• The Korean Journal of Mycology
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• v.33 no.2
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• pp.69-74
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• 2005

Fibrinolytic enzyme has been isolated and purified from the edible mushroom, Lepista nuda. The apparent molecular mass of purified enzyme was estimated to be 34 KDa by SDS-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence of the enzyme was Tyr-Pro-Ser-Pro-Ser-His-Gln-Thr-Ala-Val-Asn-Ala-Ile-Ile-X. It has a pH optimum at $7.0.{\sim}9.5$, suggesting that the purified enzyme is an alkaline protease. It shows the maximum fibrinolytic activity at $55^{\circ}C$. The fibrinolytic activity was inhibited by phenylmethylsulfonyl fluoride, indicating that the purified enzyme is a serine protease. The activity of the purified enzyme was totally inhibited by $Hg^{2+}$.

• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.6
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• pp.593-598
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• 2005

A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be approximately 35.0kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Ser-Asn. The optimum temperature and pH for the enzyme activity were $35^{\circ}C$ and 7.5, respectively. The enzyme activity was stable within the pH and temperature ranges 6.8-8.0 and $20{\sim}35^{\circ}C$, respectively. The purified enzyme was strongly activated by $Zn^{2+},\;Li^{2+},\;and\;Ca^{2+}$, but inhibited by $Cu^{2+}$. In addition, the enzyme was strongly inhibited by 1, 10-phenanthroline and EDTA. The purified enzyme was suggested to be a neutral metalloprotease.

• Journal of Microbiology and Biotechnology
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• v.5 no.4
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• pp.206-212
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• 1995

A strain BL-29, which produces a extracellular lytic enzyme on E. coli was isolated from the soil. The strain was identified as belonging to the genus Bacillus sp. The lytic enzyme was purified to homogeneity by ion exchange chromatography and gel filtration. Specific activity of the purified enzyme was 28, 850 U/mg protein and yield of the enzyme was 5$%$. The purified enzyme showed a single band on SDS-PAGE and its molecular weight was estimated to be 31, 000 by SDS-polyacrylamide gel electrophoresis and gel filtration column chromatography. The optimum temperature and pH were $55^{\circ}C$ and pH 10.0, respectively. The enzyme was stable at $45^{\circ}C$ but enzyme activity was reduced by up to 50$%$ when the temperature was raised to $55^{\circ}C$ for 15 min. Stable range of pH was from 5.0 to 11.0. but Enzyme activity was inhibited by lead-acetate, mercuric chloride, ethylene glycol-bis-[$\beta$-aminoethyl ether]-N, N, $N^1, $N^1$-tetraacetic acid (EGTA), and ethylenediamine tetraacetic acid (EDTA), but not affected considerably by treatment with other chemical reagents.

• Analytical Science and Technology
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• v.8 no.4
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• pp.591-596
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• 1995

Enzyme multilayers composed of avidin and biotin-labeled enzymes were prepared on the surface of electrode, through a strong affinity between avidin and biotin (binding constant: ca $10^{15} M^{-1}$). The enzyme multilayers were useful for the improvement of the performance characteristies of enzyme sensors. The output current of the enzyme sensors depended linearly on the number of enzyme layers deposited. Thus, lactate oxidase (LOx) and alcohol oxidase (AlOx) were deposited after being modified with biotin for constructing enzyme sensors sensitive to L-lactate and ethanol respectively. It was also possible to deposit two different kinds of enzymes successively in a single multilayer. The glucose oxidase (GOx) and ascorbate oxidase (AsOx) were built into a multilayer structure on a Platinum electrode. The GOx, AsOx multilayer-modified electrode was useful for the elimination of ascorbic acid interference of the glucose sensor.

• The Journal of Korean Medicine
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• v.18 no.1
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• pp.506-514
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• 1997

This study was conducted to improve preparations of oriental drugs by enzyme. Total sugar, reduced sugar, hydrolysis rate, and amylose content were compared in Korean yam starch and some oriental drugs treated different enzyme levels and treatment times. The results were as follows. Reduced sugar and hydrolysis rate by enzyme of yam starch were significantly increased according to increments of enzyme level and treatment time. Amylose content in yam starch was significantly decreased to increment of enzyme level and treatment time. Total sugar content in some oriental drugs of Sangmaeksan, Yukmigiwhang, Yukshinsan, Manbungsarungsan, and Sanyaksogalum were 46.08, 44.87, 11.15, 10.67, and $6.l6mg/m{\ell}$, respectively. There was no significant difference in hydrolysis rate by enzyme of Sangmaeksan, Yukmigiwhang, Manbungsarungsan. However, hydrolysis rates of Yukshinsan and Sanyaksogalum were significantly highest in 0.2% enzyme and 0.5% enzyme groups, respectively.

• The Korean Journal of Food And Nutrition
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• v.7 no.1
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• pp.51-57
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• 1994

A nuluk, a Korean traditional koji for brewing, was made with wheat flour and Aspergillus usamii mot. shirousamii S1 which had strong abilities in producing amylase and protease. The cultural conditions for the production of saccharogenic and proteolytic enzymes were tested. The productivities of saccharogenic and dextrogenic enzymes were improved when nuluk was made with unsteamed wheat flour as compared with steamed one, but those of proteolytic enzyme and organic acid were reduced. The addition of water containing 0.5% of hydrochloric acid was unfavorable for the production of saccharogenic, dextrogenic and proteolytic enzymes. The optimum ratios of water added to wheat flour for the production of saccharogenic enzyme and proteolytic enzyme were 32% and 28%, respectively on the basis of wheat flour. The optimum temperatures for the production of saccharogenic enzyme and proteolytic enzyme were 36$^{\circ}C$ and 28$^{\circ}C$, respectively. The activity of saccharogenic enzyme reached its maximum after 120 hours of cultivation at 36$^{\circ}C$, but that of proteolytic enzyme 96 hours. The productivity of saccharogenic enzyme was enhanced when the nuluk was molded after 24 hours of precultivation but that of proteolytic enzyme was reduced as compared with no molding.

• Journal of the Korean Society of Food Science and Nutrition
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• v.24 no.4
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• pp.563-569
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• 1995

Myrosinase from Korean cabbage(Bogdoli) was purified and its enzymatic properties were investigated. Myrosinase from the Korean cabbage was purified by DEAE Bio-Gel Sepharose, Concanavalin-A, and Mono-Q column chromatography and exhibited a 55KD molecular weight with a single band on the gel of SDS-PAGE. The enzyme was purified about 21-fold compared to its crude enzyme and a specific activity of purified enzyme was 15, 120units/mg. Optimum pH of the myrosinase was 7.0 in both phosphate and Tris-HCl buffer solutions, the enzyme was stable at pH 6.5~7.0. Optimum temperature of enzyme was 37~38$^{\circ}C$. The enzyme activity was significantly inhibited by Cu2+ and Hg2+, but enhanced by ascorbic acid, resulting in a maximum activity at 1mM ascorbic acid. Among the ascorbic acid analogues, dehydro-ascorbic acid did not affect, whereas others showed a little effect on the enzyme activity, but less than ascorbic acid itself. Reducing agents such as 2-mercaptoethanol and dithiothreitol had no effect on the enzyme activity, but the enzyme activity was enhanced when 2-mercaptoethanol was mixed with ascorbic acid.

• Korean Chemical Engineering Research
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• v.54 no.2
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• pp.171-174
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• 2016

Enzyme fuel cells were composed of enzyme cathode and PEMFC anode. Enzyme cathode was fabricated by compression of a mixture of graphite particle, laccase as a enzyme and ABTS as a redox mediator, and then coated with Nafion ionomer. Open circuit voltage (OCV) were measured with variation of cathode manufacture factors, to find optimum condition of enzyme cathode. Optimum pressure was 4.0 bar for enzyme cathode pressing process. Highest OCV was obtained at 95% graphite composition in enzyme cathodee. Optimum glucose concentration was 0.4 mol/l in cathode substrate solution.

• Korean Journal of Agricultural Science
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• v.46 no.1
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• pp.1-10
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• 2019

The objective of this study was to determine the effect of multi-enzyme supplementation in a corn and soybean meal-based diet on the growth performance, apparent nutrient digestibility, blood profile, fecal microbes and noxious gas emission in growing pigs. A total of 80 crossbred [(Landrace ${\times}$ Yorkshire) ${\times}$ Duroc] growing pigs with an average body weight (BW) of $25.04{\pm}1.44kg$ were used in a 6-week experiment. The experimental treatments were as follows: CON, basal diet and; T1, basal diet + 100 mg/kg multi-enzyme. During the experiment, the pigs fed the diet with multi-enzyme supplementation had a higher gain to feed ratio (G/F) (p < 0.05) than the pigs fed the diet without multi-enzyme supplementation. On day 42, the pigs fed the diet with multi-enzyme supplementation had decreased $H_2S$ and $NH_3$ emissions (p < 0.05) than the pigs fed the diet without multi-enzyme supplementation. However, no effect was observed on nutrient digestibility, blood profiles and fecal microbes among the treatments (p > 0.05). In conclusion, it is suggested that multi-enzyme supplementation in a corn and soybean meal based diet can partly improve the growth performance and noxious gas emission of growing pigs.

• Korean Journal of Agricultural Science
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• v.48 no.2
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• pp.201-207
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• 2021

This study evaluated the influence of enzyme mixture supplementation on the growth performance, nutrient digestibility, and fecal score of growing pigs. A total of 72 pigs with an initial body weight of 20.23 ± 1.46 kg were randomly assigned to two treatments consisting of a basal diet and the basal diet supplemented with 0.5% enzyme mixture. During a 19-day trial, no significant difference was observed in the body weight (BW) and average daily feed intake (ADFI) of the pigs. However, a gradual increase in the average daily gain (ADG) was observed during the period from day 14 to day 19 and the overall period in pigs fed a diet supplemented with the 0.5% enzyme mixture (p < 0.10) as compared to the pigs that were fed the control diet. From days 4 to 14 and in the overall experiment, a gradual increase in the feed conversion ratio (FCR) (p < 0.10) was observed with the inclusion of 0.5% enzyme mixture supplementation. The nutrient digestibility of dry matter (DM), nitrogen (N), and energy were not affected by enzyme mixture supplementation. In addition, dietary supplementation with the enzyme mixture had no significant effects on the fecal score of growing pigs. In summary, supplementation with the enzyme mixture had beneficial effects on the ADG performance but failed to have a significant effect on growth performance (BW), nutrient digestibility, and fecal score.