• Title/Summary/Keyword: endo/exo

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A Study on the Reaction Pathway for Isomerization of Tetrahydrotricyclopentadiene Using Ionic Liquid Catalyst (이온성 액체 촉매를 이용한 Tetrahydrotricyclopentadiene의 이성화 반응 경로에 관한 연구)

  • Kim, Dae Hyun;Han, Jeong-Sik;Jeon, Jong-Ki;Yim, Jin-Heong
    • Applied Chemistry for Engineering
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    • v.26 no.3
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    • pp.366-371
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    • 2015
  • The kinetic behavior of tetrahydrotricyclopentadiene (THTCPD) isomerization was studied by using two kinds of chloroaluminate ionic liquid (IL) catalyst with different Lewis acidity. THTCPD isomerization pathway was discussed under the different temperature and time as reaction parameters using IL catalysts consisting of 1-butyl-3-methylimidazolun chloride $(BMIC)/AlCl_3$ with low acidity and pyridine hydrochloride $(PHC)/AlCl_3$ with high acidity. The conversion of THTCPD isomerization increased with increasing Lewis acidity of IL catalyst. The THTCPD isomerization pathway changed as a function of reaction temperature and catalyst acidity. In the case of $BMIC/AlCl_3$ IL catalyst, THTCPD isomerization pathway was similar to that of using conventional $AlCl_3$ catalyst. However, two different types of additional pathways (endo, exo, endo-NB ${\rightarrow}$ exo, exo, endo-NB ${\rightarrow}$ exo, exo, exo-NB and endo, exo, endo-NB ${\rightarrow}$ exo, exo, endo-NB ${\rightarrow}$ exo, exo, exo-CP) were appeared when using $PHC/AlCl_3$ IL catalyst.

The Degradation of Paper Cultural Properties by Cellulase (셀룰라아제에 의한 지류 문화재의 분해)

  • 장영훈
    • KSBB Journal
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    • v.17 no.6
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    • pp.549-554
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    • 2002
  • The hydrolysis of old book(Hanji) was performed using endoglucanase Ⅰ(endo Ⅰ), and exoglucanase II(exe II) and their mixtures purified from Trichoderma viride cellulase. The optimum degradation of old book(Hanji) with endo Ⅰ, exo II and endo-exo mixture(Ⅰ:Ⅰ) were exhibited at pH 4.5, 5.5, 5.0, respectively. Maximum degradations using endo Ⅰ, exo II and endo-exo mixture(Ⅰ:Ⅰ) occurred at 50$\^{C}$. The yield decreased an increasing the enzyme concentration. Especially, the yield was lowest for treatment with the endo Ⅰ-exo II mixture(Ⅰ:Ⅰ), which may be regarded as being due to a synergistic action of the cellulase components. Physical strength increased with increasing exo II concentration, and decreased with increasing concentration of endoglucanase Ⅰ. These results indicated that the degradation of old book(Hanji) depends largely upon the action of endoglucanase. Therefore, the most effective method of conserving paper cultural properties is to repress the action of endoglucanase.

Purification and Properties of Polygalacturonase from Ganoderma lucidum (Ganoderma lucidum이 생산하는 Polygalacturonase의 정제 및 특성)

  • Yoon, Sook;Kim, Myung-Kon;Hong, Jai-Sik;Kim, Myeong-Sook
    • The Korean Journal of Mycology
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    • v.22 no.4
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    • pp.298-308
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    • 1994
  • The properties of polygalacturonase by Ganoderma lucidum in liquid culture were investigated. The enzyme was composed of an endo- and an exo-polygalacturonase. The endo- and exo-polygalacturonase were purified approximately 56 and 9.2-fold, respectively, through ammonium sulfate fractionation, gel filtration on Biogel P-100, anion exchange chromatography on DEAE-cellulose, gel chromatography on Sephadex G-150 and re-gel chromatography on Sephadex G-150. The endo- and exo-polygalacturonase had higher affinity for apple pectin than for citrus pectin or pectic acid. The Km values of the endo- and exo-polygalacturonase for apple pectin, determined on the Lineweaver-Burk plot, were 1.44 and 10.6 mg $ml^{-1}$ for apple pectin, respectively. Purified endo-polygalacturonase was found to be homogeneous electrophoretically and had a molecular weight of 54,000 estimated on SDS polyacrylamide gel. The optimal pH for the activity of the enzymes was 4.0. The endo- and exo-polygalacturonase were stable in the pH range of 4.0 to 6.0 and 3.5 to 5.5, respectively. The optimal temperatures of the endo- and exo-polygalacturonase were 40 and $60^{\circ}C$, respectively. The exo-polygalacturonase was more resistant to heat than the endo-polygalacturonase, requiring heating for 40 min at $80^{\circ}C$ for complete inactivation. The activity of the endo-polygalacturonase was increased by $Ca^{++}$ and $Mn^{++}\;ions$, while that of the exo-polygalacturonase was increased by $Ca^{++}\;ion$ only, and was not affected by $Mn^{++}\;ion$.

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Production and Inhibition of Cellulolytic and Pectolytic Enzymes by Cylindrocarpon destructans(Zins.) Scholten Causing Root Rot of Ginseng (인삼뿌리썩음병균, Cylindrocarpon destructans에 의한 섬유소분해효소 및 펙틴질분해효소의 분필 및 억제)

  • Lee Jin Woo;Chung Hoo Sup
    • Korean journal of applied entomology
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    • v.13 no.1 s.18
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    • pp.1-10
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    • 1974
  • The activities of pectolytic and cellulolytic enzymes produced from slices of ginseng root infected with Cylindrocarpon destructains(Zins.) Scholtern were proportional to each concentration and reaction time. Activities of cellulase(Cx), endo-polygalacturonase(endo-PG), endo-polymethylg-alacturonase(endo-PMG), exo-polygalacturonase(exe-PG), and exe-polymethylgalacturonase(exo-PMG) were maximum on the 4th day after inoculation. No endo-PG and endo-PMG were detected at the first and second days, while exo-PG exo-PMG were active. On the 6th day, all pectic enzymes were completely lost, whereas Cx remained at a high concentration. pH optima of Cx, endo-PG, endo-PMG, exo-PG, and exo-PMG were 6.0, 5.5, 8.0, 7.0 to 7.5, and 8.5, respectively. Temperature optima of Cx, endo-PG, endo-PMG exo-PG, and exo-PMG were $66^{\circ}C\;53^{\circ}C\;41^{\circ}C\;37^{\circ}C\;and\;40^{\circ}C$, respectively. Cx was only inhibited by $0.05M\; Hg^{++}$ among 16 ions tested. Inhibitory effects of ions on pectolytic enzymes varied, however$M Fe^{+++}\;and\;0.05M\;Al^{+++}$ were the best in general. Among 8 fungicides, none of them inhibited all the enzymes studied at $0.1\%$, active ingredients. Exo-PG were highly inhibited by all of the fungicides, of which difolatan was the most inhibitory to all the pectic enzymes. $Ca^{++}\; at\; 0.02M\; and\;Fe^{+++}\;at\;0.02M$ completely inhibited all the pectolytic enzymes, and Cx was inhibited $30\%$ and $70\%$ at the same concentration, respectively Formalin almost inhibited exo-PG and exe-PMG at $0.8\%$ but not the other enzymes especially Cx. Difolatan at $0.8\%$ inhibited all the enzymes concerned above $80\%$. The cellulolytic and pectolytic enzymes of C. destructans must be closely associated with the ginseng root rot and should be inhibited to control the disease effectively.

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Adsorption Characteristic of Endo I and Exo II Purified from Cellulase by Trichoderma viride on Celluloses with Different Crystallinity (결정성이 다른 셀룰로오스에 대한 Trichoderma viride속 Cellulase로부터 분리한 Endo I 및 II의 흡착특성)

  • 김동원;홍영관;장영훈;이재국
    • KSBB Journal
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    • v.13 no.2
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    • pp.162-167
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    • 1998
  • The adsorption behaviors of two major cellulase components, endo I and exo II, from Trichoderma viride were investigated using $\alpha$-celluloses with different correlation crystallinity index(Cc) as substrates. The adsorption of cellulase enzyme components was significantly affected by the reaction condition and the physicochemical properties of the cellulose. The $\alpha$-cellulose was hydrolyzed in the presence of cellulase for various periods. The correlation crystallinity index of $\alpha$-cellulose increased with increasing the hydrolysis time. The adsorption was apparently found to obey the first-order kinetics, and the adsorption activation energy(Ea) was calculated from the adsorption rate constant(ka). The value of adsorption rate constant for endo I was larger than that of exo II. This means that endo I are adsorbed more rapidly than exo II. With the increase in correlation crystallinity index, the values of the adsorption rate constants for endo I and exo II decreased, respectively. The activation energy for the adsorption of exo II on the cellulose also was larger than that of endo I. Also adsorption activation energy of endo I and exo II increased with an increase in the crystallinity of sample cellulose.

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Global and Local Competition between Exogenously Introduced microRNAs and Endogenously Expressed microRNAs

  • Kim, Doyeon;Kim, Jongkyu;Baek, Daehyun
    • Molecules and Cells
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    • v.37 no.5
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    • pp.412-417
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    • 2014
  • It has been reported that exogenously introduced micro-RNA (exo-miRNA) competes with endogenously expressed miRNAs (endo-miRNAs) in human cells, resulting in a detectable upregulation of mRNAs with endo-miRNA target sites (TSs). However, the detailed mechanisms of the competition between exo- and endo-miRNAs remain uninvestigated. In this study, using 74 microarrays that monitored the whole-transcriptome response after introducing miRNAs or siRNAs into HeLa cells, we systematically examined the derepression of mRNAs with exo- and/or endo-miRNA TSs. We quantitatively assessed the effect of the number of endo-miRNA TSs on the degree of mRNA derepression. As a result, we observed that the number of endo-miRNA TSs was significantly associated with the degree of derepression, supporting that the derepression resulted from the competition between exo- and endo-miRNAs. However, when we examined whether the site proficiency of exo-miRNA TSs could also influence mRNA derepression, to our surprise, we discovered a strong positive correlation. Our analysis indicates that site proficiencies of both exo- and endo-miRNA TSs are important determinants for the degree of mRNA derepression, implying that the derepression of mRNAs in response to exo-miRNA is more complex than that currently perceived. Our observations may lead to a more complete understanding of the detailed mechanisms of the competition between exo- and endo-miRNAs and to a more accurate prediction of miRNA targets. Our analysis also suggests an interesting hypothesis that long 3'-UTRs may function as molecular buffer against gene expression regulation by individual miRNAs.

Hypoglycemic Effect of Exo- and Endo-biopolymers Produced by Submerged Mycelial Culture of Ganoderma lucidum in Streptozotocin-Induced Diabetic Rats

  • Yang, Byung-Keun;Michael A Wilson;Cho, Kai-Yip;Song, Chi-Hyun
    • Journal of Microbiology and Biotechnology
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    • v.14 no.5
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    • pp.972-977
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    • 2004
  • The hypoglycemic effect of an exo-biopolymer (EXO) and endo-biopolymer (ENDO) produced from submerged mycelial culture of Ganoderma lucidum was investigated in streptozotocin (STZ)-induced diabetic rats. Both the EXO and ENDO showed hypoglycemic potential, however, the former proved to be more potent than the latter. The administration of the EXO at the dose of 100 mg/kg body weight (BW) significantly reduced the plasma glucose level (23.5%) and increased the plasma insulin level (2.2 fold) in the diabetic animals. The EXO also lowered the plasma total cholesterol, triglyceride, low-density lipoprotein (LDL) cholesterol, and athrogenic index by 14.7, 31.4, 24.1, and 45.4%, respectively, and reduced the liver total cholesterol and triglyceride levels by 6.7 and 25.8%, respectively. It increased the plasma high-density lipoprotein (HDL) cholesterol (37.7%), compared to the control group. Furthermore, the alanine transaminase (ALT) and aspartate transaminase (AST) showed lower activities in the EXO administered groups than the other experimental groups. Taken together, these results suggest that the exo-biopolymer may alleviate the blood glucose level by increased insulin secretion.

Effect of a Nonionic Surfactant on the Adsorption and Kinetic Mechanism for the Hydrolysis of Microcrystalline Cellulose by Endoglucanase Ⅰ and Exoglucanase II

  • 김동원;장영훈;정영규;손기향
    • Bulletin of the Korean Chemical Society
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    • v.18 no.3
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    • pp.300-305
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    • 1997
  • Effect of a nonionic surfactant, Tween 20 on the adsorption and kinetic mechanism for the hydrolysis of a microcrystalline cellulose, Avicel PH 101, by endoglucanase Ⅰ (Endo Ⅰ) and exoglucanase Ⅱ (Exo Ⅱ) isolated from Trichoderma viride were studied. The Langmuir isotherm parameters, amount of maximum adsorption (Amax) and adsorption equilibrium constant (Kad) for the adsorption, were obtained in the presence and the absence of nonionic surfactant. On the addition of Tween 20, the Kad and Amax values of Exo Ⅱ were decreased, while those of Endo Ⅰ were not affected. These indicate that the adsorption affinity of Exo Ⅱ on the cellulose is weakened by nonionic surfactant, and the surfactant enhanced desorption of Exo Ⅱ from insoluble substrate. The enzymatic hydrolysis of the cellulose can be described by two parallel pseudo-first order reactions using the percentages of easily (Ca) and hardly (Cb) hydrolyzable cellulose in Avicel PH 101 and associated rate constants (ka and kb). The Ca value was increased by adding Tween 20 for all enzyme samples (Exo Ⅱ, Endo Ⅰ and their 1:1 mixture) implying that the low-ordered crystalline fraction in the cellulose may be partly dispersed by surfactant. The ka value was not affect by adding Tween 20 for all enzyme samples (Exo Ⅱ, Endo Ⅰ and their 1:1 mixture). The kb value of Exo Ⅱ was increased by adding Tween 20, while that of Endo Ⅰ was not affected. This suggests that the surfactant helps the Exo Ⅱ desorb from microcrystalline cellulose, and increase the hydrolysis rate. These results were show that the increase of hydrolysis of cellulose by the nonionic surfactant is due to both the activation of Exo Ⅱ and partial defibrillation of the cellulose.

The Character Variation of Wood-Pulp treated Three Enzyme ; Endo-xylanase, Exo-xylanase and Acetyl-esterase (Endo-xylanase, Exo-xylanase 몇 Acetyl-esterase 효소 처리한 펄프의 특성 변화)

  • Kim, Byong-Hyun
    • Journal of the Korean Graphic Arts Communication Society
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    • v.26 no.1
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    • pp.17-28
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    • 2008
  • The wood-pulp is treated with the three enzymes; Endo-xylanase, exo-xylanase and acetyl-esterase. The maximum value of relative activity appeared 0.95 in acetyl-esterase at $40^{\circ}C$, 0.9 in exo-xylanase at $40^{\circ}C$, and 0.8 in endo-xylanase at $50^{\circ}C$, respectively. And it has measured 0.8 in endo-xylanase, 0.95 in acetyl-esterase at pH 6 and 0.9 in exo-xylanase at pH 5, while the maximum value of relative activity does not rely on reaction time for three enzymes treatment, and the value was about 0.9, respectively. We have watched that decreased Kappa number and increased brightness. And it turned out that the three enzyme produced a lot of reducing sugar with wood-pulp treatment.

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Hydrolysis of Inulin by Endo- and Exo-Inulinase (Endo- 및 Exo-Inulinase를 이용한 Inulin 가수분해)

  • 박선규;최용진
    • Microbiology and Biotechnology Letters
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    • v.19 no.1
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    • pp.52-56
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    • 1991
  • Inulin degradation was examined using patially puriiied enzyme mixtures of the Exo-inulinase from a Bacillus spp. and the Endo-inulinase from a Pseudomonas spp.. The highest synergistic xtion of the two cnzymcs was observcd when the Exo- and the Endo-inulinase werc mixed at the ratio of 1 to 13, and the rate of hydrolysis of the above process was enhanced approximately 1.6 times I1ight.1- than that of the reaction catalysed with a single enzyme of the same units. The enzymc mixture showed the maximal activity at pH 6.0 and $55^{\circ}C$, and in the prescncc of 0.5 mM each of $CO^{2+}$ and $Mn^{2+}$. Under the optimal condition described above fructosu was accumulated with the overitll concentration of 84% after 36 hours of the reiiction.

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