• Title/Summary/Keyword: E2 enzyme

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Effects of Silk Fibroin Powder on Lipofuscin, Acetylcholine and Its Related Enzyme Activities in Brain of SD Rats (뇌조직의 리포푸신, 아세틸콜린 및 그 관련효소 활성에 미치는 실크 피브로인의 영향)

  • 최진호;김대익;박수현;김동우;이광길;여주홍;김정민;이용우
    • Journal of Sericultural and Entomological Science
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    • v.42 no.2
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    • pp.120-125
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    • 2000
  • This study was designed to investigate the effects of silk fibroin (Mw 500) powder (SFP) on lipofuscin, acetylcholine (ACh) and its related enzyme activities in brain of rats. Sprague-Dawley (SD) male rats (160$\pm$10 g) were fed basic diet (control group), and experimental diets (SFP-2.5 and SFp-5.0 groups) added 2.5 and 5.0 g/kg BW/day for 6 weeks. In case of liver membranes, lipofuscin (LF) levels resulted in a considerable decreases (11.5% and 13.8%, respectively) in SFP-2.5 and SFP-5.0 groups compared with control group. But in case of brain as the most sensitive organ, LF levels were remarkably inhibited about 18.3% and 21.7% in SFP-2.5 and SFP-5.0 groups compared with control group. Acetylcholine (ACh) levels were considerable decrease (3.0% and 9.2%, respectively) in brain membranes of SFP-2.5 and SFP-5.0 groups compared with control group. choine acetyltranferase (ChAT) activities as a synthesis enzyme of ACh, and acetylcholinesterase (AChE) activities as a hydrolysis enzyme resulted in a slight increases (2.4% and 3.0%, 4.6% and 6.3%, respectively), but significance difference between ChAT and AChE activities by SFP administration could be not obtained. Monoamine oxidase-B (MAO-B) activities were significantly inhibited (9.5% and 12.6%, respectively) in brain of SEP-2.5 and SFP-5.0 groups compared with control group. These results suggest that inhibiting effects of LF accumulation and MAO-B activity of silk fibroin(SFP) may play a pivotal role in protecting learning memory impairments by attenuating a various age-related changes for improvement of brain function.

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Characterization of laccase from pleurotus ostreatus (Pleurotus ostreatus의 laccase 작용특성)

  • 김규중;신광수;맹진수;강사욱;하영칠;홍순우
    • Korean Journal of Microbiology
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    • v.25 no.2
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    • pp.148-156
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    • 1987
  • Extracellular laccase (E.C. 1.10.3.2) from the culture filtrate of Pleurotus ostreatus was purified by ammonium sulfate precipctation, protamine sulfate precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel permeation chromatography. The molecular weight of the enzyme was estimated by SDS-polyacrylamide gel electrophoresis to be 58,000 and the isoelectric point was 3.75. The optimum temperature for the enzyme was about $45^{\circ}C$ and the optimum pH was 6.5. The enzyme was found to be stable at temperature below $35^{\circ}C$ and rapidly inactivated at higher temperatures. Km values for ferulic acid, vanillic acid, dihydroxyphenylalanine (DOPA) were 48.6.$\mu$M, 0.52mM, and 2.73mM, respectively, which indicates that the enzyme has much higher affinity towards ferulic acid. The reaction products of the enzyme were separated by TLC and HPLC.

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Cloning, Nucleotide Sequencing, and Characterization of the ptsG Gene Encoding Glucose-Specific Enzyme II of the Phosphotransferase System from Brevibacterium lactofermentum

  • Yoon, Ki-Hong;Lee, Kyu-Nam;Lee, Jung-Kee;Park, Se-Cheol
    • Journal of Microbiology and Biotechnology
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    • v.9 no.5
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    • pp.582-588
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    • 1999
  • A Brevibacterium lactofermentum gene coding for a glucose-specific permease of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) was cloned, by complementing an Escherichia coli mutation affecting a ptsG gene with the B. lactofermentum genomic library, and completely sequenced. The gene was identified as a ptsG, which enables an E. coli transformant to transport non-metabolizable glucose analogue 2-deoxyglucose (2DG). The ptsG gene of B. lactofermentum consists of an open reading frame of 2,025 nucleotides encoding a polypeptide of 674 amino acid residues and a TAA stop codon. The 3' flanking region contains two stem-loop structures which may be involved in transcriptional termination. The deduced amino acid sequence of the B. lactofermentum enzyme $II^{GIe}$ specific to glucose ($EII^{GIe}$) has a high homology with the Corynebacterium glutamicum enzyme $II^{Man}$ specific to glucose and mannose ($EII^{Man}$), and the Brevibacterium ammoniagenes enzyme $II^{GIc}$ specific to glucose ($EII^{GIc}$). The 171-amino-acid C-terminal sequence of the $EII^{Glc}$ is also similar to the Escherichia coli enzyme $IIA^{GIc}$ specific to glucose ($IIA^{GIc}$). It is interesting that the arrangement of the structural domains, IIBCA, of the B. lactofermentum $EII^{GIc}$ protein is identical to that of EIIs specific to sucrose or $\beta$-glucoside. Several in vivo complementation studies indicated that the B. lactofermentum $EII^{Glc}$ protein could replace both $EII^{ Glc}$ and $EIIA^{Glc}$ in an E. coli ptsG mutant or crr mutant, respectively.

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An alkaline proteinase produced by Yarrowia lipolytica 504D (Yarrowia lipolytica 504D의 Alkaline Proteinase 특성)

  • Kim, Chang-Hwa;Jin, Ingnyol;Yu, Choon-Bal
    • Korean Journal of Microbiology
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    • v.34 no.3
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    • pp.82-86
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    • 1998
  • An alkaline proteinase secreted from Yarrowia lipolytica 504D was purified by salting-out and column chromatography. The molecular weight of the purified enzyme was about 32,000 Da estimated by SDS-PAGE. The optimal condition for the activity of the enzyme was at pH 9.5 and $42^{\circ}C$ The enzyme was stable up to $45^{\circ}C$ and at the range of pH 4-10. Because the enzyme was inhibited by PMSF as well as EDTA, EGTA, and phenan-throlin, it is uncertain whether the enzyme is serine proteinase or metalloproteinase. However, almost all metal salts tested did not increase the enzyme activity, and Ca salt restored the activity of the enzyme inactivated by EDTA. Therefore, the purified enzyme seems to be an serine proteinase (E.C. 3.4.21.14).

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Exogenous emulsifiers and multi-enzyme combination improves growth performance of the young broiler chickens fed low energy diets containing vegetable oil

  • Wickramasuriya, Samiru Sudharaka;Macelline, Shemil Priyan;Kim, Eunjoo;Shin, Taeg Kyun;Cho, Hyun Min;Jayasena, Dinesh D.;Heo, Jung Min
    • Animal Bioscience
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    • v.35 no.10
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    • pp.1585-1591
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    • 2022
  • Objective: The present study examined the effects of exogenous emulsifiers and multi-enzyme supplementation into a low energy density diet on growth performance, visceral organ parameters, blood metabolites, ileal morphology, and nutrient digestibility in broiler chickens from hatch to 21 days. Methods: One hundred and sixty-eight one-day-old Ross 308 broiler chickens were allocated in a completely randomized design to 24 pens and each pen was assigned to one of four dietary treatments to give six replications with seven chickens in a cage. Dietary treatments were: i) positive control with standard energy level (PC); ii) negative control with 100 kcal/kg lower energy of the standard level (NC); iii) NC diet supplemented 0.05% calcium stearoyl-2 lactylate as an emulsifier (NC+E); and iv) NC diet supplemented with both 0.05% calcium stearoyl-2 lactylate and 0.05% multi-enzyme (NC+E+M). Corn and soybean meal-based control diets containing vegetable oil were formulated to meet the Ross 308 nutrition specification. Chickens were fed ad-libitum with the treatment diets and sampling was conducted on day 21. Results: Our results revealed that emulsifier and multi-enzyme supplementation into NC diets improved (p<0.05) feed efficiency of the broiler chickens compared to the broiler chickens fed NC diets from hatch to 21 days. Supplementation of emulsifier and multi-enzyme into NC diet improved (p<0.05) nutrient digestibility of the broiler chickens. However, emulsifier and multi-enzyme supplementation into diet did not influence (p>0.05) visceral organ weight, blood metabolites, and intestinal morphology in broiler chickens fed NC diets. Conclusion: Supplementation of emulsifier and multi-enzyme in the NC diet would support improving growth performance in young broiler chickens with improved feed efficiency and increased nutrient digestibility thereby curtailing the negative impact of energy reduction in the diets.

Effect of Supplementation of Antioxidant Nutrient Against Oxidant Stress during Exercise

  • Kim, Hye-Yount
    • Journal of Nutrition and Health
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    • v.30 no.9
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    • pp.1061-1066
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    • 1997
  • This study was undertaken to evaluate the effect of 4 weeks of $\alpha$-tocopherol(800 I.U./d) supplementation on oxidant stress of eleven female aerobic -majoring students during rest and exercise. Changes in the activity of the antioxidant enzyme glutathione peroxidase were also studied. Serum $\alpha$-tocopherol concentration was significantly increased with vitamin E supplementation(710.1$\pm$113.8$\mu\textrm{g}$/dl vs. 1,485,8$\pm$105.2$\mu\textrm{g}$/dl). In addition, serum MDA concentration, an index of lipid peroxidation, significantly decreased after vitamin E supplementation. However, MDA values after exercise increased to pre-supplementation levels. Serum glutathione peroxidase activity significantly increased with vitamin E supplementation. The enzyme activity showed a trend toward decrease after exercise. Serum cholesterol values were not significantly affected by vitamin E supplementation. However, serum triglycerides significantly increased after supplementation against oxidative stress during resting periods. These supplements appraently work by decreasing lipid peroxidation and increasing glutathione peroxidase activity. However, vitamin E supplementation did not prevent exercise-induced increases in lipid peroxidation.

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Effect of Allylisothiocyanate on the Enzyme Activities During the Culture of Aspergillus parasiticus R-716 (Allylisothiocyanate첨가가 Aspergillus parasiticus R-716의 배양중 효소활성에 미치는 영향)

  • 김성영
    • Journal of Food Hygiene and Safety
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    • v.12 no.2
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    • pp.97-101
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    • 1997
  • Effect of allylisothiocyanate on the enzyme activites including malate degydrogenase, isocitrate dehydrogenase, NADPH and acetyl CoA which were related to aflatoxin production of Aspergillus parasticus R-716 were invetigated. The activities of malate dehydrogenase (EC.1.1.1.37), isocitrate dehydrogenase (E.C.1.1.1.42) and NADPH oxidase (E.C.1.6.99.1) indicated relatively high in the 50 ppm allylisothiocyanate-added-culture. In contrast, the activity of acetyl CoA in the 50 ppm allylisothiocyanate-added-culture showed rather lower level through the cultivation.

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Antioxidative Action of Enzymatic Hydrolysates of Mackerel Muscle Protein (고등어 근육단백질 효소 가수분해물의 항산화 작용)

  • 염동민;김영숙
    • The Korean Journal of Food And Nutrition
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    • v.7 no.2
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    • pp.128-136
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    • 1994
  • Mackerel muscle protein hydrolysates, which were prepared from defatted mackerel meal by proteases such as complex enzyme, alcalase, bromelain, pancrease, pepsin, w-chymotrypsin, trypsin and papain, were tested for the antioxidative action against linoleic acid. Among proteases tested, the hydrolysates obtained from the treatment of complex enzyme, bromelain and alcalase showed higher antioxidative effects. Also, the hydrolysates showed the synergistic effects with o-tocopherol and the inhibitory effects for peroxidation of metal ions(Fe3+, Cua+) From the profiles of fractionation of the hydrolysates with Bio-gel P-2 column, the most active fractions, part I(complex enzyme-derived) and part e(bromelain-derived), had below MW 1,400 and the antioxidative effects were closely related to the binding capacity with metal ion(Cua+). Amno acid composition of the part I was abundant in histidine, arginine, phenylalanine and lysine, and the part e was abundant in lysine, glutamic acid and leucine.

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5-Aminolevulinic Acid Biosynthesis in Escherichia coli Coexpressing NADP-dependent Malic Enzyme and 5-Aminolevulinate Synthase

  • Shin, Jeong-Ah;Kwon, Yeong-Deok;Kwon, Oh-Hee;Lee, Heung-Shick;Kim, Pil
    • Journal of Microbiology and Biotechnology
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    • v.17 no.9
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    • pp.1579-1584
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    • 2007
  • 5-Aminolevulinate (ALA) synthase (E.C. 2.3.1.37), which mediates the pyridoxal phosphate-dependent condensation of glycine and succinyl-CoA, encoded by the Rhodobacter sphaeroides hemA gene, enables Escherichia coli strains to produce ALA at a low level. To study the effect of the enhanced C4 metabolism of E. coli on ALA biosynthesis, NADP-dependent malic enzyme (maeB, E.C. 1.1.1.40) was coexpressed with ALA synthase in E. coli. The concentration of ALA was two times greater in cells coexpressing maeB and hemA than in cells expressing hemA alone under anaerobic conditions with medium containing glucose and glycine. Enhanced ALA synthase activity via coupled expression of hemA and maeB may lead to metabolic engineering of E. coli capable of large-scale ALA production.

Effects of Normal Diet with or without Naringin Supplement Following Ethanol Diet on Changes in Lipid Profiles and Antioxidant Enzyme Activities in Rats

  • Seo, Hyun-Ju;Lee, Hyo-Sun;Choi, Myung-Sook
    • Nutritional Sciences
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    • v.9 no.2
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    • pp.82-91
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    • 2006
  • This study was performed to investigate the effect of normal diet with or without naringin supplement on the lipid and antioxidant metabolism in ethanol-treated rats for a short tenn. Male Sprague-Dawley rats were divided into three groups (n=10), which were assigned to one of three dietary categories : $E_8$ : ethanol diet for 8 wks, $E_4N_4$ : ethanol diet for the first 4 wks and normal diet for the last 4 wks, $E_4Nna_4$ : ethanol diet for the first 4 wks and normal diet with naringin supplement for the last 4 wks. Plasma total cholesterol concentrations were significantly higher in ethanol fed rats for 8 weeks. The HDL-C/total-C ratios of the $E_4N_4$ and the $E_4Nna_4$ groups were significantly higher than that of the $E_8$ group, while the atherogenic index was lower in the $E_4N_4$ and the $E_4Nna_4$ groups than in the $E_8$ group. The $E_4N_4$ and $E_4Nna_4$ diets significantly lowered both the hepatic cholesterol and triglyceride levels compared to the $E_8$ group. Accumulation of hepatic lipid droplets was observed to be the highest in the $E_8$ group. In the current study, the naringin supplement to normal diet significantly lowered both the hepatic HMG-CoA reductase and ACAT activities in ethanol pre-treated rats for 4 weeks. Antioxidant enzyme activities were also upregulated when ethanol feeding was ceased. Naringin supplement given for 4 weeks after ethanol cessation resulted in a significant decrease in the plasma cholesterol and hepatic lipids and plasma TBARS as well as the hepatic HMG-CoA reductase and ACAT activities compared to the rats given ethanol diet for the entire 8 weeks. Replacement of normal diet following a short tenn ethanol feeding was effective for the recovery of ethanol-induced fatty liver and for normalizing plasma and hepatic lipid profiles and antioxidant enzyme activities, regardless of an additional phytochemical supplement, naringin. The effect of naringin could seemingly be more evident if its supplementation period had been extended longer than 4 weeks after ethanol cessation.