• Title/Summary/Keyword: Hydrolysis Reaction

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Extraction of anti-microalgal material from Laminaria spp. and effect of oligo-alginate derivatives on membrane potential (다시마 유래 항미세조류 물질 추출 및 알긴산 올리고 유도체의 막전위에 대한 영향)

  • Lee, Gunsup;Chang, Man;Shin, Kyoungsoon;Kim, Donggiun;Auh, Chung-Kyoon;Lee, Taek-Kyun
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.13 no.12
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    • pp.6196-6202
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    • 2012
  • Oligo-alginate derivatives were extracted from brown algae and its antimicroalgal effects and reaction mechanism were investigated. Oligo-alginate derivatives were produced from sequential hydrolysis of high molecular weight alginate by treatment of 2 N HCl and 1% $H_2O_2$. Antimicroalgal activity of extracts was proportional to reaction time and activity was highest at 4 hrs. When oligo-alginate derivatives were treated to Akashiwo sanguinea and Cochlodinium polykrikoides, mobilities of cells were ceased. A. sanguinea cells were crushed and plasmolysis was induced in C. polykrikoides cells. To investigate the action mechanism of oligo-alginate derivatives, changes of intracellular (pHi) and extracellular pH (pHe) were determined in the microalgal cells exposed to 0.05% of oligo-alginate derivatives. pHi was decreased about 0.3 unit and pHe was increased about 0.9 unit. These results suggested that change of membrane potential by oligo-alginate derivatives could led to microalgal cell death.

Antimicrobial activity of protein hydrolysate by protease (효소 단백 가수분해물의 항균 활성)

  • Joo, Jeong-Hyeon;Yi, Sang-Duk;Lee, Jeong-Ok;Oh, Man-Jin;Rhee, K.C.
    • Korean Journal of Agricultural Science
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    • v.29 no.2
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    • pp.78-90
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    • 2002
  • This study was carried out to investigate whether peptide produced from wheat protein by enzyme hydrolysis can be used as a natural antimicrobial agent. Antimicrobial peptide was obtained from wheat protein by protease of 7 species. The produced antimicrobial peptide was purified through ultrafiltration, membrane filtration and HPLC, and molecular weight and amino acid sequence of the purified antimicrobial peptide were determined. Among hydrolysate produced from wheat protein by protease of 7 species, antimicrobial activity was observed for the peptide obtained from Asp. saito protease. The Asp. saito protease did production antimicrobial hydrolysate showing the highest antimicrobial activity at reaction condition of $37^{\circ}C$ and pH 6.0, but not at reaction condition above $50^{\circ}C$. Wheat protein hydrolysate was fractionated by membrane filtration and showed antimicrobial activity between molecular weight 1,000 - 3,000. The antimicrobial activity fraction obtained by membrane filtration was separated through HPLC and showed antimicrobial activity in the peak of retention time 31.1 - 31.8 min. Since after wheat protein protease hydrolysate was heated during 15 min at $121^{\circ}C$, antimicrobial activity was maintained, we could be conviction as heat-stable peptide. Molecular weight of antimicrobial peptide identified by MALDI-mass was 1,633. Amino acid sequence of antimicrobial peptide was cysteine, glycine, prolin, prolin, prolin, valine, valine, alanine, alanine and arginine.

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Superhydrophilicity of Titania Hybrid Coating Film Imposed by UV Irradiation without Heat-treatment (저온 경화형 초친수성 티타니아 하이브리드 졸의 제조와 친수성 특성 평가에 관한 연구)

  • Kim, Won-Soo;Park, Won-Kyu
    • Journal of Technologic Dentistry
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    • v.29 no.1
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    • pp.121-131
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    • 2007
  • A preparation process's conditions of aqueous sol which contains anatase-type nano titania particles with photocatalyic properties was established by using Yoldas process, so called, DCS(Destabilization of Colloidal Solution) process in this study. And crystal size change and phase transformation of titania particles in aqueous titania sol depending on reaction conditions was investigated by a light scattering method and XRD analysis of frozen dried powders, respectively. This sol with photo catalytic nano titania particles was used to the following hydrophilic hybrid coating film's fabrication and its properties was evaluated. Subsequently, for coating film using the above mentioned aqueous titania sol, non-aqueous titania sol was prepared without any chemical additives and its time stability according to aging time was investigate. By using the above mentioned aqueous titania sol and non-aqueous sol, a complex oxide coating sol for metal and ceramic substrate and a organic-inorganic hybrid coating sol for polymer substrate was prepared and it's hydrophilicity depending on UV irradiation conditions was evaluated. As a conclusions, the following results were obtained. (1)Aqueous titania sol The average particle size of titania in formed aqueous titania sol was distributed between 20$\sim$90nm range depending on reaction conditions. And the crystal phase of titania powders obtained by frozen drying method was changed from amorphous state to anatase and subsequently transformed to rutile crystal phase and it is attributed to concentration gradient in aqueous sol. (2)Non-aqueous titania sol Non-aqueous titania sol was prepared using methanol as a solvent and a little distilled water for hydrolysis and nitric acid as a catalyst were used. The obtained non-aqueous titania sol was stable at room temperature for 20 days. Additionally, non-aqueous titania sol with addition of chealating reagent such as acethylaceton and ethylene glycol prolonged the stability of sol by six months. (3)Complex sol and hybrid sol with super hydrophilicity The above mentioned aqueous titania sol as a main photocataylic component and non-aqueous titania sol as a binder for coating process was used to prepare a complex sol used for metal, ceramic and wood material substrate and also to prepare the organic-inorganic hybrid sol for polymer substrate such as polycarbonate and polyethylene, in which process APMS(3-Aminopropyltrimethoxysilane), GPTS(3-Glycidoxypropyl-trimethoxysilane) as a hydrophilic silane compound and HEMA(2-Hydroxyethyl methacrylate) as a forming network in hybrid coating film were used. The hybrid coating film such as prepared through this process showed a superhydrophilicity below 1$10^{\circ}$ depending on processing conditions and a pencil's hardness over 6 H.

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The Evidence for Pepsin-Catalyzed Transpeptidation (펩신촉매에 의한 Transpeptide의 생성)

  • 조용권
    • Journal of Life Science
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    • v.8 no.4
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    • pp.410-415
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    • 1998
  • Procine pepsin hydrolysis of hexapeptide L-S-pNF-Nle-A-OMe in the presence of dipeptide L-L generates a new peak on HPLC analysis of reaction mixtures that is not seen when enzyme is incubated with either peptide alone. The peaks can be detected spectroscopically at either 214 or 254 nm, the latter consistent with a new peptide containing the p-nitro-F residue. The data suggest acyl transpeptidation between E(L-S-pNF) and L-L to form L-S-pNF-L-L. Consistent with this inference are (1) the ability of L-L-NH$_{2}$ and inability of Boc-L-L to undergo a similar transpeptidation reaction, and (2) the data from electrospray mass spectrum. This synthesis requires that Nle-A-L-OMe be released before L-S-pNF, an order opposite to that proposed on the basis of product inhibition kinetics. Consistent with this inference are reciprocal solvent isotope effects ; normal isotope effects of 1.736$\pm$0.121 on the formation of Nle-A-L-OMe and 2.281$\pm$0.184 in the formation of L-S-pNF, coupled to an inverse isotope effects of 0.576$\pm$0.045 on the formation of L-S-pNF-L-L. Because transpeptidation precedes faster in D$_{2}$O, the isotopically-sensitive step must occur after release of Nle-A-L-OMe. Isotopically-enhanced transpeptidation is consistent with the Uni-Bi iso memchanism postulated on the basis of an isotope effects on Vmax but not on Vmax/Km$^{1)}$ and confirmed by isotope effects on the onset of inhibition by pepstatin$^{2)}$.

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Optimal Production of Xylooligosaccharide by Using Recombinant Endoxylanase from Bacillus subtilis (Bacillus subtilis 유래 재조합 endoxylanase를 이용한 xylooligosaccharide의 최적 생산)

  • Kim, Yeon-Hee;Heo, Sun-Yeon;Kim, Mi-Jin;Lee, Jae-Hyung;Kim, Young-Man;Nam, Soo-Wan
    • Journal of Life Science
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    • v.18 no.1
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    • pp.52-57
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    • 2008
  • Xylan is a major hemicellulose component of the cell walls of monocots and hardwood, representing up to 30% of the dry weight of these plants. To efficiently hydrolyze xylan, the endoxylanase gene from Bacillus sp. was expressed in B. subtilis DB431 by introducing the plasmid pJHKJ4. The total activity of the recombinant endoxylanase reached about 857 unit/ml by batch fermentation of B. subtilis DB431/pJHKJ4 in LB maltose medium. The majority (>92%) of endoxylanase was efficiently secreted into the culture medium. The recombinant endoxylanase hydrolyzed more the birchwood xylan efficiently than the other xylans. When 4 % concentration of xylan was used, the highest production of xylooligosaccharide was observed, and xylobiose and xylotriose were the major products. Optimal amount of enzyme and reaction time for producing xylooligosaccharide were found to be 10 unit and 1 hr, respectively. In addition, the temperature of $40^{\circ}C{\sim}50^{\circ}C$ gave the highest production of xylooligosaccharide. Consequently, the optimized conditions for the production of xylooligosaccharide through the hydrolysis of xylan were determined as follows: 10 unit endoxylanase, $50^{\circ}C$, 4% birchwood xylan, 1 hr reaction.

Swelling Ratio and Mechanical Properties of SBR/organoclay Nanocomposites according to the Mixing Temperature; using 3-Aminopropyltriethoxysilane as a Modifier and the Latex Method for Manufacturing (유기화제로 3-aminopropyltriethoxysilane 을 이용하여 라텍스법으로 제조된 SBR/organoclay 컴파운드의 혼련 온도에 따른 팽윤도 및 기계적 물성)

  • Kim, Wook-Soo;Park, Deuk-Joo;Kang, Yun-Hee;Ha, Ki-Ryong;Kim, Won-Ho
    • Elastomers and Composites
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    • v.45 no.2
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    • pp.112-121
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    • 2010
  • In this study, styrene butadiene rubber(SBR)/organoclay nanocomposites were manufactured using the latex method with 3-aminopropyltriethoxysilane(APTES) as a modifier. The X-ray diffraction(XRD), transmission electron microscopy(TEM) images, Fourier transform infrared(FTIR) spectroscopy, swelling ratio and mechanical properties were measured in order to study the interaction between filler and rubber according to the mixing temperature in the internal mixer. In the case of SBR/APTES-MMT compounds, the dispersion of the silicates within the rubber matrix was enhanced, and thereby, the mechanical properties were improved. The characteristic bands of Si-O-C in APTES disappeared after hydrolysis reaction in the MMT-suspension solution and the peak of hydroxyl group was increased. Therefore the formation of chemical bonds between the hydroxyl group generated from APTES on the silicate surface and the ethoxy group of bis(triethoxysilylpropyl) tetrasulfide(TESPT) was possible. Consequently, the 300% modulus of SBR/APTES-MMT compounds was further improved in the case of using TESPT as a coupling agent. However, the silanization reaction between APTES and TESPT was not affected significantly according to the increase of mixing temperature in the internal mixer.

Physicochemical Characteristics for the Transformation of Blue Pigments from Genipin of Gardenia jasminoides with Amino Acids (치자 Genipin과 아미노산의 청색소변환반응에 관한 물리화학적 연구)

  • Lee, Jae-Youn;Hahn, Tae-Ryong;Paik, Young-Sook
    • Applied Biological Chemistry
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    • v.41 no.5
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    • pp.399-404
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    • 1998
  • Genipin was obtained from hydrolysis of geniposide isolated from gardenia fruits with ${\beta}-glucosidase$. Reaction of genipin with glycine, alanine, histidine, lysine, phenylalanine and glutamate in aqueous buffer solution converted colorless starting materials to blue pigments. Effect of pH for the formation of blue pigments was tested using UV/Vis spectrophotometer. The optimum pH for the formation of blue pigments was 7.0. No pigment and trace amounts were formed at acidic (pH 3.0) and alkaline (pH 12.0) conditions, respectively. The amount and tincture of blue color were distinct with different amino acids. In contrast with lysine $({\lambda}_{max}=573\;nm)$, glycine $({\lambda}_{max}=595\;nm)$, phenylalanine $({\lambda}_{max}=602\;nm)$ and alanine $({\lambda}_{max}=595\;nm)$, the reaction of genipin with histidine $({\lambda}_{max}=601\;nm)$ and glutamate $({\lambda}_{max}=601\;nm)$ produced relatively small amounts of blue pigments. Rate constants for the formation of blue pigments from genipin with amino acids at various temperatures $(60,\;70,\;80,\;90^{\circ}C,\;pH\;7.0\;phosphate\;buffer)$ were obtained. Rate constants of genipin with basic amino acids were larger than neutral or acidic amino acids. Arrhenius activation energies of the formation of blue pigments indicated that activation energy of glycine $(E_A=9.8\;kcal/mol)$ was especially lower than those of other amino acids $(E_A=13.3{\sim}15.4\;kcal/mol)$.

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Purification and Characterization of an Invertase Produced with Saccharomyces cerevisiae JS59 Isolated from Home-made Wine (포도주에서 분리한 Saccharomyces cerevisiae JS59가 생성하는 Invertase의 정제 및 특성)

  • Yoo, Ji-Soo;Paik, Hyun-Dong;Kim, Soo-Young;Lee, Si-Kyung
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.40 no.9
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    • pp.1321-1327
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    • 2011
  • The microorganism producing an invertase (E.C. 3.2.1.26) was isolated from wine and tentatively identified as Saccharomyces cerevisiae by cellular fatty acid analysis. The invertase was purified to homogeneity by ammonium sulfate precipitant, dialysis, ion-exchange chromatography on DEAE-Sephadex A-50, and gel chromatography on Sephadex G-200 from the culture supernatant of Saccharomyces cerevisiae JS59. The specific activity and the purification fold of the purified invertase were 7620.9 unit/mg protein and 13.9, respectively. The molecular weight of the purified invertase was estimated to be 38.5 kDa by SDS-PAGE. The optimum pH and temperature for the invertase activity were pH 5 and $55^{\circ}C$, respectively. The invertase activity was relatively stable at pH 4~6 and temperature $55^{\circ}C$. The activity of invertase was inhibited by $Ag^{2+}$ and $Hg^{2+}$, but on the contrary, activated by $Co^{2+}$ and $Mn^{2+}$. Michaelis constant ($K_m$) for invertase reaction in sucrose solution was 11.5 mM. TLC analysis of the products produced in sucrose solution during invertase reaction showed the progressive presence of glucose and fructose in accordance with sucrose hydrolysis.

Chemical Reactions in Surfactant Solutions(Ⅲ). Nucleophilic and Micellar Catalyses on Hydrolysis of an Organic Phosphate by Sodium 2-Alkylbenzimidazole-5-sulfonates in Aqueous and CTABr Solutions (계면활성제 용액속에서의 화학반응(제3보) 유기인산 에스테르의 가수분해반응에 미치는 2-알킬벤즈이미다졸-5-술포네이트의 친핵적 및 미셀 촉매효과)

  • Hong, Yeong Seok;Park, Hui Hyeon;Park, Han Seok
    • Journal of the Korean Chemical Society
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    • v.34 no.6
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    • pp.629-636
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    • 1990
  • Dephosphorylation of p-nitrophenyldiphenylphosphate(p-NPDPP) mediated by anions of sodium 2-alkylbenzimidazole-5-sulfonate(R-BI-SO$_3$Na) in CTABr micellar solutions are obviously slower than that by anion of sodium benzimidazole-5-sulfonate(BI-SO$_3$Na), and the reation rates were decreased with increase of lengths of alkyl groups. This presents a striking contrast to the reactions in aqueous solutions without added CTABr, of which the reaction rates are on approximately same levels. It seems due to steric effect of alkyl groups of R-BI$^-$SO$_3$Na in the Stern layer of micelle, and it is supported by measured activation parameters(△H$^\neq$/TEX>, △G$^\neq$/TEX> and △S$^\neq$/TEX>) of the reactions in aqueous and micellar solutions. In addition to nucleophilic ability of benzimidazole moiety of R-BI$^-$SO$_3$Na on the reactions, these compounds with long alkyl groups(nonyl to pentadecyl) are micellized for themseleves, and increase the reaction rates due to their micellar catalyses in aqueous solutions, not including CTABr.

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Production and Characterization of Cyclodextrin Glucanotransferase fronm Bacillus sp. JK-43 Isolated from Kimchi (김치 분리균인 Bacillus sp. JK-43이 생산하는 Cyclodextrin Glucanotransferase의 생산 및 특성)

  • Jun, Hong-Ki;Bae, Kyung-Mi;Kim, Young-Hee;Baik, Hyung-Suk
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.29 no.1
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    • pp.41-48
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    • 2000
  • A bacterial strain, designated as JK-43, producing extracellular cyclodextrin glucanotransferase (CGTase)[EC 2.4.1.19] was isolated from kimchi. The CGTase from isolated strain JK-43 showed the transglucosylation activity from soluble starch to L-ascorbic acid(AA) compared to those obtained from other strains. A main product formed by this reaction was identified as $2-O-{\alpha}-glucopyranosyl$ L-ascorbic acid(AA-2G) by testing its susceptibility to ${\alpha}-glucosidase$ hydrolysis, the HPLC profiles, and through the elementary analysis. the ${\beta}-CD,\;{\gamma}-CD$, potato starch and corn starch were identified to be suitable glucosyl donor for transglucosylation reaction on AA by CGTase. Acceptor specificity on AA-2G production was examined by use of AA, Iso-AA and AA-2P. Transglucosylation was observed toward AA-2P as well as AA and Iso-AA. The microorganism isolated from kimchi was identified as a strain of Bacillus sp. JK-43 based on the morphological, cultural, biochemical characteristics and partial 16SrDNA sequence analysis. The maximal CGTase production was observed in a medium containing 1.0% soluble starch, 1.0% yeast extract, 1.0% $Na_2CO_3\;0.1%\;K_2HPO_4,\;and\;0.02%\;MgSO_4{\cdot}7H_2O$ with initial pH 7.0. The strain was cultured at $37^{\circ}C$ for 26 hrs with reciprocal shaking.

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