• Title/Summary/Keyword: Carboxyl groups

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Manufacturing of Enzyme Immobilized Sheet Using Carboxymethylated RMP Substrate (카르복시메틸화 RMP를 이용한 효소 고정화시트의 제조)

  • 조남석
    • Journal of Korea Technical Association of The Pulp and Paper Industry
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    • v.35 no.2
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    • pp.39-45
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    • 2003
  • This study was performed to develop the new type enzyme immobilization sheet from carboxymethylated refiner mechanical pulp (CRMP) substrate. Enzyme immobilization was attempted to couple carboxyl groups of CRMP with amino groups of the enzyme, trypsin, through the reaction of carbodiimide reagent, 1-ethyl-3-(3-dimethyl aminopropyl)-carbodimide (EDC ). Immobilization carrier, water insoluble CRMP fraction (CRMP-IS), was successfully reacted with the enzyme, formed peptide linkage like -CONH- at 1680$cm^{-1}$ / and new ester linkage like -COO$CH_3$, methylester at 1735$cm^{-1}$ /, and produced enzyme immobilized substrate (CRMP-IST). The enzyme immobilized handsheet was prepared by mixing the above chelated enzyme immobilized substrate(CRMP-IST) with kraft pulp by paper sheet machine like papermaking process. The sheet weight and strength were increased with increasing dosage of CRMP-IST, and decreased at more than 10% mixing of CRMP-IST, but higher than the controls. Concerning activities of immobilized trypsin(CRMP-IST) sheet by caseinolysis, the teared-off sheet with shaking was shown higher enzyme activities than sheet shape without shaking. In conclusion, this enzyme immobilized sheet would be expected easy handling for practical application and reutilization.

Activated Carbon Fibers from Chemically Modified Coal Tar Pitches

  • Ryu, S.K.;Shim, J.W.;Yang, K.S.;Mochida, I.
    • Carbon letters
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    • v.1 no.1
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    • pp.6-11
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    • 2000
  • Coal tar pitch was chemically modified with 10 wt% benzoquinone (BQ) to raise the softening point of isotropic pitch precursor and the precursor was melt-spun into pitch fibers, stabilized, carbonized and activated with steam at $900^{\circ}C$. The weight loss of carbon fiber-benzoquinone (CF-BQ) increased with the increase of activation time like other fibers, but was lower than those of Kureha fiber at the same activation time in spite of larger geometric surface area. Those adsorption isotherms fitted into 'Type I' according to Brunauer, Deming, Deming and Teller classification. However, there was very thin low-pressure hysteresis that lower closure points of the hysteresis are about 0.42-0.45. From the pore size distribution curves, there might be some micropores having narrow-necked bottle; a series of interconnected pore is more likely than discrete bottles. FT-IR studies showed that the functional groups such as carboxyl, quinone, and phenol were introduced to ACFs-BQ surface after steam activation. Methylene blue decolorization and iodine adsorption capacity of ACF-BQ increased linearly with the increase of specific surface area and was larger than that of ACF-Kureha at the same specific surface area.

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Effect of surface modification of carbon felts on capacitive deionization for desalination

  • Lee, Jong-Ho;Ahn, Hong-Joo;Cho, Donghwan;Youn, Jeong-Il;Kim, Young-Jig;Oh, Han-Jun
    • Carbon letters
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    • v.16 no.2
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    • pp.93-100
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    • 2015
  • Surface modified carbon felts were utilized as an electrode for the removal of inorganic ions from seawater. The surfaces of the carbon felts were chemically modified by alkaline and acidic solutions, respectively. The potassium hydroxide (KOH) modified carbon felt exhibited high Brunauer-Emmett-Teller (BET) surface areas and large pore volume, and oxygen-containing functional groups were increased during KOH chemical modification. However, the BET surface area significantly decreased by nitric acid ($HNO_3$) chemical modification due to severe chemical dissolution of the pore structure. The capability of electrosorption by an electrical double-layer and the efficiency of capacitive deionization (CDI) thus showed the greatest enhancement by chemical KOH modification due to the appropriate increase of carboxyl and hydroxyl functional groups and the enlargement of the specific surface area.

Enzyme-Conjugated CdSe/ZnS Quantum Dot Biosensors for Glucose Detection

  • Kim, Gang-Il;Sung, Yun-Mo
    • Korean Journal of Materials Research
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    • v.19 no.1
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    • pp.44-49
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    • 2009
  • Conjugated nanocrystals using CdSe/ZnS core/shell nanocrystal quantum dots modified by organic linkers and glucose oxidase (GOx) were prepared for use as biosensors. The trioctylphophine oxide (TOPO)-capped QDs were first modified to give them water-solubility by terminal carboxyl groups that were bonded to the amino groups of GOx through an EDC/NHS coupling reaction. As the glucose concentration increased, the photoluminescence intensity was enhanced linearly due to the electron transfer during the enzymatic reaction. The UV-visible spectra of the as-prepared QDs are identical to that of QDs-MAA. This shows that these QDs do not become agglomerated during ligand exchanges. A photoluminescence (PL) spectroscopic study showed that the PL intensity of the QDs-GOx bioconjugates was increased in the presence of glucose. These glucose sensors showed linearity up to approximately 15 mM and became gradually saturated above 15 mM because the excess glucose did not affect the enzymatic oxidation reaction past that amount. These biosensors show highly sensitive variation in terms of their photoluminescence depending on the glucose concentration.

Surface Modification of Phosphoric Acid-activated Carbon in Spent Coffee Grounds to Enhance Cu(II) Adsorption from Aqueous Solutions

  • Choi, Suk Soon;Choi, Tae Ryeong;Choi, Hee-Jeong
    • Applied Chemistry for Engineering
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    • v.32 no.5
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    • pp.589-598
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    • 2021
  • The purpose of this study was to analyze the efficiency with which phosphorylated spent coffee grounds (PSCG) remove cationic Cu(II) ions from an aqueous solution. The pHpzc of the SCG was 6.43, but it was lowered to 3.96 in the PSCG, confirming that an acidic functional group was attached to the surface of the PSCG. According to FT-IR analysis, phosphorylation of the SCG added P=O, P-O-C (aromatic), P=OOH, and P-O-P groups to the surface of the adsorbent, and the peaks of the carboxyl and OH groups were high and broad. Also, the specific surface area, mesopore range, and ion exchange capacity increased significantly by phosphorylation. The adsorption kinetics and isothermal experiments showed that Cu(II) adsorption using SCG and PSCG was explained by PSO and Langmuir models. The maximum Langmuir adsorption capacity of SCG and PSCG was 42.23 and 162.36 mg/g, respectively. The adsorption process of both SCG and PSCG was close to physical adsorption and endothermic reaction in which the adsorption efficiency increased with temperature. PSCG was very effective in adsorbing Cu(II) in aqueous solution, which has great advantages in terms of recycling resources and adsorbing heavy metals using waste materials.

Lipase Treatment of Polyester Fabrics

  • Kim, Hye-Rim;Song, Wha-Soon
    • Fibers and Polymers
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    • v.7 no.4
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    • pp.339-343
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    • 2006
  • The aim of this paper is to improve moisture regain of PET fabrics using a lipase treatment. Effects of nine lipase sources, lipase activator and nonionic surfactant on moisture regain of PET fabrics are examined. Moisture regains of lipase-treated samples improve by two times in average compared with untreated and buffer-treated samples. Alkaline treatment creates larger pitting by more aggressive attack into fiber which is proved by SEM and water contact angle measurement. Moisture regain by alkaline treatment ($0.568%{\pm}0.08$) does not improve. However, lipase-treatment (L2 treatment) improves moisture regain up to 2.4 times ($1.272%{\pm}0.05$). Although lipase treatment is more moderate than alkaline treatment, lipase hydrolysis on PET fabrics improves moisture regain, efficiently. K/S values improved confirm that carboxyl and hydroxyl groups are produced on the surface of PET fabrics by lipase hydrolysis. Moisture regain and dyeability improve by lipase hydrolysis on PET fabrics.

Enzymatic synthesis of sugar esters of L-lysine and L-aspartic acid

  • Jeon, Gyu-Jong;Park, O-Jin;Sin, Mun-Sik;Yang, Ji-Won
    • 한국생물공학회:학술대회논문집
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    • 2001.11a
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    • pp.646-647
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    • 2001
  • The enzymatic synthesis of conjugates of lysine and aspartic acid with D-glucose was studied. Optimase M-440 showed the very poor regioselectivity in the transesterification of $N{\alpha}$,$N'{\varepsilon}-di-t-Boc-L-Lys-OTFE$ and N-t-Boc-L-Asp-diOTFE with D-glucose. The acylation of glycosidic -OH and primary -OH of D-glucose occurred. However, Optimase M-440 catalyzed only the acylation of primary -OH group in the transesterification of $N{\alpha}$,$N'{\varepsilon}-di-t-Boc-L-Lys-OTFE$ and N-t-Boc-L-Asp-diOTFE with ${\alpha}-$ and ${\beta}-methylglucopyranoside$ in high yields without any other transesterification. Optimase M-440 also discriminated carboxyl groups of N-t-Boc-L-Asp-diOTFE.

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Surface Interactions of Model Peptides for Mussel Adhesive Protein

  • Cho, Eun-Kyung;Lee, Yoon-Hee;Cho, Nam-Jun;Cha, Hyung-Joon
    • 한국생물공학회:학술대회논문집
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    • 2003.10a
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    • pp.630-633
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    • 2003
  • The mussel adhesive protein Mefp-1 is a natural, strong and durable adhesive that is stable under corrosive, saline conditions. Mefp-1 is found in the marine mussel Mytilus edulis and it has a molecular weight of ca. 130,000. The primary structure is mainly composed of repeating decapetides: Ala-Lys-Pro -Ser-Tyr Hyp-Hyp-Thr-DOPA-Lys. To elucidate the mechanism by which Mefp-1 bonds to metal surfaces, we have used surface-enhanced Raman spectroscopy to study the interactions of peptides related to the Mefp-1 decapeptide repeat with gold surfaces. We have concluded that the tyrosine residue and the carboxyl terminus interact strongly with the gold surface, and that proline and hydroxyproline constrain the conformations of the peptides, thereby limiting the types of possible interactions of the functional groups with the gold surface.

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Removal Characteristics of Lead by Immobilizing Agents and Immobilized Seaweed (고정화제와 고정화된 해조류에 의한 납의 제거 특성)

  • 이학성;서정호;서근학
    • Journal of Environmental Health Sciences
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    • v.27 no.1
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    • pp.83-87
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    • 2001
  • In this study, the characteristics of lead removal by PVA and alginate bead which used widely as immobilizing agents were investigated, and the difference of removal amounts between pure PVA/alginate bead and Sargassum thunbergii immobilized bead was studied. All PVA beads, pure and S. thunbergii immobilized, reached an equilibrium state in about 1 hour, and S. thunbergii immobilized bead adsorbed more lead than pure one. But in the case of alginate beads, they needed much time, about 5 hours, to reach an equilibrium state, and adsorbed lead four times higher than PVA beads. Therefore, it was considered that alginate beads had more mass transfer resistance and function groups which adsorb lead such as hydroxyl, carboxyl and etc. than PVA bead. To examine the continuous usage of alginate beads, the process of adsorption/desorption of lead was conducted repeatedly. As the process proceeded, the amounts of lead adsorption decrease, so it was indicated that the non-desorbed lead from alginate bead at first adsorption/desorption process remained constantly.

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Stabilization of Subtilisin Carlsberg in Polar Organic Solvents by Chemical Modification (화학적 변환에 의한 Subtilisin Carlsberg의 극성 유기용매에서의 안정성 향상)

  • 류근갑
    • KSBB Journal
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    • v.11 no.2
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    • pp.186-192
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    • 1996
  • The effects of chemical modification on the enzymes' stability in polar organic solvents were studied with subtilisin Carlsberg in dimethylformamide-water mixtures as a model system. Three out of nine lysine residues of subtilisin Carlsberg were coupled to either trimellilic or pyromellitic anhydrides thereby, for each lysine residue modified, resulting in the net replacement of one basic amino group by two or three acidic carboxyl groups, respectively. In water at 60$^{\circ}C$, both trimellitic and pyromellitic anhydride-modified subtilisin Carlsberg showed increased thermostability by 2.6 times and 1.6 times, respectively, as compared to that of unmodified enzyme. In 70% dimethylformamide at 25$^{\circ}C$, however, only pyromellitic acrid was shown to enhance the stability of subtilisin Carlsberg by 5.5 times increasing the half life time of irreversible inactivation from 4.9hr for unmodified enzyme to 27.8hr for modified enzyme.

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