• Applied Biological Chemistry
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• v.33 no.2
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• pp.109-115
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• 1990

This study was carried out to investigate the effect of L-cysteine and sodium sulfite on heat inactivation of soybean trypsin inhibitor(STI) and to determine cultivar difference in the inhibitory activity of STI. Effect of L-cysteine and sodium sulfite at different concentrations, pH's, and lengths of treatment on inactivation of STI were studied. The inactivation of STI was spectrophotometrically determined by measuring the rate of production of p-nitroaniline from synthetic substrate, N-benzoyl-DL-arginine-p-nitroanilide. Addition of L-cysteine and sodium sulfite increased magnitude of heat inactivation and greatly inhibited the re-activation of STI. There was no difference STI inactivation in among soybean cultivars employed. The trypsin inhibitory activity of STI of the soybean cultivars ranged from 64.7 to 86.4 TIU(trypsin inhibitor unit) per gram soyflour and the decreasing order of the TIU was Jangback>Hill>Jangyeab, Kwangkyo> Danyeab>Dangkyung>Paldal, Saeal, Duckyu>Hwangkeum. Inhibitory activity of STI was correlated with cysteine $content(r=0.6568^*)$ and with $digestivility(r=-0.7695^{**})$, but there was no correlation between the protein content and the inhibitory activity of STI.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1385-1389
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• 2007

5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the formation of EPSP and inorganic phosphate from shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) in the biosynthesis of aromatic amino acids. To delineate the domain-specific function, we successfully isolated the discontinuous C-terminal domain (residues 1-21, linkers, 240-427) of EPSP synthase (427 residues) by site-directed mutagenesis. The engineered C-terminal domains containing no linker (CTD), or with gly-gly ($CTD^{GG}$) and gly-ser-ser-gly ($CTD^{GSSG}$) linkers were purified and characterized as having distinct native-like secondary and tertiary structures. However, isothermal titration calorimetry (ITC), $^{15}N-HSQC$,\;and\;^{31}P-NMR$ revealed that neither its substrate nor inhibitor binds the isolated domain. The isolated domain maintained structural integrity, but did not function as the half of the full-length protein.

• Archives of Pharmacal Research
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• v.11 no.3
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• pp.230-239
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• 1988

Thirty kinds of medicinal plants were screened to examine inhibitory activities on rat brain monoamine oxidase A, using serotonin as a substrate. As active principles, various kinds of stilbenes were isolated from Veratri Rhizoma, Reynoutriae Radix and Rhei undulati Rhizoma, and several kinds of flavonoids from Sophorae Flos, Chrisanthemi Flos and Glycine max. Among the compounds isolated, resveratrol(I) strongly inhibited MAO-A competitively, and its $IC_{50}$ and Ki values were 2 ${\mu}M$ and 2.5 ${\mu}M$, respectively. Inhibitory potencies towards MAO-A of some stilbenes and flavonoids were also compared.

• KSBB Journal
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• v.16 no.3
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• pp.259-263
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• 2001

The development of hollow fiber reactor system for the production of chiral 1,2-epoxy-7-octence by epoxide hydrolase for Rhodotorula glutinis was investigated. Dodecane with high solubility of the racemic substrate passed through the lumen side of the hollow fiber reactor and cell suspension was recirculated through the shell side. The 2nd hollow fiber reactor was coupled to the production reactor to extract the diol byproduct which was the inhibitor of epoxide hydrolase. Optically pure (S)-1,2-epoxy-7-octene (0.6 M in dodecane) could be obtained using hollow-fiber reactor system.

• Microbiology and Biotechnology Letters
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• v.18 no.5
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• pp.471-475
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• 1990

A thermostable adenylate kinase isolated from the sonic extracts of Thermus caldophilus cells revealed higher substrate-specificity to the nucleoside monophosphate than to the nucleoside triphosphate. A $P', P^5$-di(adenosine-5') pentaphosphate was acted as a competitive inhibitor to the various substrates. Various divalent cations were activated the enzyme activity following orders: $Mg^{2+}, Ca^{2+}, Mn^{2+}, Ba^[2+}, $ and $Fe^{2+}$-. The enzyme activity was not affected by the sulfurhydryl reagent, p-chloromeric uribenzoic acid and activated by addition of the sodium chloride or phosphoenol pyruvate to the reaction mixture.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.1
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• pp.35-39
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• 1991

Properties of a protease purified from Neungee[Sarcodon aspratus(Berk, ) S. Ito] have been investigated. The enzyme displays a glycosylated serine protease. The enzyme is able to hydrolyze alanine glycine methionine glutamine and cysteine of N-CBZ and N-t-BOC-L-amino acid derivatibes relatively strongly but splits valine proline and isoleucine derivatives with low affinity which means the enzyme has the broad substrate spectrum toward the amino acids. Interestingly the enzyme was inhibited by bromelain inhibitor. That is the active site environ-ment of the enzyme is believed to be similar to that of bromelain However peptide mapping studies show that the two enzymes have distinct different cleavage sites.

• Biomedical Science Letters
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• v.14 no.1
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• pp.63-68
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• 2008

The aqueous extract from the fruit body of Lentinus edodes was evaluated for inhibitory activities against $\alpha$-glucosidase isolated from Spargue-Dawley male rats. A aqueous extract of Lentinus edodes exhibited 13.8% inhibitory activity on using 2 mM p-nitrophenyl $\alpha$-D-glucopyranoside as a substrate ($IC_{50}$ 75.3 mg/ml). The aqueous extract of Lentinus edodes inhibition type on $\alpha$-glucosidase was determined to be competitive inhibition. When it was oral administered to increase of blood glucose levels after STZ-induced in a dose dependent dietary. These results suggest that aqueous extract of Lentinus edodes effect a metabolism of intestine, and thereby reducing the increase of blood glucose after STZ-induced.

• Journal of Environmental Science International
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• v.4 no.2
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• pp.215-222
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• 1995

Thiokncillus neapolitanus R-10 isolated from sludge of night soil, showed an oxidizing activity on several malodorous sulfur compounds. The microbe successfully utilized hydrogen sulfide(H2S), methy mercaptan(MM), dimethyl sulfide(DMS) and dimethyldisulfide(DMDS) during the batch culture reaction, of which H2S was rather rapidly oxidized. To examine the ability for removal of malodorous sulfur compounds, various concentrations of sulfide substrates were supplemented separately to basal medium and their responses were investigated. As the concentration of sulfide was increased, growth was accelerated within three days of cultivation. 2.5mM was the most favorable substrate concentration of sulfide added for all cases tested. However, when the concentration of sulfur compounds were raised over 4M, they behaved as a growth inhibitor.

• YAKHAK HOEJI
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• v.38 no.6
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• pp.791-794
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• 1994

Sixteen kinds of naturally occurring phenolic compounds including 5 stilbenes, 7 flavonoids and 4 anthraquinones were examined in the inhibitory activity against rat liver AADC(aromatic L-amino acid decarboxylase) in vitro, using 5-hydroxytryptophan as a substrate. Three hydroxystilbenes, resveratrol 1, rhapontigenin 3 and piceatanol 5, which were known to be monoamine oxidase A inhibitors, exhibited a significant inhibition against AADC($IC_{50}$=20, 8 and $5\;{\mu}M$, respectively). By the comparison of the activity of each phenolic compound, it was suggested that the 3',4'-dihydroxyphenyl group of stilbenes or flavones was the best pharmacophore for the AADC inhibitory activity.

• Archives of Pharmacal Research
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• v.21 no.2
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• pp.207-211
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• 1998

Three prolyl endopeptidase inhibitors were isolated and identified as luteolin, quercetin and ${\beta}$-sitosterol-3-O-${\beta}$-D-glucopyranoside with $IC_{50}$ of 0.17, 0.19 and 27.5 ppm, respectively. The inhibition of two flavonoids were non-competitive with substrate. Twenty authentic flavonoids were tested in order to investigate structure-activity relationship. No significant relationship was found in them, however, catechol moiety of B-ring and 7-OH group in flavonoid skeleton were seemed to be responsible for the stronger activity.