• Advances in Traditional Medicine
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• v.3 no.1
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• pp.46-50
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• 2003

We studied the inhibitory effect of Green Life Enzyme (GLE) on compound 48/80-induced anaphylactic response in a murine model. GLE inhibited compound 48/80-induced systemic anaphylactic shock at the dose of 10 g/kg by 87.5%. When GLE was given as pre-treatment at concentrations ranging from 0.01 to 1.0 g/kg, it inhibited passive cutaneous anaphylaxis activated by anti-dinitrophenyl (DNP) IgE. In addition, GLE (0.1 mg/ml) inhibited anti-DNP IgE-induced tumor necrosis $factor-{\alpha}$ production from mast cells by 69% compared to saline value. These results indicate that GLE may possess anti-anaphylactic and anti-inflammatory activity.

• Journal of the East Asian Society of Dietary Life
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• v.16 no.5
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• pp.550-558
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• 2006

The study investigated the serum lipid metabolism and enzyme activities of Korean teas for their preventative activity against chronic disease and obesity. Male Sprague-Dawley rats were raised for 8 weeks on four experimental diets: normal diet, hyperlipidemic diet, and hyperlipidemic diet to which green and black teas (2% each) were added. Various biological actions, including lipid metabolism and enzyme activities of the serum, were investigated. Diet-induced, hyperlipidemic rats fed with green and black teas, showed significant decrease in food efficiency ratio, triglyceride, total lipid, and phospholipid compared to control, i.e. the normal and diet-induced, hyperlipidemic rats. Total cholesterol, LDL-cholesterol, Al(atherogenic index), LHR, VLDL-cholesterol, ester-cholesterol, and free-cholesterol also showed a significant decrease. However, there was no significant difference between the tea-fed, diet-induced, hyperlipidemic dieted groups. HDL-cholesterol concentration was increased significantly in the tea-dieted and normal groups compared to the control. There was a little difference in lipase activity between the normal and control groups, although green and black tea-dieted experimental groups were both increased compared to the control. The contents of total lipid, triglycerides, and total cholesterol were decreased in the normal and experimental groups compared to the control. The GOT, GPT, ALP and LDH serum enzyme activities of the experimental groups were significantly reduced compared to those of the control groups.

• Journal of Microbiology and Biotechnology
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• v.24 no.1
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• pp.80-86
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• 2014

Tannase (Tan410) from a soil metagenomic library was immobilized on different supports, including mesoporous silica SBA-15, chitosan, calcium alginate, and amberlite IRC 50. Entrapment in calcium alginate beads was comparatively found to be the best method and was further characterized. The optimum pH of the immobilized Tan410 was shifted toward neutrality compared with the free enzyme (from pH 6.4 to pH 7.0). The optimum temperature was determined to be $45^{\circ}C$ for the immobilized enzyme and $30^{\circ}C$ for the free enzyme, respectively. The immobilized enzyme had no loss of activity after 10 cycles, and retained more than 90% of its original activity after storage for 30 days. After immobilization, the enzyme activity was only slightly affected by $Hg^{2+}$, which completely inhibited the activity of the free enzyme. The immobilized tannase was used to remove 80% of tannins from a green tea infusion on the first treatment. The beads were used for six successive runs resulting in overall hydrolysis of 56% of the tannins.

• Korean Journal of Veterinary Research
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• v.32 no.4
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• pp.677-681
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• 1992

This experiment was carried out to establish a proper method of indocyanine green(ICG) excrection test for a applicable liver function test in three Korean native cattle average weighing about 450kg and dairy cattle parity of 3~5. The results obtained the half life($T^1/_2$), fractional clearance rate(KICG), retention rate and plasma enzyme activities before or after injection of ICG were as follows. 1. The maximum absorbance of ICG in plasma was at 805nm. 2. Average half life and fractional clearance rate following the injection of ICG 0.25mg/kg body weight were $5.53{\pm}1.27$ minute and $0.131{\pm}0.031$/minute in Korean native cattle, $4.55{\pm}0.68$ minute and $0.156{\pm}0.031$/minute in dairy cattle, respectively. The ICG removal rate was exponentially liner for the first 15 minutes after injection both of Korean native cattle and dairy cattle. 3. Average plasma retention rate when 10, 15, 30 minutes after injection was $35.7{\pm}13.9$, $23.2{\pm}7.1$, $10.8{\pm}3.5%$ in Korean native cattle, $26.8{\pm}3.3$, $14.2{\pm}1.2$, $5.5{\pm}2.2%$ in dairy cattle, respectively. 4. Plasma enzyme activities(AST, ALT, r-GTP) were no variation among the before, during and after injection of ICG. From these results, ICG excretion test to cattle is applicable to evaluation of liver funtion in both clinical and research, and adopted the 15 minutes plasma sample as the sample taken at the ideal time for comparative purposes.

• Journal of Microbiology and Biotechnology
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• v.19 no.11
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• pp.1421-1430
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• 2009

With an aim to evaluate dye decolorization by white rot fungus on natural living conditions, reproducing by solid-state fermentation, the process of triphenylmethane dyes decolorization using the white rot fungus P. ostreatus BP, cultivated on rice straw solid-state medium, has been demonstrated. Three typical dyes, including malachite green, bromophenol blue, and crystal violet, were almost completely decolorized by the fungus after 9 days of incubation. During the process of dye decolorization, the activities of enzyme secreted by the fungus, and the contents of soluble components, such as phenolic compounds, protein, and sugar, changed regularly. The fungus could produce ligninolytic, cellulolytic, and hemicellulolytic enzymes and laccase was the most dominant enzyme in solid-state medium. Laccase, laccase isoenzyme, and the laccase mediator could explain the decolorization of malachite green, bromophenol blue, and crystal violet by the fungus in solid-state medium, respectively. It is worth noting that the presence of the water-soluble phenolic compounds could stimulate the growth of fungus, enhance the production of laccase, and accelerate dye decolorization.

• Food Science and Biotechnology
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• v.15 no.6
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• pp.838-843
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• 2006

The chemical processes involved in the formation of green pigment in crushed garlic cloves were investigated based on the principle of pink pigmentation in macerated onions. Intact greening and non-greening garlic cloves were either left untreated or heated at $90^{\circ}C$ for 3 min to inactivate enzyme activities. First, a colorless ether soluble compound referred to as color developer reacted with glycine (among all free amino acids) in garlic to form a second compound insoluble in ether. The latter compound then reacted with formaldehyde to yield the green colored pigment. Alliinase activity was necessary for the production of color developer and for the development of green pigment. In greening garlic that had been heat treated, green pigmentation did not proceed due to the heat-inactivation of alliinase, but the addition of alliinase solution into the garlic homogenates restored the pigmentation. However, this phenomenon was not observed in non-greening garlic with or without heat treatment. Finally, the mechanism of green pigment formation in crushed garlicis similar to that of pink pigment formation in macerated onions.

• Food Science and Biotechnology
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• v.15 no.6
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• pp.914-919
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• 2006

We investigated the catechin content in green tea leaf (GTL) and green tea seed (GTS), the antiproliferative and detoxifying phase II enzyme-inducing activities of the methanolic (80%, v/v) extracts from GTL and GTS. GTL and GTS contained $8,685{\pm}1,061$ and $108{\pm}32\;{\mu}g/g$ epigallocatechin gallate (EGCG), $11,486{\pm}506$ and $116{\pm}72\;{\mu}g/g$ epigallocatechin (EGC), $3,535{\pm}308$ and $821{\pm}95\;{\mu}g/g$ epicatechin gallate (ECG), and $1,429{\pm}177$ and $37{\pm}44\;{\mu}g/g$ epicatechin (EC), respectively. The methanolic extract of GTS showed a greater increase in quinone reductase activity and antiproliferation potential against mouse hepatoma cells than GTL extract did. GTS treatment resulted in the accumulation at sub-G1 phase of mouse hepatoma hepa1c1c7 cells as assessed by flow cytometry. Enhancement of phase II enzyme activity by GTS extract was shown to be mediated, directly or indirectly, via interaction with the antioxidant response element (ARE) sequence in the genes encoding the phase enzymes. As the catechin content in GTS was significantly lower than that in GTL, components other than catechins appear to be responsible for the anticarcinogenic activity of the seed. In summary, these results suggest that the 80% methanolic extract of GTS deserves further study to evaluate its potential as an anticarcinogenic agent and to investigate its mechanism of action.

• Molecules and Cells
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• v.40 no.10
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• pp.773-786
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• 2017

The loss of green coloration via chlorophyll (Chl) degradation typically occurs during leaf senescence. To date, many Chl catabolic enzymes have been identified and shown to interact with light harvesting complex II to form a Chl degradation complex in senescing chloroplasts; this complex might metabolically channel phototoxic Chl catabolic intermediates to prevent oxidative damage to cells. The Chl catabolic enzyme 7-hydroxymethyl Chl a reductase (HCAR) converts 7-hydroxymethyl Chl a (7-HMC a) to Chl a. The rice (Oryza sativa) genome contains a single HCAR homolog (OsHCAR), but its exact role remains unknown. Here, we show that an oshcar knockout mutant exhibits persistent green leaves during both dark-induced and natural senescence, and accumulates 7-HMC a and pheophorbide a (Pheo a) in green leaf blades. Interestingly, both rice and Arabidopsis hcar mutants exhibit severe cell death at the vegetative stage; this cell death largely occurs in a light intensity-dependent manner. In addition, 7-HMC a treatment led to the generation of singlet oxygen ($^1O_2$) in Arabidopsis and rice protoplasts in the light. Under herbicide-induced oxidative stress conditions, leaf necrosis was more severe in hcar plants than in wild type, and HCAR-overexpressing plants were more tolerant to reactive oxygen species than wild type. Therefore, in addition to functioning in the conversion of 7-HMC a to Chl a in senescent leaves, HCAR may play a critical role in protecting plants from high light-induced damage by preventing the accumulation of 7-HMC a and Pheo a in developing and mature leaves at the vegetative stage.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.11
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• pp.1501-1506
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• 2011

In this study, we optimized the reaction conditions for the bioconversion of green tea using tannase, and to evaluate its radical scavenging activities. Tea catechins such as (-)-epigallocatechin gallate (EGCG) or (-)-epicatechin gallate (ECG) were hydrolyzed by tannase to produce (-)-epigallocatechin (EGC) or (-)-epicatechin (EC), respectively, and a common product, gallic acid. The bioconversion of tea catechins by tannase was increased as enzyme concentration, substrate concentration and incubation time for enzyme dose. The results indicated the optimum reaction conditions for tannase were tannase 30 U/mL (enzyme concentration) on 1% green tea (substrate concentration) for 1 hr (incubation time for enzyme). Tannase enhanced the radical-scavenging properties of green tea; the 2,2-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) and 1,1-diphenyl-2-picrylhydrazyl (DPPH) radicals scavenging abilities were significantly (p<0.001) greater for the tannase-treated green tea extract compared to the untreated green tea extract. It is reported that ECG has the greatest antioxidant activity among the catechins in green tea, and the release of gallic acid is considered to be beneficial because of its significant antioxidant potency. The results of this study suggest that the tannase-treated green tea increases antioxidant activities under optimum reaction conditions.

• Mycobiology
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• v.40 no.3
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• pp.173-180
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• 2012

A ${\beta}$-glucosidase from Penicillium italicum was purified with a specific activity of 61.8 U/mg, using a chromatography system. The native form of the enzyme was an 88.5-kDa tetramer with a molecular mass of 354 kDa. Optimum activity was observed at pH 4.5 and $60^{\circ}C$, and the half-lives were 1,737, 330, 34, and 1 hr at 50, 55, 60, and $65^{\circ}C$, respectively. Its activity was inhibited by 47% by 5 mM $Ni^{2+}$. The enzyme exhibited hydrolytic activity for p-nitrophenyl-${\beta}$-D-glucopyranoside (pNP-Glu), p-nitrophenyl-${\beta}$-D-cellobioside, p-nitrophenyl-${\beta}$-D-xyloside, and cellobiose, however, no activity was observed for p-nitrophenyl-${\beta}$-D-lactopyranoside, p-nitrophenyl-${\beta}$-D-galactopyranoside, carboxymetyl cellulose, xylan, and cellulose, indicating that the enzyme was a ${\beta}$-glucosidase. The $k_{cat}/K_m\;(s^{-1}mM^{-1})$ values for pNP-Glu and cellobiose were 15,770.4 mM and 6,361.4 mM, respectively. These values were the highest reported for ${\beta}$-glucosidases. Non-competitive inhibition of the enzyme by both glucose ($K_i=8.9mM$) and glucono-${\delta}$-lactone ($K_i=11.3mM$) was observed when pNP-Glu was used as the substrate. This is the first report of non-competitive inhibition of ${\beta}$-glucosidase by glucose and glucono-${\delta}$-lactone.