• Journal of the Korean Wood Science and Technology
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• v.45 no.6
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• pp.857-871
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• 2017

The major substrates used in soilless growing media are peat moss and perlite, where peat moss is a limited and expensive natural resource. Determination of appropriate substrates based on technical and economic feasibility is the vital aspect of research and the key to success in any soilless production system. This research work was performed to evaluate different low-cost and sustainable alternative substrate as soilless growing media for horticulture plant. The objective of this study was to compare the effect of sawdust species and steam treatment, for physico-chemical properties and growth of horticultural plant. This study involves the physical and chemical characterization and growth test of four substrate (pine sawdust, oak sawdust, steamed pine sawdust and steamed oak sawdust) in order to evaluate their use as components of growing media. Steamed oak sawdust ($121^{\circ}C$, 30 min) showed adequate physical and chemical properties compared to peat moss for their use as growing media. The growing media were prepared using different mixture proportion to grow Brassica campestris L., Festuca arundinacea and Lespedeza cyrtobotrya Miq. The highest germination, stem length and leaf area of Brassica campestris L., Festuca arundinacea and Lespedeza cyrtobotrya were observed in 30 minute steamed oak sawdust mixture growing media. The steam treatment condition of sawdust used in the growing media significantly positive affected the germination, the stem length and the leaf area.

• Korean Journal of Ecology and Environment
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• v.41 no.3
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• pp.311-319
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• 2008

To understand the relative immigration activities (RIA) of hibernal diatom community in Lake Ilgam (at the station with and without macrophyte) and River Han (at the station with different current and nutrient), a natural and artificial bed substrate was deposited from 15 to 29 January 2008. For the study period, both waters comprised huge biomass of diatom, over 75% of total abundance. Nutrients in water column, ash-free dry matter (AFDM) and chlorophyll-a (Chl-a) concentration in substrates were decreased with increasing of current in rivers, while in lakes the macrophyte largely affected the diatom community and water quality. Algal RIA in rivers was high at stations with high concentration of nutrient, AFDM and Chl-a, and in high nutrients and no macrophytes in lakes, respectively. The species showing a higher RIA was Nitzschia amphibia in rivers and Aulacoseira italica in lakes, while the dominant species were Navicula sp. in rivers and Syndera acus in lakes, suggesting no relationship between water algal biomass and its RIA. These results suggest that the RIA of stream diatom community depends exclusively on the current, while the planktonic diatom in lake was of the macrophyte.

• Journal of Plant Biotechnology
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• v.47 no.3
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• pp.235-241
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• 2020

This is the first study to establish a complete protocol for micropropagation of Rehmannia glutinosa from root segments. The study involved investigating the effect of plant growth regulators on in vitro shoot regeneration and rooting and identifying substrates supporting survival and growth performance of ex vitro seedlings. A Murashige and Skoog (MS) medium containing 30 g/L sucrose for shoot induction and 0.2 mg/L indole-3-acetic acid (IAA), 1 mg/L 6-benzylaminopurine (BAP), and 1 g/L polyvinylpyrrolidone (PVP) for shoot multiplication resulted in the highest number of shoots per explant and shoot height. Applying a medium containing 0.5 mg/L IAA and 1 g/L PVP yielded optimal rooting of the shoots grown in vitro. Compost enriched with microbial inoculants and perlite enhanced seedling growth better than that with organic biofertilizer-free substrates (soil and sand). We recommend the continuous production of micropropagated R. glutinosa seedlings from root segments under the aforementioned conditions as a possible propagation technique for crops of this species.

• BMB Reports
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• v.29 no.6
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• pp.500-506
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• 1996

We have isolated a water-extracted novel regulator for blood coagulation from an earthworm, Lumbricus rubellus. As a folk remedy, the earthworm has been known to facilitate blood circulation. After complete heat inactivation of endogenous proteases in the earthworm, an anticoagulant(s) was purified through ammonium sulfate fractionation and three consecutive gel permeation chromatography of Sephacryl S-300, Sephadex G-75, and G-150 by measuring activated partial thromboplastin time (APTT) The anticoagulant was further purified to 2,800 fold with a C4 reversed-phase HPLC This activity was stable under heat ($100^{\circ}C$ for 30 min) and acidic conditions (0.4 N HCl). The effects of this partially purified anticoagulant on thrombin were observed with various substrates such as N${\alpha}$-benzoyl-DL-arginine-p-nitroanilide (BApNA), H-D-phenylalanyl-L-pipecoyl-L-arginine-p-nitroanilide (S-2238), N${\alpha}$-p-tosyl-L-arginine methyl ester (TAME), and fibrinogen as a natural substrate. Only TAME hydrolysis, due to an esterase activity of the enzyme, was inhibited among the chromogenic substrates. In addition, the anticoagulant not only inhibited the conversion of fibrinogen to fibrin but also prolonged the fibrin clot formation monitored with the in vitro coagulation test. Based on these observations, we suggest the significance of measuring the ability of antithrombotic drugs to inhibit the esterase activity of thrombin. In this report, it was also shown that the earthworm indeed contained a water-extractable, heat- and acid-stable anticoagulant which could be used as a novel antithrombotic agent.

• Molecules and Cells
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• v.41 no.4
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• pp.331-341
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• 2018

L-pipecolic acid is a non-protein amino acid commonly found in plants, animals, and microorganisms. It is a well-known precursor to numerous microbial secondary metabolites and pharmaceuticals, including anticancer agents, immunosuppressants, and several antibiotics. Lysine cyclodeaminase (LCD) catalyzes ${\beta}$-deamination of L-lysine into L-pipecolic acid using ${\beta}$-nicotinamide adenine dinucleotide as a cofactor. Expression of a human homolog of LCD, ${\mu}$-crystallin, is elevated in prostate cancer patients. To understand the structural features and catalytic mechanisms of LCD, we determined the crystal structures of Streptomyces pristinaespiralis LCD (SpLCD) in (i) a binary complex with $NAD^+$, (ii) a ternary complex with $NAD^+$ and L-pipecolic acid, (iii) a ternary complex with $NAD^+$ and L-proline, and (iv) a ternary complex with $NAD^+$ and L-2,4-diamino butyric acid. The overall structure of SpLCD was similar to that of ornithine cyclodeaminase from Pseudomonas putida. In addition, SpLCD recognized L-lysine, L-ornithine, and L-2,4-diamino butyric acid despite differences in the active site, including differences in hydrogen bonding by Asp236, which corresponds with Asp228 from Pseudomonas putida ornithine cyclodeaminase. The substrate binding pocket of SpLCD allowed substrates smaller than lysine to bind, thus enabling binding to ornithine and L-2,4-diamino butyric acid. Our structural and biochemical data facilitate a detailed understanding of substrate and product recognition, thus providing evidence for a reaction mechanism for SpLCD. The proposed mechanism is unusual in that $NAD^+$ is initially converted into NADH and then reverted back into $NAD^+$ at a late stage of the reaction.

• Microbiology and Biotechnology Letters
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• v.19 no.4
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• pp.331-336
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• 1991

In order to utilize natural cellulosic materials as a fermentative substrate, saccharification of a various kind of native cellulosic materials was performed by using cellulase from the isolated strain, Pseudomonas sp. LBC-505 which potently produced cellulase complex and xylanase. Cellulase complex production was repressed by the low concentration of glucose, induced by cellulosic compounds such as CMC, wheat bran and rice straw et al. and showed to be highest on the PY-CMC medium containing 5% (w/v) wheat bran instead of CMC. Optimal temperature for enzyme reactions of CMCase and xylanase was $50^{\circ}C$, and $55^{\circ}C$ for $\beta$-glucosidase. Optimal pH for these enzyme reaction was 6.6. Rate of saccharification for natural cellulose was low by the treatment of crude enzyme. Among their substrates, rice straw was the most effective substrate of enzymatic reaction in this work. After treating rice straw with 5% (v/v) HC1 and hydrolysing with crude enzyme, rate of saccharification was 18.4% (w/w) on dry substrate. Sugars of cellulosic hydrolyzate mainly contained glucose, xylose and cellobiose.

• Journal of the Korea Organic Resources Recycling Association
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• v.7 no.2
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• pp.73-82
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• 1999

To verify the usefulness of enzyme activity as a index for the stability or maturity of apple pomace composting. the succession of microbial populations using viable count procedure. and Vmax of ${\beta}$-glucosidase and cellobiohydrolase were measured. based on an increase in fluorescence as the nonfluorescent methylumbelliferyl substrates were enzymatically hydrolyzed, leading to the highly fluorescent methylumbelliferyl molecule 4-methylumbelliferone(MUF). The activities of these enzymes in the decomposition of carbohydrates were gradually decreased in the course of the time. Correlation between microbial population and enzyme activity was not significant with exception of fungi. and the fungi were represented in high density. This indicates that the fungi probably play a major role in composting of apple pomace.

• Journal of Life Science
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• v.14 no.2
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• pp.252-254
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• 2004

The mutant tryptophan synthases at $\alpha$Asp$^{56}$ have low catalytic activities. The enzymes were treated with $\alpha$ and $\beta$ subunit-specific ligands in the presence of L-serine and indoline. It was shown that the cations resulted in changes of absorbance patterns among the proteins, while glycerophosphate showed similar pattern of absorbance. The glycerophosphate binds to the active site of $\alpha$ subunit so that $\alpha$Asp$^{56}$ may not be involved in the allosteric control with the active site of $\alpha$ subunit occupied by substrate. The results suggest that $\alpha$Asp$^{56}$ may playa role in the step of a series of reaction occurring without bound substrates in the active site of asubunit.

• 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.

• Korean Journal of Microbiology
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• v.23 no.3
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• pp.177-183
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• 1985

Some properties of an extracellular cytosine deaminase produced from Arthrobacter sp.JH-13 were examined after 20-80% of ammonium sulfate fractionation. Among some substrates, this enzyme utilized cytosine and 5-fluorocytosine as a substrate. The optimum pH and temperature for the activity of this enzyme were found to be near 8.0 and $40^{\circ}C$, respectively. The ensyme was more stable in 0.2M of Tris-HCl buffer than 0.2M of potassium phosphate buffer. The enzyme was generally stable below $50^{\circ}C$, but inactivated completely at $70^{\circ}C$. 1mM of $Fe^{3+},\;K^+\;and\;Na^+$ increased the enzyme activity, but 0.01mM of $Co^{2+},\;Cu^{2+},\;Ni^{2+},\;Hg^{2+},\;Ag^{2+},\;Zn^{2+},\;Ba^{2+},\;and\;Mg^{2+}$ markedly inactivated the enzyme activity. 0.1mM of p-chloromercuribenzoate, trichloroacetic acid, and N-ethylmaleimide compleyely inhibited the enzyme activity, but 0.1mM of 2-mercaptoethanol slightly increased the enzyme activity.