• Korean Journal of Animal Reproduction
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• v.22 no.1
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• pp.81-87
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• 1998

This experiment was carried out with 12 Korean native heifers(8~12month old, body weight, 160~240kg) raised at a farm of Chang-Soo Livestock Cooperatives to evaluate the effects of rGH(recombinant growth hormone) on serum concentrations of growth hormone, estrogen, and IGF-I, weight gain, teat volume gain and processing enzyme activity of IGF-I, binding protein III at 28 day intervals. Animals used were injected with 250mg rGH at 14 day intervals from December to Ferbruary in 1994. The significant difference was found in the group of treatment on the 4th week in the endogenous GH(p<.01) and 8th week in estrogen and IGF-I(p<.05) after injectin of rGH in Korean native heifers. There were significant differences between control group and treatment group in weight and teat volume on 8th week after treatment(p<.05). Processing enzyme activity before injection of rGH were low. However, heifers injected with 250mg of rGH showed that processing enzyme activity of IGF binding protein was highly increased throughout the experiment. Present results suggest that injection of exogenous rGH to heifers can increase the growth performance and udder development of Korean native heifers by the endogenous hormonal changes.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.2
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• pp.118-125
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• 2011

In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

• Journal of the East Asian Society of Dietary Life
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• v.7 no.1
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• pp.29-33
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• 1997

The efficient production of glucose isomerase (G. I0.) produced form Arthrobacter sp. L-3 was studied. The optimum culture time of the enzyme was 40hr. The maximum enzyme activity was found at glucose concentration 1%. G. I. activity did not affect inoculum size. The glucose isomerase activity was strongly influenced by the addition of glucose.

• Korean Journal of Microbiology
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• v.29 no.5
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• pp.301-306
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• 1991

Extracellular fructosyl transferase from Aureobasidium pullulans C-23 was characterized. The molecular weight of the isolated enzyme was determined to be approximately 170,000 by SDS polyacrylamide gel electrophoresis. The enzyme has the pI value of about 3.7. The enzyme was almost completely inhibited by 5mM $Hg^{2+}$ , but was not significantly affected by other cations tested. The enzyme was inactivated by treatment of tryptophan-specific reagent N-bromo- succinimide and tyrosine-specific reagent iodine. The substrate sucrose showed protective effect on the inactivation of the enzyme by the both reagents. These results suggest that tryptophan and tyrosine residues are probably located at or near active site of the enzyme.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.35 no.3
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• pp.66-73
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• 2003

Alkaline cellulolytic enzymes are prepared from Coprinus cinereus 2249. Recovery method of enzyme protein from cultured medium and effect factors on enzyme activity of protein were investigated. The results could summarized as follows, \circled1 Amount of enzyme protein from cultured medium was highest in incubation with shaking and addition of skim milk. \circled2 Protein from cultured medium was alkaline enzymatic protein which shows the highest activity at pH 9.0. \circled3 The most effective recovery method of enzyme protein was the precipitation of protein by addition of cultured medium of protein in ethanol. \circled4 The enzyme activity was enhanced by tween-80 and decreased with $Al_2(SO_4)_3$, $H_2O_2$et al, and was little changed with metal ions except $Hg^{++}$.

• Korean Journal of Microbiology
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• v.29 no.6
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• pp.345-352
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• 1991

A serine proteinase of molecular weight 60 kd was purified from culture supernatant of P. aeruginosa using DEAE-Trisacryl M ion-exchange and AcA 54 gel filtration column chromatography, and the properties of serine proteinase were characterized. By means of SDS-polyacrylamide gel electrophoresis, the molecular weight of the enzyme was 55 kd. The optimal pH for the activity of purified enzyme was 7.5. The activity of the purified enzyme was completely inhibited by Di-isopropylfluorophosphate(DFP) and N-.alpha.-p-tosyl-L-lysine choloromethyl detone(TLCK) but not by other proteinase inhibitors such as E-64, pepstatin A, 1, 10-phenanthroline. The purified enzyme was capable of degrading type I and type IV collagen. Antisera obtained from hymans infected with Pseudomonas aeruginosa reacted to the purified serine proteinase in immunoblots. These results indicate that the purified enzyme is trypsin-like serine proteinase and this enzyme of P. aeruginosa may play an important role in tissue damage as a spreading factor and may be useful for serodiagnosis of Pseudomonas infections.

• Journal of Environmental Science International
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• v.17 no.12
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• pp.1325-1330
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• 2008

This study was carried out with the detection for multiresidue of the carbamate pesticide such as carbaryl and cabofuran by enzyme-inhibition method. The check time for determination of acetylcholinesterase(AChE) activity was selected at 60 sec. The AChE activity in chicken brain determined by the Ellman's method was $162{\mu}$mol/min/g protein. $I_{50}$ for AChE by carbamate pesticide with wet kit was 0.169mg/L of carbaryl and 0.089mg/L of cabofuran, respectively. The incubation time for enzyme kit with substrate kit was 30min for determination of AChE activity. Enzyme kit with substrate kit was stable at $4^{\circ}C\;and\;25^{\circ}C$ for 5 days. Limit detection concentration of carbaryl with dry kit for AChE was 0.05mg/L. The dry kit such as wet kit applied Enzyme-Inhibition(EI) method with AChE was confirmed the multi residue method to detect the carbamate pesticides.

• Biomolecules & Therapeutics
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• v.14 no.4
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• pp.226-234
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• 2006

Disturbance of antioxidant system is very common in chronic alcoholics and herbal or natural products with antioxidant activity have been used for its treatment. This study was to investigate the effect of Vitis vinifera extract(V), Schisandra chinensis extract(S), Taraxacum officinale extract(T), Gardenia jasminoides extract(G), Angelica acutiloba extract(A) and Paeonia japonica extract(P), and their combinations on the antioxidant and ethanol oxidation system. Male Sprague-Dawley rats were subjected to Lieber-DeCarli ethanol liquid diet(ED) and were then given different herbal extract mixtures for 6 weeks including VST(V 100+S 150+T 150mg/kg/day), VSG(V 100+S 150+G 150mg/kg/day), VTG(V 100+T 150+G 150mg/kg/day), and VAP(V 100+A 150+P 150mg/kg/day). When the activity of alcohol dehydrogenase(ADH) and acetaldehyde dehydrogenase(ALDH) were compared between ED only group and herbal extracts treatment group, the differences were statistically significant. Phase I and II(glutathione-S-transferase, phenol sulfatransferase) enzyme activities were found to be significantly higher in the VAT treatment group compared to the ED group. Herbal extracts not only repressed the ethanol-induced elevation of malondialdehyde level, but also protected against ethanol-induced decrease in glutathione content, glutathione reductase, glutathione peroxidase, catalase and superoxide dismutase activities. The administration of the herbal extracts was found to be effective in eliminating lipid-peroxides induced by long-term consumption of alcohol by activating various enzyme systems and physiological active compound formation system. After a chronic consumption of alcohol, Angelica Radix protected the liver via activating the ethanol-metabolism enzyme system, and Paeoniae Radix via activating the ethanol-metabolism enzyme and the phase I, II-metabolism enzyme system. Taraxaci Herba was also effective in liver protection via activating the ethanol-metabolism enzyme system and the phase I, II-metabolism enzyme system, Gardeniae Fructus via activating the phase II-metabolism enzyme system and the anti-oxidation system enzyme, and Schisandra Fructus and a grapestone via activating the anti-oxidation system. Our data suggest that these herbal extracts may be useful as a health functional food or new drug candidate for fatty liver and hepatotoxicity induced by chronic alcohol consumption.

• BMB Reports
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• v.37 no.4
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• pp.422-428
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• 2004

Raw-starch-digesting $\alpha$-amylase (Amyl III) was purified to an electrophoretically pure state from the extract of a koji culture of Aspergillus awamori KT-11 using wheat bran in the medium. The purified Amyl III digested not only soluble starch but also raw corn starch. The major products from the raw starch using Amyl III were maltotriose and maltose, although a small amount of glucose was produced. Amyl III acted on all raw starch granules that it has been tested on. However, it was considered that the action mode of the Amyl III on starch granules was different from that of glucoamylase judging from the observation of granules under a scanning electron microscope before and after enzyme reaction, and also from the reaction products. Glucoamylase (GA I) was also isolated and it was purified to an electrophoretically pure state from the extract. It was found that the electron micrographic features of the granules after treatment with the enzymes were quite different. A synergistic effect of Amyl III and GA I was observed for the digestion of raw starch granules.

• Textile Coloration and Finishing
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• v.14 no.1
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• pp.18-26
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• 2002

Chitosan has reactive amino and hydroxyl groups which can be used to chemically alter its properties under the mild reaction conditions. Thus the cationization of Tencel with Chitosan is effective to modify the fabric. To investigate the modified properties of Tencel fabric, the tests were performed under the several finishing process with enzyme/glutaraldehyde/softener. The internal structure of Tencel which has the structure of cellulose II wasn't changed by enzyme, chitosan and crosslinking agent treatment and the thermal stability was improved by chitosan and crosslinking agent treatment. Wrinkle recovery angle under the dry condition increased highly until $0.1\textrm{mol}/\ell$ of glutaraldehyde concentration, and then decreased. Tensile strength of modified Tencel fabric decreased with increasing of weight loss, but it was improved more or less by chitosan, crosslinking agent and softener. Moisture regain was improved by enzyme and chitosan treatment. And antibacterial activity showed nearly 100% on Tencel fabric treated with 0.5% chitosan and adsorption of metal ion increased with increasing of chitosan concentration.