• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.5
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• pp.849-855
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• 1994

Actively growin Excherichia coli(KCTC 1039) cells were treated with paraquat (1, 1'-dimethyl-4, 4'-bipyridili-um dichloride) by cultivating them in the presence of 1.0mM paraquat. The treatment was carried out with or without shaking to understand the effect of oxygen on paraquat action to thebacterial superoxide dismutase (SOd). By the treatment with vigorous shaking , population growth of the organism almostly stopped and specific activities of SOD of the cells drastically decreased. On contrast ot it, the herbicide showed only l limited inhibitory action on bacterial growth and SOD activity by stationary treatment. Proteins prepared from parquat-treated cells divided into two peaks by Sephacryl column chormatogrpahy, while proteins from the intact cells formed a single peak. Cytoplasmic proteins and plasma membrane proteins of intact cells formed separated three peaks by Sephadex G-75 column chormatography. respectively. Among them the second peak disappeared by paraquat treatment , while the third peak became more apparent. Fractions from the first and the third peak showed SOD activity. Paraquat was detected from the same fractions.

• BMB Reports
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• v.32 no.2
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• pp.127-132
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• 1999

The NAD(P)H-quinone oxidoreductase (EC 1. 6. 99. 2) was purified from S. cerevisiae. The native molecular weight of the enzyme is approximately 111 kDa and is composed of five identical subunits with molecular weights of 22 kDa each. The optimum pH of the enzyme is pH 6.0 with 1,4-benzoquinone as a substrate. The apparent $k_m$ for 1,4-benzoquinone and 1,4- naphthoquinone are 1.3 mM and $14.3\;{\mu}M$, respectively. Its activity is greatly inhibited by $Cu^{2+}$ and $Hg^{2+}$ ions, nitrofurantoin, dicumarol, and Cibacron blue 3GA. The purified NAD(P)H-quinone oxidoreductase was found capable of reducing aromatic nitroso compounds as well as a variety of quinones, and can utilize either NADH or NADPH as a source of reducing equivalents. The nitroso reductase activity of the purified NAD(P)H-quinone oxidoreductase is strongly inhibited by dicumarol.

• 한국유가공학회:학술대회논문집
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• 1997.05a
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• pp.23-34
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• 1997

Calcium-stimulated ATPase ($Ca^{2+}$-ATPase) which has optimal pH value at 7.0 was found in the membrane fraction of human milk, and its enzymatic properties were studied. The purified $Ca^{2+}$-ATPase required 0.45 mM Ca ion for maximal activity. Among the nucleosides, $Ca^{2+}$-ATPase showed a higher substrate specificity to ATP and UTP than to CTP and GTP. $Ca^{2+}$-ATPase had apparent Km value of 0.065, and V max of 7.63 mol ATP hydrolyzed/mg pro-tein per min, respectively. $Ca^{2+}$-ATPase was potently inhibited by lanthanide, vanadate, and p-chloromercuribenzoate, and inactivated by EDTA, and CDTA and EGTA, but were unaffected by N-ethylmaleimide, $NaN_3$, ouabain, or oligomycin, and was completely inactivated by heating at $60^{\circ}C$ for 10 min. This enzyme activity was concentrated in the membrane fraction of the cream and skim milk membrane, but not founded in bovine milk.

• BMB Reports
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• v.45 no.2
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• pp.91-95
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• 2012

Glutamate dehydrogenase from axenic bacterial cultures of a new microorganism, called GWE1, isolated from the interior of a sterilization drying oven, was purified by anion-exchange and molecular-exclusion liquid chromatography. The apparent molecular mass of the native enzyme was 250.5 kDa and was shown to be an hexamer with similar subunits of molecular mass 40.5 kDa. For glutamate oxidation, the enzyme showed an optimal pH and temperature of 8.0 and $70^{\circ}C$, respectively. In contrast to other glutamate dehydrogenases isolated from bacteria, the enzyme isolated in this study can use both $NAD^+$ and $NADP^+$ as electron acceptors, displaying more affinity for $NADP^+$ than for $NAD^+$. No activity was detected with NADH or NADPH, 2-oxoglutarate and ammonia. The enzyme was exceptionally thermostable, maintaining more than 70% of activity after incubating at $100^{\circ}C$ for more than five hours suggesting being one of the most thermoestable enzymes reported in the family of dehydrogenases.

• Microbiology and Biotechnology Letters
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• v.22 no.3
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• pp.266-270
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• 1994

A bacteriocin was isolated from the supernatant fluid of M17G broth culture of Lactococcus sp. HY 449 strain, which showed strong inhibitory activity against the growth of selective indicator strain, Lactobacillus fermentum IFO3023. When the bacteriocin wasa added to the growing indicator cells or cell suspensions, viable cells and optical density were density were decreased, indicating bacteriolytic mode of action. Electron microscopic observation of indicator cells treated with bacteriocin revealed apparent damages on the cell surface and eventual lysis of cell walls.

• KSBB Journal
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• v.5 no.3
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• pp.223-227
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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 glucose-fructose oxidoreductase activity due to leaking of enzyme from the cells. In order to prevent this leakage, the permeabilized cells were immobilized in alginate and chitin. No significant loss of enzyme activity was apparent during 210h operation in a continuous process. The productivity of the continuous process was estimated to be about 3.5g/l -h for sorbitol at dilution rate $0.2h^{-1}$.

• Asian-Australasian Journal of Animal Sciences
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• v.3 no.1
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• pp.27-31
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• 1990

Influences of plant phenolic acids and their possible metabolites(non-phenolic aromatic acids involved) in the rumen on the cellulolytic activity of mixed rumen populations were examined by a simple in vitro culture technique. Initial concentrations of aromatic acids were 1, 5, 10 and 20 mM/l. All the tested aromatic acids reduced microbial cellulose digestion especially at the higher initial concentration. P-Coumaric acid, ferulic acid and cinnamic acid, those having unhydrogenated propenoic side chain were more inhibitory than were 3-phenylpropinic acid and phloretic acid, those having hydrogenated propanoic side chain. Lag-time for cellulose digestion was prolonged by former three acids by 16 h. Apparent reduction in p-coumaric acid concentration was observed at 24 h when cellulose digestion began. Volatile fatty acid productions from cellulose fermentation were shifted by former three aromatic acids to produce more acetate and less propionate. This suggests that the selection of celluloytic organisms was induced by these aromatic acids.

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.1
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• pp.87-93
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• 1999

This study was carried out to investigate the effects of nucleic acid related compounds and metal ions on activities of cytidine deaminase from Bacillus subtilis ED 213. The purified cytidine deaminase was weakly inhibited by 1mM GMP, IMP and ATP, but not affected by other nucleic acid related compounds such as CMP and UDP. The apparent Km values for cytidine, deoxycytidine, 5 methylcy tidine, fluorodeoxycytidine, and 5 bromocytidine were calculated to be 6.6$\times$10-4M, 6.0$\times$10-4M, 0.9$\times$10-4M, 0.8$\times$10-4M, and 2.0$\times$10-3M, respectively. The cytidine deaminase was completely inhibited by 1mM Hg2＋, and mildly inhibited over 40% by metal ions such as Na＋ and Fe2＋. However the enzyme activity was activated more than 40% by 1mM Mg2＋.

• Archives of Pharmacal Research
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• v.23 no.4
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• pp.407-412
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• 2000

The presence of the nitric oxide synthase (NOS) enzyme from Salmonella typhimurium (S. typhimurium) was identified by measuring radiolabeled L-$[^3H]$citrulline and NO, and Western blot analysis. NOS was partially purified by both Mono Q ion exchange and Superose 12HR size exclusion column chromatography, sequentially. The molecular weight of NOS was estimated to be 93.3 kDa by Western blot analysis. The enzyme showed a significant dependency on the typical NOS cofactors; an apparent Km for L-arginine of 34.7 mM and maximum activity between $37^{\circ}C$ and $43^{\circ}C$. The activity was inhibited by NOS inhibitors such as aminoguanidine and $N^{G}$ $N^{G}$-dimethyl-L-arginine. taken together, partially purified NOS in S. typhimurium is assumed to be a different isoform of mammalian NOSs.OSs.

• Advances in Traditional Medicine
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• v.4 no.4
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• pp.227-234
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• 2004

An ${\alpha}-Amylase$ was purified to apparent homogeneity from germinating soybean seeds (Glycine max). Enzyme showed high specificity for starch. ${\alpha}-Amylase$ from soybean has optimum pH at 7.6 in the pH range 4.0-10.6. At this pH, the $K_m$ of starch was 2.63 mg/ml and the $V_{max}$ was equal to 52.6 mg/ml/min protein. Optimum temperature of the enzyme was found to be $55^{\circ}C,\;Q_{10}$ equal to 1.85 and energy of activation equal to 12 kcal/mol. Additives like, EDTA reduced the activity of ${\alpha}-amylase$ whereas PMSF enhanced the activity. ${\alpha}-Amylase$ was inhibited by several heavy metal ions.