect of pretreatment was similar to batch and percolation process, but the yield of enzymatic hydrolysis was higher in batch than percolation. This batch pretreatment enhanced enzymatic hydrolysis rate and increased glucose yield from about 15 to 20%. The inhibition factors influenced the rate of enzymatic hydrolysis was investigated, and the ink contented newspaper was the major factor.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1978.10a
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• pp.208.2-208
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• 1978

Rice Straw was delignified by autoclaving with 1％ NaOH solution at $121^{\circ}C$ for one hour and was disintegrated by a Wiley mill to 60 mesh. This substrate was saccharified with cellulase produced by Trichoderma viride T04 in solid culture me-dium. The rate and extent of hydrolysis were both increased when high enzyme concentration and low substrate concentration were employed. The original cellulose was treated with 0.19 FPA unit for three hours and followed by the second treatment for the same period with the same concentration of enzyme after washing. By doing this the hydrolysis rate at the second stage could increase four folds of that unwashed. The same experiment with 0.32 FPA unit yielded two folds suggesting an end-product inhibition on the recaction system. The extent of hydrolysis however, could not be in-creased by this process.

• Biotechnology and Bioprocess Engineering:BBE
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• v.2 no.2
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• pp.101-104
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• 1997

Lactic acid production from ${\alpha}$-cellulose by simultaneous saccharification and fermentation (SSF) was studied. The cellulose was converted in a batch SSF using cellulase enzyme Cytolase CL to produce glucose sugar and Lactobacillus delbrueckii to ferment the glucose to lactic acid. The effects of temperature, PH, yeast extract loading, and lactic acid inhibition were studied to determine the optimum conditions for the batch processing. Cellulose was converted efficiently to lactic acid, and enzymatic hydrolysis was the rate controlling step in the SSF. The highest conversion rate was obtained at 46$^{\circ}C$ and pH 5.0. The observed yield of lactic acid from ${\alpha}$-cellulose was 0.90 at 72 hours. The optimum pH of the SSF was coincident with that of enzymatic hydrolysis. The optimum temperature of the SSF was chosen as the highest temperature the microoraganism could withstand. The optimum yeast extract loading was found to be 2.5g/L. Lactic acid was observed to be inhibitory to the microorganisms' activity.

• Journal of the Korean Ceramic Society
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• v.27 no.5
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• pp.625-630
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• 1990

Cordierite powders were prepared from Si(OC2H5)4, Al(OC3H7i)3 and Mg(OC2H5)2 by the sol-gel method. Two different methods were applied for producing fine and homogeneous powders. One is that Si(OC2H5)4 with a lowr rate of hydrolysis was partially hydrolyzed and then Al(OC3H7i)3 and Mg(OC2H5)2 were mixed and reacted. The other is based on the simultaneous hydrolysis of these metal alkoxides using i-C4H9OH which retards the rate of hydrolysis of Al(OC3H7i)3 and Mg(OC2H5)2. It was confirmed that ifne and homogeneous powders were obtained from both methods. Also these powders were calcined at four different temperatures during two hours. X-ray diffraction patterns show only ${\mu}$-cordierite phase at 1000$^{\circ}C$, ${\mu}$-cordierite and ${\alpha}$-cordierite phases at 1100-1200$^{\circ}C$ and ${\alpha}$-cordierite phase at 1300$^{\circ}C$ respectively.

• Bulletin of the Korean Chemical Society
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• v.18 no.8
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• pp.880-886
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• 1997

Ab initio calculations were carried out on the gas phase acid-catalyzed hydrolysis reactions of sulfinamide using the 3-21G* basis sets. Single point calculations were also performed at the MP2/6-31G* level. The first step in the acid-catalyzed hydrolysis of N-methylmethanesulfinamide, Ⅰ, involves protonation. The most favorable form is the O-protonated one, Ⅱ, which is then transformed into a sulfurane intermediate, Ⅲ, by addition of a water molecule. The reaction proceeds further by an intramolecular proton transfer from O to N (TS2), which is followed by N-S bond cleavage (TS3) leading to the final products. The rate determining step is the N-S bond cleavage (TS3) at the RHF/3-21G* level, whereas it becomes indeterminable at the MP2/6-31G*//3-21G* level of theory. However, the substituent effect studies with N-protonated N-arylmethanesulfinamide, ⅩⅢ, at the MP2/6-31G*//3-21G* level support the N-S bond breaking step as rate limiting.

• Bulletin of the Korean Chemical Society
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• v.11 no.3
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• pp.194-200
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• 1990

Various mechanistic aspects of the A2 hydrolysis of methyl acetimidate were explored using the MNDO method. As in thecorresponding reactions of acetamide and methyl carbamate, a proton transfer pre-equilibrium exists between the N-protonated and the O-protonated tautomers, and the subsequent hydrolysis proceeds from the more stable N-protonated form. Of the two reaction pathways, the $A_{AL}2$ path is favored in the gas phase and in concentrated acid solutions, whereas the $A_{AC}2$ path is favored in less acidic solutions with a stable cationic tetrahedral intermediate formed in the rate determining step. Negative charge development on the alkoxy oxygen in the transition state suggested a rate increase with the increase in the electron withdrawing power of the alkoxy group. Calculations on the reaction processes with AM1 indicated that MNDO is more reliable in this type of work, although AM1 is better than MNDO in reproducing hydrogen bonds.