• Journal of Life Science
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• v.14 no.1
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• pp.45-50
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• 2004

To investigate the effect of the cell wall on the pigmentation and branching in Aspergillus nidulans, ultrastructure of cell wall in suppressor mutant of the null pigmentation (SU-NPG, SU602) has been examined. Scanning electron microgrphs (SEM) revealed that the most outer layer of conidia wall peeled off in SU-NPG on day 6 from the complete conidiation. They also showed that hyphal growth and branching were not well developed in SU-NPG. Transmission electron micrographs (TEM) showed that the plasma membrane was not crenulated and the hyphal wall was thick in SU-NPG. These results indicated that the ultrastructure of cell wall in SU-NPC might be modified. Cytochemical analysis showed that the cell wall in SU-NPG was differentiated into Cl, C3, C2 and C4 layer in conidia and H1, H3, H2 and H4 layer in hyphae. C3 layer and H3 layer existed in SU-NPG. The increment of the diameter in SU-NPG hyphae might be caused by the thickness of H3 layer. These results suggest that SU-NPG may have an immature but the differentiated structure for the pigmentation in cell wall.

• Journal of the Korean Electrochemical Society
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• v.15 no.2
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• pp.83-89
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• 2012

We investigate the electrocatalytic activities for oxygen reduction at nanoporous gold (NPG) surfaces fabricated by selective dissolution of Ag from electrodeposited Ag-Au layers on electrode surfaces. The structure of NPG was controlled by changing the concentration ratios of precursor metal complexes during the electrodeposition of Ag-Au layers and the corresponding surface morphology and surface area was examined. NPG structures with Ag/Au ratio of 2.0 exhibited the highest electrocatalytic activity for oxygen reduction, where the nanoporous structure plays a key role, but the surface area does not affect on the electrocatalytic activity. The mechanism of electroreduction of oxygen was investigated by rotating disk electrode techniques. In acidic media, oxygen was first reduced to hydrogen peroxide followed by further reduction to water through 2-step 4-electron mechanism, whereas the oxygen was reduced directly to water by 4-electron mechanism in basic media.

• Food Science of Animal Resources
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• v.33 no.1
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• pp.24-30
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• 2013

This study was conducted to compare the physicochemical and sensory properties of yogurt added with nanopowdered ginseng (NPG) and powdered ginseng (PG) of different concentrations (0.1, 0.3, 0.5, and 0.7%) (w/v) during the storage at $7^{\circ}C$ for 20 d. The pH and viscosity values of yogurt added NPG or PG decreased during the storage. The pH values of the yogurt samples were ranged from 4.0 to 4.6 as a reflective of the fresh state. Viscosity values of yogurt with NPG at lower concentrations 0.1 and 0.3% (w/v) showed higher values during increased storage time. DPPH radical scavenging activity was significantly higher in the NPG-added yogurt than in the PG during the storage period (p<0.05). The lactic acid bacteria (LAB) counts ranged from $3.0{\times}10^9$ to $1.3{\times}10^9$ and $2.2{\times}10^9$ to $1.1{\times}10^9CFU/mL$ in 0.3% NPG and PG-added yogurts, respectively. Increased storage period showed decrease in LAB counts irrespective of the type of ginseng powder and storage period. In sensory test, 0.1 and 0.3% NPG-added yogurt showed similar results to control in yellowness, viscosity, and bitterness. Based on the data obtained from the present study, it was concluded that the concentrations 0.1 and 0.3% (w/v) of NPG could be used to produce NPG-added yogurt without significant adverse effects on physicochemical and sensory properties, and enhance functional value of yogurt.

• Journal of Life Science
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• v.16 no.7 s.80
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• pp.1148-1157
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• 2006

A hyperthermophilic bacterium Thernotoga maritima produced thermostable ${\beta}-glucosidase$. The gene encoding ${\beta}-glucosidase$ from T. maritima MSB8 was cloned and expressed in Escherichia coli. The en-zyme (BgIB) hydrolyzed ${\beta}-glucosidase$ linkages between glucose and alkyl, aryl of saccharide groups such as salicin, arbutin, and $_pNPG$. The insert DNA contained ORF with 2,166 bp encodes a 721 amino acids (calculated molecular mass of 80,964 and pl of 4.93). The amino a.id sequence of BglB showed the similarity to family 3 glycosyl hydrolases. The molecular weight of the enzyme was estimated to be approximately 81kDa by MUG-nondenaturing PAGE (4-methylumbelliferyl 13-D-glucoside-nondenaturing polyacrylamide gel electophoresis) and SDS-PACE. The ${\beta}-glucosidase$ exhibited maximal activity at pH 7.0 and $80^{\circ}C$. By exchanging two possible residues (Glu-232 and Asp-242) to Ala by site-directed mutagenesis method, it was found that these were essential for enzymatic activity.