• 한국진공학회:학술대회논문집
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• 한국진공학회 2012년도 제42회 동계 정기 학술대회 초록집
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• pp.557-557
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• 2012

Silicatein-${\alpha}$, the enzyme extracted from silica spicules in glass sponges, has been studied extensively in the way of chemistry from 1999, in which the pioneering work by Morse, D. E. - the discovery of the enzymatic hydrolysis in Silicatein-${\alpha}$ - was published. Since its reaction conditions are physiologically favored, synthesis of various materials, such as gallium oxide, zirconium oxide, and silicon oxide, was achieved without any hazardous wastes. Although some groups synthesized oxide films and particles, they have not achieved yet controlled morphogenesis in the reaction conditions mentioned above. With the knowledge of catalytic triad involved in hydrolysis of silicone alkoxide and oligomerization of silicic acid, we designed the novel peptide amphiphiles to not only form self-assembled structure, but also display similar activities to silicatein-${\alpha}$. Designed templates were able to self-assemble into left-handed helices for the peptide amphiphiles with L-form amino acid, catalyzing polycondensation of silicic acids onto the surface of them. It led to the formation of silica helices with 30-50 nm diameters. These results were characterized by various techniques, including SEM, TEM, and STEM. Given the situation that nano-bio-technology, the bio-applicable technology in nanometer scale, has been attracting considerable attention; this result could be applied to the latest applications in biotechnology, such as biosensors, lab-on-a-chip, biocompatible nanodevices.

• 한국염색가공학회지
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• 제5권4호
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• pp.10-19
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• 1993

Broad, mercerized broad, mercerized twill cotton fabrics and rayon fabric were treated with cellulase for 30~480 minutes at different temperature, concentration, time, and also treating methods such as continuously-treated or repeatedly-treated, and dyed with two direct dyes before or after enzyme treatment. From the experimental result by treating under the various conditions above, it was obtained that the weight loss increased more in thin fabric than thick one. In addition, it was considered that the treatment in 5$0^{\circ}C$ for 240 minutes brought about the ideal weight loss and flexible hand of the specimens. For both broad and mercerized broad, repeated treatment showed more weight loss than continuous. Direct dye on cotton fabric apparently inhibited hydrolysis. Ionic surfactants showed the inhibition effect of the catalytic hydrolysis of enzyme, on the other hand, nonionic surfactant did not.

• Journal of Microbiology and Biotechnology
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• 제24권4호
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• pp.440-446
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• 2014

The carbohydrate-binding module (CBM) is an important domain of most cellulases that plays a key role in the hydrolysis of cellulose. The neutral endoglucanase (EG1) gene was reconstructed. A redesigned endoglucanase, named EG2, was constructed with a CBM containing a linker from Corticium rolfsii (GenBank Accession No. D49448). The redesigned EG genes were expressed in Escherichia coli, and their characteristics are discussed. Results showed that the degradation of cellulose by EG2 was about double that by EG1. The specific activities of EG1 and EG2 were tested under optimal conditions, and EG2 had higher activity ($169.1{\pm}2.74$ U/mg) toward CMC-Na than did EG1 ($84.0{\pm}1.98$) in the process of cellulose degradation. The optimal pH and temperature, pH stability, and heat stability of EG1 and EG2 were similar. Results indicated that the CBM plays an essential role in the hydrolysis of cellulose. We can improve EG's catalytic power by adding the CBM from Corticium rolfsii.

• Biotechnology and Bioprocess Engineering:BBE
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• 제6권2호
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• pp.89-94
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• 2001

The binding of cellobiohydrolases to cullulose is a crucial initial step in cellulose hydrolysis. In the search for a detailed understanding of the function of cellobiohydrolases, much information concerning how the enzymes and their constituent catalytic and cellulose-binding changes during hydrolysis is still needed. The adsorption of purified two cellobiohydrolases (Ce17A and Ce16A) from Trichoderma reesei cellulase to microcrystalline cellulose has been studied. Cellobiohydrolase II (Ce16A) does not affect the adsorption of cellobiohydrolase I (Ce17A) significantly, and there are specific binding sites for both Ce17A and Ce16A. The adsorption affinity and tightness of the cullulase binding domain (CBD) for Ce17A are larger than those of the CBD for Ce16A. The CBD for Ce17A binds more rapidly and tightly to Avicel than the CBD for Ce16A. The decrease in adsorption observed when the two cellobihydrolases are studied together would appear to be the result of competition for binding sites on the cellulose. Ce17A competes more efficiently for binding sites than Ce16A. Competition for binding sites is the dominating factor when the two enzymes are acting together, furthermore adsorption to sites specific for Ce17A and Ce16A, also contributes to the total adsorption.

• 대한화학회지
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• 제59권3호
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• pp.238-245
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• 2015

The crystallization and morphology change of amorphous titanias by hydrothermal treatment have been investigated. The amorphous titanias were prepared by pure water hydrolysis of two different precursors, titanium tetraisopropoxide (TTIP) and TTIP modified with acetic acid (HOAc) and characterized prior to hydrothermal treatment. In order to avoid complicate situation, the hydrothermal treatment was performed in a single solvent water with and without strong acids at various temperatures. The effects of strong acid, temperature and time were systematically investigated on the transformation of amorphous titania to crystalline TiO₂ under simple hydrothermal condition. Without strong acid the titanias were transformed into only anatase phase nanoparticle regardless of precursor type, temperature and time herein used (up to 250 ℃ and 48 hours). The treatment temperature and time effected only on the crystalline size, not on the crystal phase et al. However, it was clearly revealed that the strong acids such as HNO₃ and HCl catalyzed the formation of rutile phase depending on temperature. HCl was slightly better than HNO₃ in this catalytic activity. The morphology of rutile TiO₂ formed was also a little affected by the type of acid. The precursor modifier, HOAc slightly reduced the catalytic activity of the strong acids in rutile phase formation.

• Journal of Microbiology and Biotechnology
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• 제17권7호
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• pp.1098-1105
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• 2007

Quantum mechanical and molecular dynamics simulation analysis has been performed on the model system for CALB (Candida antarctica lipase B) with esters to study the reaction mechanism and conformational preference of catalytic hydrolysis and the esterification reaction. Using quantum mechanical analysis, the ping-pong bi-bi mechanism was applied and energies and 3-dimensional binding configurations of the whole reaction pathways were calculated. Further molecular dynamics simulation analysis was performed on the basis of the transition state obtained from quantum mechanical study to observe the effect of structures of the substrates. Calculation results using substrates of different chain length and chiral configurations were compared for conformational preference. The calculated results showed very small influence on chain length, whereas chiral conformation showed big differences. Calculated results from molecular modeling studies have been compared qualitatively with the experimental data using racemic mixtures of (${\pm}$)-cis-4-acetamido-cyclopent-2-ene-1-ethyl acetate as substrates.

• 한국추진공학회:학술대회논문집
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• 한국추진공학회 2009년도 춘계학술대회 논문집
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• pp.331-334
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• 2009

본 연구에서는 우주 및 수중 동력원을 위한 연료전지 기반 공기 불요 추진 시스템을 개발하였다. 공기 불요 동력 시스템을 위해 과산화수소를 산화제로 선택하였고, 촉매 분해 반응을 통해 산소와 물을 발생하였다. 순수한 산소는 연료전지에 공급되고, 물은 분리한 후 저장된다. 본 연구에서는 고체 상태의 수소화붕소나트륨을 수소원으로 사용하였고, 촉매 가수분해 반응을 통해 순수한 수소를 발생할 수 있었다. 연료전지 기반 공기 불요 동력 시스템을 검증하기 위해 연료전지 시스템을 구축하였고 다양한 조건에서 평가를 수행하였다.

• BMB Reports
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• 제35권3호
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• pp.306-312
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• 2002

The effects of salts on the biochemical properties of D-amino acid aminotransferase from Bacillus sp. YM-1 have been studied to elucidate both the inhibitory effects of salts on the activity and the protective effects of salts on the substrate-induced inactivation. The results from UV-visible spectroscopy studies on the reaction of the enzyme with D-serine revealed that salt significantly reduced the rate of the formation of the quinonoid intermediate and its accumulation. The kinetic and spectroscopy studies of the reaction with $\alpha$-[$^2H$]-DL-serine in different concentrations of NaCl provided evidence that the rate-limiting step was changed from the deprotonation of the external aldimine to another step(s), presumably to the hydrolysis of the ketimine. Gel filtration chromatography data in the presence of NaCl showed that the enzyme volume was reduced sharply with the increasing NaCl concentration, up to 100 mM. An additional increase of the NaCl concentration did not affect the elution volume, which suggests that the enzyme has a limited number of salt-binding groups. These results provide detailed mechanistic evidence for the way salts inhibit the catalytic activity of D-amino acid aminotransferase.

• Journal of Microbiology and Biotechnology
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• 제15권2호
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• pp.296-301
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• 2005

The effect of aqueous methanol on the catalytic properties of porcine pancreatic lipase has been investigated. The k$_{CAT}$, values for the hydrolysis of N$^{alpha}$-benzyloxycarbonyl-L­lysine p-nitrophenyl ester at 0$^{circ}$C increased in a linear manner with increasing methanol concentration. However, the K$_{M}$ values were not influenced at methanol concentrations lower than $30\%$ and then began to increase at higher concentrations in an exponential fashion. Based on product analysis, the increase in k$_{CAT}$, with increasing methanol concentration can be accounted for by nucleophilic competition of methanol for the acyl enzyme intermediate, indicating that the rate-limiting step of the porcine pancreatic lipase-catalyzed reaction is deacylation under current experimental conditions. The exponential increase in K$_{M}$ at methanol concentrations higher than $30\%$ is attributed to the hydrophobic partitioning effect on substrate binding. There was no loss of lipase activity over a 4 h period in $60\%$ methanol concentration at pH$^{circ}$ 5.5 and 0$^{circ}$C. By monitoring the intrinsic fluorescence and absorbance, no evidence for structural changes by methanol was observed.

• Bulletin of the Korean Chemical Society
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• 제28권2호
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• pp.271-275
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• 2007

γ -Glutamyl transpeptidase (EC 2.3.2.2) plays a key role in glutathione metabolism by catalyzing the transfer of the γ -glutamyl residue and hydrolysis of glutathione. The functional residues at the active site of the rat kidney γ -glutamyl transpeptidase were investigated by kinetic studies at various pH, the treatment of diethylpyrocarbonate (DEPC), and photooxidation in presence of methylene blue. An ionizable group affecting the enzymatic activity with an apparent pKa value of 7.1, which is in the range of pKa values for a histidine residue in protein, was obtained by examining the pH-dependence of kinetic parameters. The pH effect on the photoinduced inactivation rate of the enzyme corresponds to that expected for the photooxidation of the free histidine. The involvement of a histidine in the catalytic site of the enzyme was further supported by DEPC modification accompanied by an increase in absorbance at 240 nm, indicating the formation of Ncarbethoxyhistidine. The histidine located at the position of 382 in the precursor of the enzyme is primarily suspected based on the amino acid sequence alignment of the transpeptidases from various organisms.