• 한국표면공학회:학술대회논문집
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• 한국표면공학회 2017년도 춘계학술대회 논문집
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• pp.126-126
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• 2017

Using first principles calculations we unveil fundamental mechanism of hydrolysis reactions of two hazardous chemicals $PCl_3$ and $POCl_3$ with molecular water clusters nearby. It is found that the water molecules play a key role as a catalyst significantly lowing the activation barriers by transferring its protons to the reaction intermediates. Interestingly, torsional angles of molecular complexes at transition states are identified as a vital descriptor on the reaction rate. Analysis of charge distribution over the complexes further reinforces the finding with atomic level correlation between the torsional angle and variation of the orbital hybridization state of P in the complex. Electronic charge separation (or polarization) enhances thermodynamic stability of the activated complex at transition state and reduces the activation energy through hydrogen bonding network with water molecules nearby. Calculated potential energy surfaces (PES) for the hydrolysis reactions of $PCl_3$ and $POCl_3$ depict their two contrastingly different profiles of double- and triple-deep wells, respectively. It is ascribed to the unique double-bonding O=P in the $POCl_3$. Our results on the activation free energy show well agreements with previous experimental data within $7kcalmol^{-1}$ deviation.

• Bulletin of the Korean Chemical Society
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• 제10권6호
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• pp.600-604
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• 1989

In order to find the rational methods for improving the thermal stability of subtilisin Carlsberg, the mechanisms of irreversible thermoinactivation of the enzyme were studied at $90^{\circ}C.$ At pH 4, the main process was hydrolysis of peptide bond. This process followed first order kinetics, yielding a rate constant of $1.26\;{\times}\;10^{-1}h^{-1}$. Hydrolysis of peptide bond of PMS-subtilisin occurred at various sites, which produced new distinct fragments of molecular weights of 27.2 KD, 25.9 KD, 25.0 KD, 22.3 KD, 19.0 KD, 17.6 KD, 16.5 KD, 15.7 KD, 15.0 KD, 13.7 KD, and 12.7 KD. Most of the new fragments originated from the acidic hydrolysis at the C-side of aspartic acid residues. However 25.0 KD, 15.7 KD, and 13.7 KD which could not be removed in purification steps stemmed from the autolytic cleavage of subtilisin. The minor process at pH 4 was deamidation at asparagine and/or glutamine residues and some extend of aggregation was also observed. However, the aggregation was main process at pH 7 with a first order kinetic constant of $16 h^{-1}.$ At pH 9, the main process seemed to be combination of deamidation and cleavage of peptide bond.

• Tribology and Lubricants
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• 제34권4호
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• pp.160-167
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• 2018

Vegetable oils can contribute to the goal of energy independence and security owing to their naturally renewable resources. One of the representative vegetable oils is biodiesel, which is being used in domestic and European markets as a blended fuel with automotive diesel. Vegetable oils are promising candidates as base fluids to replace petroleum lubricants because of their excellent lubricity and biodegradability. We prepared biodiesel with a purity of 99.9% via the esterification of waste cooking oil. Blended biodiesel and Petro-lube base oil were mixed to produce five types of mixed lubricating oil. We analyzed the various characteristics of the blended biodiesel with Petro-lube base oil for different blending ratios. The lubricity of the vegetable lubricant improves as the content of biodiesel increases. In addition, since zinc dialkyldithiophosphates (ZnDTPs) are widely used as multifunctional additives in petroleum-based lubricants, we optimized the blending ratio for lubricity, oxidation stability, and shear stability by adding ZnDTP as a performance additive to improve the biodiesel properties, such as oxidation stability and hydrolysis. The optimized lubricants improve by approximately 25% in lubricity and by 20 times in oxidation stability and shear stability after the addition of ZnDTP.

• Journal of Microbiology and Biotechnology
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• 제7권4호
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• pp.258-261
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• 1997

For the efficient production of lysophospholipid the hydrolysis of phospholipid using phospholipase $A_1$ from Serratia sp. MK1 was studied in an aqueous-solvent, a two-phase and an emulsion system. Judged on the basis of productivity and the degree of hydrolysis, the yield of lysophospholipid in a two-phase system was found to be better than that obtained in an emulsion system. Among the 13 organic solvents tested phospholipase $A_1$ showed the most efficient catalytic activity and stability in butyl acetate. When 20% phospholipid was used it was completely hydrolyzed in this two-phase system.

• 한국염색가공학회:학술대회논문집
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• 한국염색가공학회 2006년도 춘계학술발표회 논문집
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• pp.180-181
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• 2006

The hydrolysis of some vinylsulfonyl (VS) typed reactive dyes were investigated at the pH, temperature and other experimental conditions. The hydrolytic behaviour, especially, stability in various pH value, of the water soluble reactive dyes are examined. In neutral and acid condition, mother dyes are a quite stable. Other hand, it was found that dimerization and decomposition for these dyes were estimated in an aqueous alkaline medium. These alkaline hydrolysis behaviour was monitored by the high performance liquid chromatography.

• Biotechnology and Bioprocess Engineering:BBE
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• 제10권4호
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• pp.329-333
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• 2005

This study was designed to investigate the stability of a lipase fused with a cellulose­binding domain (CBD) to cellulase. The fusion protein was derived from a gene cluster of a CBD fragment of a cellulase gene in Trichoderma hazianum and a lipase gene in Bacillus stearother­mophilus L1. Due to the CBD, this lipase can be immobilized to a cellulose material. Factors affecting the lipase stability were divided into the reaction-independent factors (RIF), and the re­action-dependent factors (RDF). RIF includes the reaction conditions such as pH and tempera­ture, whereas substrate limitation and product inhibition are examples of RDF. As pH 10 and $50^{\circ}C$ were found to be optimum reaction conditions for oil hydrolysis by this lipase, the stability of the free and the immobilized lipase was studied under these conditions. Avicel (microcrystal­line cellulose) was used as a support for lipase immobilization. The effects of both RIF and RDF on the enzyme activity were less for the immobilized lipase than for the free lipase. Due to the irreversible binding of CBD to Avicel and the high stability of the immobilized lipase, the enzyme activity after five times of use was over $70\%$ of the initial activity.

• 생명과학회지
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• 제20권11호
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• pp.1656-1661
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• 2010

난황단백질 가수분해를 위한 알칼리성 단백질분해효소를 5가지 담체 Duolite A568, Celite R640, Dowex-1, Dowex 50W 그리고 Silica gel R60 에 고정화하였다. Duolite A568의 경우에 24.7%의 최대 고정화 효율을 나타내었다. 자유 효소와 고정화 효소에 대한 최적의 pH는 각각 8과 9였고, 최적의 pH는 고정화에 의해 염기성으로 1만큼 증가하였다. 그러나 최적 온도는 자유 효소와 고정화 효소 모두 $50^{\circ}C$로 같았다. 고정화 효소가 자유 효소에 비해 높은 열 안정성을 보였다. 재사용 회분식 공정에서 10 cycle 동안 효소활성은 초기 활성의 86%를 유지하였다. 연속 공정을 위한 충진층 반응기에서 여러 유속에 대한 장기 조업에서 효소 활성의 안정성 평가하였는데 낮은 유속일수록 높은 활성을 유지하였다. 연속 조업에서 casein과 난황 단백질을 사용하여 원료에 대한 고정화 효소의 활성에 대한 영향을 조사하였다. 96시간 연속 조업에서 casein의 경우는 초기 활성의 83%를 유지하였고 난황 단백질의 경우는 초기 활성의 61%를 유지하였다.

• Archives of Pharmacal Research
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• 제18권2호
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• pp.75-78
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• 1995

The analysis method nad stability test of antineoplaston A10, a new anticancer drug candidate, were established. A10 and phenylacetyl- L-glutamine, one of the degradation products, can be detected by high-performance liquid chromatography. The degradation kinetics of antineoplaston A10 in aqueous solutions from pH 1 to 10 buffers were carried out at 40, 50 and 60.deg.C. Pseudo-first order kinetics were obtained throughout the entire pH ranges studied. The pH-rate profiles showed that antineoplaston A10 was very unstable in alkaline conditions and most stable at pH 4.

• 생명과학회지
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• 제17권9호통권89호
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• pp.1260-1265
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• 2007

자석으로 분리가 가능한 ${\alpha}-Amylase$가 코팅된 나노고분자를 제조하여 녹말의 분해공정에 활용하였다. 본 연구에서 개발된 고정화 효소의 안정성은 크게 증가하여 상온에서 200rpm으로 교반하면서 보관한 경우 30일 동안에 92.7%의 활성도를 유지하였다 . 고정화 효소를 자석을 이용하여 재사용한 경우 10 회 동안 사용했을 경우 95.2%의 활성도 회수율을 보 여 효소의 재사용 가능성을 확인시켜 주었다 . 고정화 효소 0.5mg을 사용하여 녹말 분해 공정 에 활용하였을 때 2 ml의 40 g/l 녹말 용액을 40분만에 완전히 분해 시켰다, 이러한 고정화 효소를 사용하여 연속 효소반응기를 개발하여 녹말 분해공정에 활용한 결과 체류시간을 1시간으로 하였을 때 녹말 30 g/l를 76% 분해시켜 산업적으로 활용 가능성을 보여 주었다.

• 한국미생물·생명공학회지
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• 제25권2호
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• pp.166-172
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• 1997

Aspergillus niger was selected as a strain producing the potent raw starch hydorlyzing enzyme. These experiments were conducted to investigate the conditions of the glucoa- mylase production, the purification of the enzyme, some characteristics of the purified enzyme and hydrolysis rate on various raw starches such as com, rice, potato, glutinous rice, sweet potato, wheat and barley. The optimum cultural temperature and time for the enzyme production on wheat bran medium were $30^{\circ}C$ and 96hrs, respectively. The respective addition of yeast extract and nutrient broth on wheat bran medium increased slightly the enzyme production. The enzyme was purified by ammonium sulfate fractionation and DEAE-cellulose column chromatography. The specific activity of the purified enzyme was 30.7u/mg-protein and the yield of enzyme activity was 25.8%. The purified enzyme showed a single band on polyacrylamide disc gel electrophoresis and its molecular weight was estimated to be 56,000 by SDS-polyacrylamide disc gel electrophoresis. The isoelectric point for the purified enzyme was pH3.7. The optimum temperature and pH were $65^{\circ}C$ and pH 4.0, respectively. The purified enzyme was stable in the pH range of pH 3.0-9.5 and below $45^{\circ}C$, and its thermal stability was slightly increased by the addition of $Ca^{2+}$. The purified enzyme was activated by $Co^{2+},\;Sr^{2+},\;Mn^{2+},\;Fe^{2+},\;Cu^{2+}$. Raw rice starch, raw corn starch, raw glutinous rice starch, raw sweet potato starch, raw wheat starch and raw barley starch showed more than 90% hydrolysis rate in 48hrs incubation. Even raw potato starch, most difficult to be hydrolyzed, showed 80% hydrolysis rate. The purified enzyme was identified as glucoamylase.