• Journal of Ginseng Research
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• v.23 no.2 s.54
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• pp.93-98
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• 1999

In order to evalulate the qualities of red ginseng extract and decrease precipitate fonnation in ginseng drink, red ginseng extract was hydrolized with ${\beta}-amylase$ and transglucosidase. $5.2\%$ isomaltose was produced as isomaltooligosaccharides and glucose content was increased in the enzyme treated ginseng extract. Contents of ginsenoside $R-b_1\;and\;R-b_2$ were decreased, whereas ginsenoside-Rd was increased by the enzyme treatments. The growth of 3 strains of bifidus spp. and 4 strains of lactobacillus spp., beneficial intestinal bacteria, were enhanced by adding of the enzymatically hydrolized ginseng extract. Sweetness and sourness were increased, however, bitterness and astringency were decreased in the hydrolized ginseng extract. The fonnation of precipitates in hydrolized red ginseng extract of $pH\;3.0\~4.5$ were significantly decreased in the storage condition of $40^{\circ}C$ for 1 month compared to that of control.

• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.197-205
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• 1996

The $\beta$-xylosidase was purified 99- fold from the culture supernatant of Pseudo onas sp. CB-33 by ammonium sulfate precipitation, PEI precipita- tion, DEAE-Sephadex column chromatography, Sephadex G-75 gel filtration chromatography and preparative disc gel electrophoresis. Molecular weight of the enzyme was estimated to be 44,000 by SDS polyacrylamide gel electrophoresis. The enzyme has a pH optimum for activity at 7.0 and is stable over pH 6.5-9.0. The optimal temperature of the enzyme was 45$\circ$C, and its enzymatic activity was completely inactivated at 55$\circ$C for 30 min. Km value of the enzyme for p-nitrophenyl-$\beta$-D-xylopyranoside was calculated to be 4.6 mM. The effect of various reagents on the $\beta$-xylosidase activity was investigated. The enzyme activity was completely inhibited by Hg$^{2+}$, Cu$^{2+}$ and Zn$^{2+}$. The $\beta$-xylosidase was inactivated by tryptophan-specific reagent, N-bromosuccinimide and tyrosine-specific reagent, iodine. The enzyme could degrade xylo-oligosaccharides to xylose and the enzyme was competitively inhibited by xylose. The $\beta$-xylosidase and endoxylanase from Psedomonas sp. CB-33 hydrolized xylan synergically. The purified enzyme also showed $\alpha$-L-arabinofuranosidase activity.

• Microbiology and Biotechnology Letters
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• v.13 no.3
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• pp.191-198
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• 1985

Seven different strains of lactic bacteria and 13 combinations of these microorganisms were tested for their acid forming capacity on a vegetable milk made from lupinseed protein concentrate(LPC). L acidophilus, L casei, S. lactis, L. mesenteroides, mixed culture of L. acidophilus and S. thermophilus, and mixed culture of S. lactis and L. mesenteroides were selected and further tested for their growth pattern and acid forming property on lupinseed milk both untreated and partly hydrolized one with carbohydrate decomposing enzymes. The enzyme hydrolized lupinseed milk had 1.5 folds of total free sugar, 8.2 folds of fructose, 3 folds glucose, 2.3 folds maltose, compared to the untreated lupinseed milk. For the untreated lupinseed milk, L. mesenteroides was appeared to be most suitable microorganism having the maximum cell concentration of 1.0 $\times$ 10$^{9}$ $m\ell$ and the final pH 4.40 with the acidity 0.46％. For the enzyme treated lupinseed milk, mixed culture of L. acidophilus and S. thermophilus showed the best performance having 1.9$\times$10$^{9}$ $m\ell$ maximum cell number and the final pH and acidity were 3.69 and 1.13％, respectively. Lactic acid fermentation altered the physical property of lupinseed milk; by fermentation the viscosity generally increased with untreated lupinseed milk, but decreased with enzyme hydrolized one. The viscosity change and sedimentation rate of fermented milk varied with the type of lactic bacteria. The results of sensory evaluation indicated that S. lactis, L. casei, mixed culture of S. lactis and L. mesenteroides, and mixed culture of L. acidophilus and S. thermophilus, grown on enzyme hydrolized lupinseed milk, could produce acceptable lactic beverage.

• Journal of the Korean Wood Science and Technology
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• v.15 no.3
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• pp.34-43
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• 1987

This study was performed to find out the types of linkage of carbohydrates in wood cell walls. To study the structure of linkage of carbohydrates in wood cell walls, we have attempted to find out the method holocellulose preparation and optimum condition of enzyme hydrolysis in holocellulose, and fractionate oligosaccharide with products that hydrolized partly by acetolysis and deacetylation in holocellulose. We have achieved four results. These results as follow; 1. At first. we reacted in wood meal $NaClO_2$ 1g per lignin lg for one hour and then the same of quantity $NaClO_2$ for four hours. Through these experiments, we have developed new holocellulose preparation method which had low loss of carbohydrates and high effect of the delignification. 2. The optimum condition of enzyme hydrolysis of holocellulose which had lignin was 0.005M sodium acetate buffer (pH 5.0). We have achieved 7.2% reducing sugar through the procedure that reactioned 0.01g holocellulose putting enzyme 0.03g for 72 hours. It may be supposed that 5.5% of lignin contained in holocellulose prevented enzyme contaction from holocellulose and so this lignin has resulted in the low efficiency of enzyme hydrolysis. 3. We did not fractionated from oligosaccharides which were preparated by the method of acetolysis and deacetylation in holocellulose. The reason is that holocellulose having a lot of lignin prevented prefectly partial hydrolysis from the method of acetolysis and deacetylation. 4. We attempted analysis of six standard substances through HPLC apparatus having sugar pak 1 column which we have changed flow rate and the column temperature variably. These six standard substances were D-glucose, D-mannose, D-xylose, D-galactose and L-rhamnose, L-arabinose, But sugar pak 1 column was not fitted analysis of four substances because D-galactose, D-mannose, D-xylose, L-rhamnose were agreement with elution time. And so, we could not analize four standard substances with sugar pak 1 column.

• Microbiology and Biotechnology Letters
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• v.2 no.2
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• pp.111-117
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• 1974

Studies were carried out on the practical use of Naringinase and some chracteristics of Naringin solublizing enzme which might hydrolyae naringin to purunin. Obtained results were as follows. 1. Selected strain for Naringinase producing was identified to be Aspergillus niger S-1 and its naringinase was applied to chinese citron processing to remove the bitter taste. 2. Of the naringinase, naringin solubilizing enzyme was purified on a DEAE-Sephadex A-50 column and crystalized from acetone and ammonium sulfate. 3. Hydrolized naringin which has higher solubility rather than naringin or naringenin were identified by thin layer chromatography. 4. Hydrolyzed naringin and naringin were separatly determinated by ethylacetate extraction and this result was compared with sensory test.

• YAKHAK HOEJI
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• v.41 no.5
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• pp.615-621
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• 1997

Dehydropeptidase-I (DHP-I) was solubilized from porcine kidney by treatment with n-butanol and partially purified 19.25 fold by $(NH_4)_2SO_4$ precipitation, DEAE-Sepharose CL-6B ion exchange chromatography and Sephacryl S-300 HR chromatography with an overall yield of 19.16. DHP-I showed its optimal activity at pH 7.5 and 25$^{\circ}C$. Its activity was stable under neutral and alkaline conditions, but was disappeared under acidic condition. And DHP-I was heat-labile and its activity remained at 45$^{\circ}C$ for 3hrs. The enzyme was not inhibited by dicationic ions, while its activity was increased by $Co^{2+}$(1mM) and $Zn^{2+}$ (0.1mM). The enzyme was inhibited by EDTA and N-ethylmaleimide. The relative molecular mass of DHP-I was estimated to be approximately 100kDa by gel filtration chromatography. The $K_m$ value of DHP-I for glycyldehydrophenylalanine (GDHP) was 1.98mM. DWP20418 [(1R, 5S, 6S)-6-[1-(R)-Hydroxyethyl]-1-methyl-2-[(2S, 4S)-2-(piperazinylcarbonyl)-1-(R)-hydroxyethyl)pyrrolidine-4-thio]carbapen-2-em-3-carboxylic acid], compared with meropenem (MEPM), was rather easily hydrolized by DHP-I, while it was four times more resistant than imipenem (IPM) to DHP-I.

• Applied Microscopy
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• v.14 no.2
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• pp.66-80
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• 1984

The organic phosphorus compounds have been widely used as an insecticide, since toxicity of these compounds is especially drastic to the insects than to men and other mammals. The organic phosphates are rapidly hydrolized and hence have little cumulative and ecologic effects. However, due to their acute toxic effects organophosphate have recorded rather high fatalities in men and domestic animals. The organic phosphorus compounds are powerful inhibitors to the carboxylic esterase enzymes such as acetylcholinesterase and pseudocholinesterase. As a result of firm binding characteristics of phosphate radicals to the active sites of enzyme, the activities of these enzymes are inhibited by the organophosphates. The organophosphates such as diazinon is easily observed from skin, gastrointestinal tract, conjunctivas and respiratory tract, and it is converted to more toxic form during metabolism in the liver The present study was carried out in order to investigate the hepatotoxicity of diazinon by observing the changes in the ultrastructure of cytoplasmic organelles of hepatic cells in albino mice. The animals were killed at 6, 12 and 24 hours after administration of 25mg/kg diazinon. The piece of hepatic tissue obtained from each animal was ultrathinly sectioned. The specimens stained by uranyl acetate and lead citrate double contrast methods were observed with JEM model 100B electron microscope. The results obtained were as follows: 1) A prominent dilatation and sacculation of the cisternae of rough endoplasmic reticulum associated with detachment of membrane bound-ribosomes, and disaggregation of the free ribosomes were recognized. 2) The hypertrophy of the smooth endoplasmic reticulum associated with depletion of the glycogen particles was observed. 3) The atrophy of cisternae of Golgi complex was observed. 4) A large number of secondary lysosomes (autophagic vacuoles and residual bodies) were formed. Consequently it is suggested that diazinon would induce disorganization of the cytoplasmic organelles of hepatocytes in albino mice.

• Korean Journal of Poultry Science
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• v.48 no.3
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• pp.133-142
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• 2021

The purpose of this study was to investigate whether enzyme-hydrolyzed poultry by-product meal (EHPBM) is more effective as a protein source than poultry by-product meal (PBM) and soybean meal (SBM) for broiler chickens. A group of 300 one-day-old broiler chicks was randomly allocated to three treatments with five replicates (20 birds/replicate) for five weeks. The treatments consisted of basal diets containing 1) SBM, 2) PBM, and 3) EHPBM. The EHPBM-fed group (1,853 g±125.60) showed the highest final body weight (P<0.05) when compared to the PBM-fed group (1,723 g±76.81) and SBM-fed group (1,545 g±62.31). The feed conversion ratio of the EHPBM treatment group (1.740±0.104) was significantly higher (P<0.05) than those of the SBM (1.653±0.056) and PBM groups (1.674±0.072). It can be speculated that the increased feed intake in the EHPBM group led to higher body weight gain and FCR. There was no significant effect of treatments on internal organ weight except for the bursa of Fabricius. Blood biochemical characteristic analysis showed that aspartate aminotransferase and alkaline phosphatase levels were higher in the EHPBM and PBM groups (P<0.05), probably due to the strained liver caused by the rapid growth of birds. In conclusion, EHPBM may partly replace conventional dietary protein sources such as soybean meal or poultry by-product meal and can be used to improve the productivity of broilers.