• YAKHAK HOEJI
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• v.28 no.1
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• pp.29-33
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• 1984

The paper aimed to review the influences of ginseng on the metabolism of foreign substances and on the activity of hepatic drug metabolizing enzyme system in mouse or rat liver. It has been known that ginseng components reduces the motality rates and the toxic effects induced by foreign materials. Chronic pretreatment of mouse or rat with ginseng extract fractions or saponin caused the increase in the metabolism of foreign materials and the activity of drug metabolizing enzymes, such as cytochrome $P_{450}$, NADPH cytochrome C reductase and glucuronyl S-transferase in liver. Thus, it may be concluded that decrease in toxic effect of foreign substances by ginseng pretreatment may be partly related to the induction of drug metabolizing enzymes in liver.

• Journal of Ginseng Research
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• v.21 no.3
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• pp.174-186
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• 1997

In this study, rat hepatocytes known to have active carbohydrate metabolism were obtained by using the liver perfusion technique to examine the hypoglycemic action of red ginseng saponin components [ginsenoside (mixture, $Rb_1$, and $Rg_1$)] and incubated in two different media-one containing insulin and glucagon (control group), and the other containing glucagon only, The specific activities of some regulatory enzymes such as glucokinase, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glucose 6-phosphatase, in main pathways which were directly related to the glucose metabolism were compared between these two kinds of hepatocytes cultured in two different media. The effects of red ginseng saponin components [ginsenoside (mixture, $Rb_1$, and $Rg_1$)] under the concentration of $10^3$~$10^6$% on these enzymes In hepatocytes were also investigated, when they were added to these two media. The results were as follows. The specific activity of enzymes such as glucokinase, glucose 6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase related to glucose-consuming pathways of insulin-deficient group was much less than control one, however, their decreased activity was recovered after the addition of ginseng components at all range of concentrations. The increased specific activity of these on - zymes was shown by the addition of ginseng components to the control group. On the other hand, the specific activity of glucose 6-phosphatase related to glucose-producing pathway of insulin-deficient group was much higher than control one, but their Increased activity was decreased after the addition of ginseng components at all range of concentrations. The same results were obtained after the addition of ginseng components to the control group. These results suggest that the red ginseng saponin components might better diabetic hyperglycemia by regulating the activity of enzymes related to glucose metabolism directly and/or Indirectly though more detailed studies were needed.

• KSBB Journal
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• v.21 no.1 s.96
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• pp.54-58
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• 2006

The purpose of this study is to search the characteristics of PVA degrading enzymes which were obtained from Microbacterium barkeri KCCM 10507 and Paenibacillus amylolyticus KCCM 10508, respectively. As a result of the PVA degrading test using crude enzymes, the activity of SAO (secondary alcohol oxidase) was maximized after 2 or 3 days from start of the test, while the activity of BDH (${\beta}$-diketone hydrolase) was gradually increased during the test. Activities of them were maintained in the presence of PVA, but as PVA was gradually degraded, their activity was decreased. PVA was inoculated again into the media, their activity was revealed. This result indicated that above two different enzymes were closely connected with PVA degradation and PVA was degraded by activity of SAO and BDH. Maximum activity of them was 1.5-1.8 unit for SAO and 1.5-2.0 unit for BDH under $35^{\circ}C$ and pH 7.8-8.8, respectively.

• BMB Reports
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• v.43 no.11
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• pp.726-731
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• 2010

We report the tissue-specific distribution of chitinolytic activity in Korean ginseng root and characterize two 31-kDa chitinolytic enzymes. These two enzymes (SBF1 and SBF2) were purified 70- and 81-fold with yields of 0.75 and 1.25%, respectively, and exhibited optimal pH and temperature ranges of 5.0-5.5 and 40-$50^{\circ}C$. With [$^3H$]-chitin as a substrate, $K_m$ and $V_{max}$ values of SBF1 were 4.6 mM and 220 mmol/mg-protein/h, respectively, while those of SBF2 were 7.14 mM and 287 mmol/mg-protein/h. The purified enzymes showed markedly less activity with p-nitrophenyl-N-acetylglucosaminide and fluorescent 4-methylumbelliferyl glycosides of D-N-acetylglucosamine oligomers than with [$^3H$]-chitin. End-product inhibition of both enzymes demonstrated that both are endochitinases with different N-acetylglucosaminidase activity. Furthermore, the $NH_2$-terminal sequence of SBF1 showed a high degree of homology with other plant chitinases whereas the $NH_2$-terminal amino acid of SBF2 was blocked.

• 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 $Hg^{++}$.

• Journal of Microbiology and Biotechnology
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• v.10 no.4
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• pp.462-469
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• 2000

Sixty-one strains representing the main genera of wood-decaying xylariaceous fungi (mainly in Daldinia, Hypoxylon, Kretzschmaria, Rosellinia, Penzigia, and Xylaria) were tested for their ability to produce ligninolytic enzymes. The phenol oxidase activity and fungal growth of the xylariaceous fungi on gallic aicid and tannic acid media showed a variation in their ability to degrade lignocellulose. A number of species showed equal 개 betterligninolytic enzyme activities than Coriolus versicolor, a known basidiomycete wood-degrader. A large variation of the enzyme activity was observed by individual strains as well as a substantial variation between the isolates of the same species. The most frequent ligninolytic enzymes were peroxidase and general oxidase. With 19% of the strains tested, peroxidase showed the strongest ligninolytic enzyme activity, while tyrosinase activity was detected only in 7% of the strains. All strains of Kretzschmaria and Rosellinia tested was positive for laccase. Xylariaceous fungi were able to degrade the macromolecule, lignin, using each specific ligninolytic enzyme in the specfic lignin degradation pathway.

• Journal of Microbiology and Biotechnology
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• v.9 no.4
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• pp.514-517
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• 1999

Hydrolysis of EFB (empty fruit bunch) derived from oil palm was studied using crude enzyme from Aspergillus terreus IMI 282743 along with commercial enzymes from Trichoderma reesei and Aspergillus niger. Hydrolysis at $40^{\circ}C$ and $50^{\circ}C$ with $\alpha$-cellulose or EFB gave significantly lower yield when commercial enzymes of T. reesei and A. niger were used and the hydrolysis time extended beyond 10 h. After 24 h of hydrolysis at $40^{\circ}C$ and $50^{\circ}C$, the filter paper activity (Fpase) from A. terreus retained as much activity as A. niger and it was significantly higher than T. reesei. Glucose concentration of 0.25% and 0.5% caused significant inhibition in the crude enzyme, but in regards to the commercial enzymes it only showed a slight effect. Crude enzymes from A. terreus could produce the highest reducing sugars when compared to commercial enzymes from T. reesei or A. niger. Nevertheless, low yield of sugar was observed for EFB for all treatments.

• Korean Journal of Microbiology
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• v.9 no.4
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• pp.155-162
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• 1971

A comparison of dextrinogenic amylase activities in the Asp. niger group was made with their crude and ethanol dialized enzymes before and after heating at high temperature (60-$65^{\circ}C$). The results obtained are as follows ; 1. THe dextrinogenic amylase activity of crude enzymes of Asp. kawachii and Asp. foetidus was strong, but Asp. phoernicis, Asp. carbonarius and Asp.japonicus showed weak activity. The others showed medial grades of activity. 2. The ethanol dialized enzymes of Asp. kawachii, Asp. foetidus and Asp. japonicus was very sesitive to high temperature (60 or $65^{\circ}C$) and their enzymatic activities were diminished greatly. The others did not show diminution of enzymatic activity at 60 or 65.deg.C, but diminished greatly at 70 or $75^{\circ}C$. 3. The ethanol dialized enzymes of the Asp.niger group heated to 65.deg.C was more sensitive at pH 6.0 and 6.5 than at pH 4.5, 5.0 and 5.5. 4. Tested strains in the Asp.niger group were subdivided into 4 subgroups by their dextrinogenic amylase activities before and after heating at 60 or $65^{\circ}C$. The first group showed a medial grade of activity before heating and no diminution of their enzymatic activities after heating. Asp. niger, Asp.pulverulentus, Asp. awamori and Asp. usmii were included in this group. The second group had strong enzymatic activity before heating, but diminished greatly after heating. Asp rawachii and Asp. phoenicis were included in this group. The fourth group showed very weak enzymatic activity before heating, and was inactivated easily by heating. Asp.oryzae of the Asp. flavus group showed a very strong dextrinogenic amylase activity before heating. After the heat treatment, however, its enzymatic activity was diminished greatly.

• Journal of Pharmaceutical Investigation
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• v.33 no.4
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• pp.273-279
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• 2003

Pancreatin is a enzyme mixture breaking down carbohydrates, proteins and lipids. Most pancreatin used in Korea is imported from foreign countries. However, guideline of each country for pancreatin produced from each country is different. Therefore, guideline for pancreatin imported from several countries, such as Europe, Japan and America, it is standardized to control its quality. Assay of enzyme activity for pancreatin in KP is similar to tat in JP, but it is significantly different from those in FP ad in USP. We measured pancreatin digestive activities of 17 commercial products. Activity assay of digestive enzymes, starch- and lipid-digestive enzymes, for pancreatin by KP method (including JP) was difficult compared to those by FIP ad USP methods. Particularly, activity assays of starch- and lipid-digestive enzymes by KP method were mistakable, ad varied in diluted samples than those by FIP. However, activity assay of protein-digestive enzyme by KP method was similar to that by FIP. Starch-digestive enzyme activities of 17 commercial pancreatins by KP method were lower 0.079-fold compared to those by FIP method. Their protein-digestive enzyme activities by KP method were higher 75.7-fold than those by FIP method. Their lipid-digestive enzyme activities by KP method were lower 0.234-fold compared to those by FIP method.

• Korean journal of food and cookery science
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• v.13 no.5
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• pp.623-626
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• 1997

The purpose of this study was to investigate the properties of proteolytic enzymes extracted from mulberry (Morus alba L.). The protease activity of the enzymes from mulberry was 2,358 unit/g. The enzymes showed strong activities toward hemoglobin and collagen. The optimum temperature and pH of the enzymes were 50$^{\circ}C$ and 6.0, respectively. The enzymes were stable at the temperature range of 30$^{\circ}C$ to 60$^{\circ}C$ and the pH from 5.0 to 7.0 for 1 hr at 37$^{\circ}C$ of incubation and also retained whole activity after incubation for 1 hr at 60$^{\circ}C$.