• Title/Summary/Keyword: Enzyme Conversion

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Sorbitol Production by Zymomonas mobilis Immobilized in Calcium Alginate Gels and Glutaraldehyde (알지네이트 및 글루타르알데하이드 고정화 Zymomonas mobilis에 의한 쏠비톨 생산)

  • Jung, In-Ho;Choi, Do-Jin;Park, Cheol-Jin;Chun, Uck-Han
    • Korean Journal of Food Science and Technology
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    • v.22 no.7
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    • pp.812-816
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    • 1990
  • This study describes the sorbitol production with permeabilized cells of Zymomonas mobilis immobilized in Ca-alginate. Toluene treated cells lose activity of glucose-fructose oxidoreductase due to the leaking of enzyme from the cells. To prevent this leakage, the permeabilized cells were treated with 0.25% glutaraldehyde by stirring for 1 h at room temperature. A continuous process with glutaraldehyde treated cells was developed and no significant reduction in the degree of conversion occurred during 210 h operation. The productivities were estimated to be about $7.2{\sim}7.5\;g/l-h$ for sorbitol at dilution rate $0.18\;h^{-1}$.

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Induction of Iron Superoxide Dismutase by Paraquat and Iron in Vitreoscilla $C_1$ (Vitreoscilla $C_1$에서 paraquat와 Iron에 의한 Iron Superoxide Dismutase의 유도)

  • 박기인
    • KSBB Journal
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    • v.18 no.6
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    • pp.517-521
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    • 2003
  • Superoxide dismutase which is metalloenzyme that decomposes superoxide radicals into hydrogen peroxide and molecular oxygen. Vitreoscilla has FeSOD. Expression of FeSOD to paraquat was largely constitutive. This suggests that the basal level of FeSOD is sufficient to provide protection against superoxide generated during normal aerobic metabolism. Induction of SOD by iron supports that insertion of the active site metal into the corresponding apoprotein. The effect of paraquat on induction by iron seemed that iron brought the synergism effect in SOD activity with paraquat. It suggests that the relief of growth inhibition is due to protection against the lethality of O$_2$afforded by the elevated SOD. There may be control of FeSOD activity posttranslationally. Posttranslation control of enzyme function is particularly feasible for a metalloenzyme, for which conversion of apo- to holoenzyme may be the rate-limiting or regulatory step.

The effects of low-protein diets and protease supplementation on broiler chickens in a hot and humid tropical environment

  • Law, Fang Lin;Zulkifli, Idrus;Soleimani, Abdoreza Farjam;Liang, Juan Boo;Awad, Elmutaz Atta
    • Asian-Australasian Journal of Animal Sciences
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    • v.31 no.8
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    • pp.1291-1300
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    • 2018
  • Objective: This experiment was conducted to investigate the effects of dietary crude protein (CP) level and exogenous protease supplementation on growth performance, serum metabolites, carcass traits, small intestinal morphology and endogenous protease activity in broiler chickens reared under a tropical climate. Methods: A total of 480 day-old male broiler chicks were randomly assigned to eight dietary treatments in a $4{\times}2$ factorial arrangement. The main effects were CP level (21.0%, 19.7%, 18.5%, or 17.2% from 1 to 21 days and 19.0%, 17.9%, 16.7%, or 15.6% from 22 to 35 days) and protease enzyme supplementation (0 ppm or 500 ppm). All experimental diets were fortified with synthetic feed-grade lysine, methionine, threonine and tryptophan to provide the minimum amino acid recommended levels for Cobb 500. Results: Reducing dietary CP linearly reduced (p<0.05) growth performance, serum albumin, total protein, and carcass traits and increased (p<0.05) serum triglycerides and abdominal fat. There was no consistent effect of reducing dietary CP on morphological parameters of the intestine and on the pancreatic and intestinal endogenous protease activity (p>0.05). Protease supplementation improved (p<0.05) feed conversion ratio, body weight gain, carcass yield and intestinal absorptive surface area. Conclusion: Protease supplementation, as measured by growth performance, intestinal morphology and carcass yield, may alleviate the detrimental effects of low protein diets in broiler chickens.

Kinetic Property and Phylogenie Relationship of 2-Hydroxy-muconic Semialdehyde Dehydrogenase Encoded in tomC Gene of Burkholderia cepacia G4

  • Reddy, Alavala-Matta;Min, Kyung-Rak;Lee, Kyoung;Lim, Jai-Yun;Kim, Chi-Kyung;Kim, Young-Soo
    • Archives of Pharmacal Research
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    • v.27 no.5
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    • pp.570-575
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    • 2004
  • 2-Hydroxymuconic semialdehyde (2-HMS) dehydrogenase catalyzes the conversion of 2-HMS to 4-oxalocrotonate, which is a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. A tomC gene that encodes 2-HMS dehydrogenase of Burkholderia cepacia G4, a soil bacterium that can grow on toluene, cresol, phenol, or benzene, was overexpressed into E. coli HB 101, and its gene product was characterized in this study. 2-HMS dehydrogenase from B. cepacia G4 has a high catalytic efficiency in terms of V$_{max}$K$_{max}$ towards 2-hydroxy-5-methyl-muconic semialdehyde followed by 2-HMS but has a very low efficiency for 5-chloro-2-hydroxymuconic semialdehyde. However, the enzyme did not utilize 2-hydroxy-6-oxo-hepta 2,4-dienoic acid and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid as substrates. The molecular weight of 2-HMS dehydrogenase from B. cepacia G4 was predicted to be 52 kDa containing 485 amino acid residues from the nucleotide sequence of the tomC gene, and it exhibited the highest identity of 78% with the amino acid sequence of 2-HMS dehydrogenase that is encoded in the aphC gene of Comamonas testosteroni TA441. 2-HMS dehydrogenase from B. cepacia G4 showed a significant phylogenetic relationship not only with other 2-HMS dehydrogenases, but also with different dehydrogenases from evolutionarily distant organisms.sms.

Inhibition of Cyclooxygenase and Prostaglandin E2 Synthesis by Crude Methanolic Extract from Euonymus Alatus (Thunb.) Sieb in SKBR3 Human Breast Cancer Cell Line

  • Kim Joong-Oh;Jang Tae-Hyun;Kim Min-Sung;Kim Dong-Il;Lee Tae-Kyun
    • The Journal of Korean Medicine
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    • v.26 no.1 s.61
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    • pp.37-45
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    • 2005
  • In the present study, we examined the effect of crude methanolic extract (CME) from Euonymus alatus (Thunb.) Sieb on arachidonic acid (AA) cascade in SKBR3 human breast cancer cell line. CME had a potent inhibitory activity of prostaglandin E2 (PGE2) release induced by A23187, a $Ca^{2+}$ ionophore. The inhibition was concentration-dependent, with the 50 value of about 5 M. CME had no inhibitory effect on A23187-induced phosphorylation of p42/p44 extracellular signal regulated kinase/mitogen-activated protein kinase or on the liberation of [14C]-AA from the cells labeled with [14C]-AA. However, CME concentration-dependently inhibited the conversion of AA to $PGE_2$ in microsomal preparations, showing its possible inhibition of cyclooxygenase (COX). In enzyme assay in vitro, CME inhibited the activities of both constitutive COX (COX­I) and inducible COX (COX-2) in a concentration-dependent manner, with the 50 values of about 0.8 and 2M, respectively. Lineweaver-Burk plot analysis indicated that CME competitively inhibited the activities of both COX-l and -2. This study is a first demonstration that CME directly inhibits COX activity.

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Enzymatic Hydrolysis of Crystalline Chitin in an Agitated Bead Reaction System and Its Reaction Characteristics

  • Lee, Yong-Hyun;Bae, Young-Ki;Jeong, Eui-Jun
    • Journal of Microbiology and Biotechnology
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    • v.6 no.6
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    • pp.432-438
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    • 1996
  • Native crystalline chitin was hydrolyzed in an agitated bead reaction system using crude chitinase excreted from Aspergillus fumigatus JC-19. The reaction was enhanced significantly, and the concentration and yield of reducing sugar after 48 hours were measured to be 35.42 g/I (w/v) and 0.64, respectively, around 1.86 times higher than those of the conventional system that was carried out without glass beads. The effect of reaction conditions, such as the amounts of chitin, chitinase and glass beads, and the size of glass bead, were examined. Ball milled chitin was also hydrolyzed in the agitated bead reaction system, the conversion yield and reaction rate of ball milled chitin for 24 hours increased up to 0.87 and 48.02 g/I, respectively. Chitinase showed relatively high stability in the agitated bead reaction system, particularly in the presence of enzyme stabilizer, $Ca^{++}$, which played a critical role in preventing the deactivation of chitinase by the physical impact of glass beads. The variations of the structural features of chitin during the reaction were followed by SEM and X-ray diffraction, and the enhanced hydrolysis reaction was caused by both the fragmentation of chitin particles and the destruction of the crystalline structure owing to the synergic effects of the attrition of glass beads and the hydrolytic action of chitinase.

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High Expression of β-Glucosidase in Bifidobacterium bifidum BGN4 and Application in Conversion of Isoflavone Glucosides During Fermentation of Soy Milk

  • You, Hyun Ju;Ahn, Hyung Jin;Kim, Jin Yong;Wu, Qian Qian;Ji, Geun Eog
    • Journal of Microbiology and Biotechnology
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    • v.25 no.4
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    • pp.469-478
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    • 2015
  • In spite of the reported probiotic effects, Bifidobacterium bifidum BGN4 (BGN4) showed no βglucosidase activity and failed to biotransform isoflavone glucosides into the more bioactive aglycones during soy milk fermentation. To develop an isoflavone-biotransforming BGN4, we constructed the recombinant B. bifidum BGN4 strain (B919G) by cloning the structural β-glucosidase gene from B. lactis AD011 (AD011) using the expression vector with the constitutively active promoter 919 from BGN4. As a result, B919G highly expressed β-glucosidase and showed higher β-glucosidase activity and heat stability than the source strain of the β-glucosidase gene, AD011. The biotransformation of daidzin and genistin compounds using the crude enzyme extract from B919G was completed within 4 h, and the bioconversion of daidzin and genistin in soy milk during fermentation with B919G also occurred within 6 h, which was much faster and higher than with AD011. The incorporation of this β-glucosidase-producing Bifidobacterium strain in soy milk could lead to the production of fermented soy milk with an elevated amount of bioavailable forms of isoflavones as well as to the indigenous probiotic effects of the Bifidobacterium strain.

Effects of Methyl Gallate on Arachidonic Acid Metabolizing Enzymes: Cyclooxygenase-2 and 5-Lipoxygenase in Mouse Bone Marrow-Derived Mast Cells

  • Kim, Se-Jong;Jin, Mei-Hua;Lee, Eun-Kyung;Moon, Tae-Chul;Quan, Zhe-Jiu;Yang, Ju-Hye;Son, Kun-Ho;Kim, Kil-Ung;Son, Jong-Kun;Chang, Hyeun-Wook
    • Archives of Pharmacal Research
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    • v.29 no.10
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    • pp.874-878
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    • 2006
  • Methyl gallate (MG) is a medicinal herbal product that is isolated from Paeonia lactiflora that inhibits cyclooxygenase-2 (COX-2) dependent phases of prostaglandin $D_2\;(PGD_2)$ generation in bone marrow-derived mast cells (BMMC) in a concentration-dependent manner with an $IC_{50}$ values of $17.0\;{\mu}M$. This compound also found inhibited the COX-2-dependent conversion of the exogenous arachidonic acid to $PGD_2$ in a dose-dependent manner with an $IC_{50}$ values of $190\;{\mu}M$, using a COX enzyme assay kit. However, at concentrations up to $80\;{\mu}M$, MG did not inhibit COX-2 protein expression in BMMC, indicating that MG inhibits COX-2 activity directly. Furthermore, MG consistently inhibited the production of leukotriene $C_4\;(LTC_4)$ in a dose dependent manner, with an $IC_{50}$ value of $5.3\;{\mu}M$. These results demonstrate that MG has a dual cyclooxygenase-2/5-lipoxygenase inhibitory activity, which might provide the basis for novel anti-inflammatory drugs.

Continuous Production of Agarooligosaccharides Using Packed-Bed Reactor (Packed-Bed 반응기를 이용한 한천올리고당의 연속생산)

  • 임동중;김종덕;강양순;공재열
    • KSBB Journal
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    • v.16 no.4
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    • pp.398-402
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    • 2001
  • Enzymatic hydrolysis of agar was carried out continuously to produce agarooligosaccharides by immobilized agarase in Packed-Bed Reactor. The reactor was constructed using a acryl tube with an internal diameter of 10 mm and a useful height of 140 mm. The Packed-Bed Reactor was 11 mL reactor volume as its length : diameter ratio was 14 : 1. The operation condition of reaction was performed with an 1 g/L agar concentration at 40$^{\circ}C$, 10 mM MOPS buffer(pH 7.0) and with the flow rate 3 mL∼48 mL/h at a dilution rate of 1.09∼5.45 h$\^$-1/. The hydrolysis products was identified DP6, DP4 and DP2 by HPLC. The conversion rate of agar was about 80% and amount of total agarooligosaccharide was 0.88 mg/mL at Packed-Bed Reactor.

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Association between Prostaglandin-endoperoxide Synthase 2 (PTGS2) Polymorphisms and Blood Pressure in Korean Population

  • Jin, Hyun-Seok;Hong, Kyung-Won;Lim, Ji-Eun;Han, Hye-Ree;Lee, Jong-Young;Park, Hun-Kuk;Oh, Berm-Seok
    • Genomics & Informatics
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    • v.6 no.3
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    • pp.110-116
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    • 2008
  • Blood pressure refers to the force exerted by circulating blood on the walls of blood vessels, and chronical elevation of blood pressure is known as hypertension. Although hypertension is affected by genetic and environmental factors, the genetic background of hypertension is not fully understood. One of the candidate genetic factors, Prostaglandin-endoperoxide synthase 2 (PTGS2), is a membrane-bound enzyme, catalyzing the conversion of arachidonic acid to prostaglandin, and recently SNPs of PTGS2 gene was associated with hypertension in Japanese population. Therefore the association of PTGS2 polymorphisms was investigated with blood pressure in healthy Korean subjects, 470 unrelated individuals randomly selected from Ansung and Ansan cohorts. The 25 SNPs of PTGS2 gene were identified by the sequencing analysis of 24 Korean samples. Among identified polymorphisms, three SNPs (rs689466, -1329A>G; rs5275, +6365T>C; rs4648308, +8806G> A) were selected for further association analysis, and rs689466 located in promoter region was associated with blood pressure as well as triglyceride level in the blood. By in silico analysis, rs689466 locates in v-Myb transcription factor binding site, and the v-Myb site disappears when the SNP is changed from A to G nucleotide. Individuals with A/G and G/G genotype in rs689466 have higher blood pressure than those with A/A genotype, and the regression p-value is 0.008 for systolic and 0.004 for diastolic blood pressure. In summary, the PTGS2 polymorphism (rs689466) is associated with blood pressure in Asian populations based on this and Japanese studies, shedding light on it as a genetic risk marker of hypertension.