• Title/Summary/Keyword: enzyme resource

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Biotransformation of Liquiritin in Glycyrrhiza uralensis Fisch Extract into Liquiritigenin by Plant Crude Enzymes (식물 유래 조효소에 의한 감소 Liquiritin의 Liquiritigenin으로의 변환)

  • Park, Min-Ju;Na, In-Su;Min, Jin-Woo;Kim, Se-Yeong;Yang, Deok-Chun
    • Korean Journal of Medicinal Crop Science
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    • v.16 no.2
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    • pp.74-78
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    • 2008
  • Liquiritin in licorice (Glycyrrhiza uralensis Fisch) extract was treated with three different plant crude enzymes (Prunus dulcis enzyme; PDE, P. armeniaca enzyme; PAE and P. persica enzyme; PPE) for biotransformation. The resulting product of liquiritin was analyzed by TLC and HPLC. The ${\beta}glucosidase$ activities of crude enzymes were 259.6 U/g (PDE), 407.6 U/g (PAE) and 445.8 U/g (PPE), respectively. The liquiritin was converted to liquiritigenin after 12 hours of incubation with the crude enzymes. Liquiritigenin content reached its maximum level after the treatment with PPE at $37^{\circ}C$.

Effects of Dietary Bio Ethanol By-product and Complex Enzyme on Meat Quality of Pork Loin (바이오 에탄올 부산물 DDGS와 복합 효소제 첨가급여가 돈육의 품질 특성에 미치는 영향)

  • Yoo, Jong-Sang;Jang, Hae-Dong;Kim, In-Ho
    • Food Science of Animal Resources
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    • v.30 no.6
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    • pp.1007-1013
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    • 2010
  • This study was conducted to evaluate the effects of dietary complex enzyme (${\beta}$-mannanase 800 IU/kg and xylanase 700 IU/kg) in a diet containing corn distiller's dried grain with soluble (DDGS) on meat quality and pork fatty acid composition. Ninety-six pigs ([(Landrace${\times}$Yorkshire)${\times}$Duroc], with an average body weight of 68.77 kg were used in the 8 wk growth assay. Dietary treatments included 1) corn-soybean meal diet, 2) corn-soybean meal diet + 0.05% enzyme complex, 3) cornsoybean meal diet with DDGS and 4) corn-soybean meal diet with DDGS + 0.05% enzyme complex. The pigs were allotted randomly into pens (n=4 per pen) with six replicate pens per treatment by a completely randomized design. Pigs were slaughtered at the end of the experiment and the loin muscle was obtained for meat quality. Meat pH (p<0.01), firmness (p<0.01) and redness (p<0.05) were higher in DDGS-supplemented diet than in the corn-soy bean meal diet. However, color, marbling, lightness, yellowness, thiobarbituric acid reactive substances, water holing capacity, driploss, cooking loss and loin muscle area were not significantly different among the diets. The pigs fed the DGGS-supplemented diet had higher total unsaturated fatty acids (UFA) and total UFA/saturated fatty acid (SFA) ratio of loin and backfat. The results indicate that a diet containing DDGS can influence pH, firmness, redness and total UFA concentration and total UFA/SFA ratio of meat and backfat, but that enzyme addition has no affect on meat quality.

Characterization of alkaline cellulase from Bacillus subtilis 4-1 isolated from Korean traditional soybean paste (전통 장류에서 분리된 알칼리성 Cellulase 생성 Bacillus subtilis 4-1 균주의 효소학적 특성)

  • Baek, Seong Yeol;Lee, You Jung;Yun, Hye Ju;Park, Hye Young;Yeo, Soo-Hwan
    • Food Science and Preservation
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    • v.21 no.3
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    • pp.442-450
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    • 2014
  • In this study, we isolated a cellulase-producing bacterium isolated from traditional Korean fermented soybean paste and investigated the effect of culture conditions on the production of cellulase. This bacterium, which was identified as Bacillus subtilis 4-1 through 16S rRNA gene sequence analysis, showed the highest cellulase activity when the cells were grown at $45^{\circ}C$ for 24 hours in the CMC medium supplemented with 1.0% of soluble starch and 0.1% yeast extract. The initial optimum pH of the medium was observed in the range of 5.0~9.0. The optimal pH and temperature for the production of cellulase from B. subtilis 4-1 were pH 9.0 and $60^{\circ}C$ respectively. In addition, the enzyme showed significant activity in the temperature range of $20{\sim}90^{\circ}C$, which indicates that B. subtilis 4-1 cellulase is an alkaline-resistance and thermo-stable enzyme. This enzyme showed higher activity with CMC as the substrate for endo-type cellulase than avicel or pNPG as the exo-type substrates for exo-type cellulase and ${\beta}$-glucosidase. These results suggest that the cellulase produced from B. subtilis 4-1 is a complex enzyme rather than a mono-enzyme.

Effects of Enzyme Complex Supplementation on Growth Performance, Nutrient Digestibility, Blood Profiles and Economic Feed Cost in Growing Pigs (복합효소제의 첨가가 육성돈의 생산성, 영양소 소화율, 혈액성상 및 사료비용에 미치는 영향)

  • Hong, Seong-Min;Jang, Hae-Dong;Kim, Hyo-Jin;Yoo, Jong-Sang;Lee, Je-Hyun;Kim, In-Ho
    • Journal of Animal Science and Technology
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    • v.53 no.2
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    • pp.113-118
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    • 2011
  • This study was conducted to evaluate effects of enzyme complex on growth performance, nutrient digestibility, blood profiles and feed cost in growing pigs. Ninety-six pigs [(Landrace ${\times}$ Yorkshire) ${\times}$ Duroc, $22.96{\pm}0.79$ kg average initial body weight] were used in 42d growth assay. Dietary treatments included:1) HC (high energy and nutrient density diet), 2) CON (control, basal diet), 3) CE1 (CON + 0.05% enzyme complex) and 4) CE2 (CON + 0.1% enzyme complex). Four pigs were allotted per pen with six replicate pens per treatment by completely randomized design. The ADG was higher in CE1 and CE2 treatments than CON treatment (P<0.05). The ADFI was linearly increased by CE treatments compared to HC treatment. The CE1 treatment had highest DM, N and GE digestibility (P<0.05). Digestibility of DM, N and GE were quadratic enhanced by enzyme complex level. No differences were found among treatments for creatinine and BUN. The enzyme complex treatments (CE1 and CE2) showed lower feed cost/body weight gain than HC treatment. In conclusion, enzyme complex can improve ADG and reduce feed cost/body weight gain when low energy diet was used. Furthermore adding 0.05% enzyme complex had highest nutrient digestibility.

The Isolation and Culture Characterization of a Lipolytic Enzyme Producing Strain from Meju (메주로부터 지질분해 효소 생산 균주의 분리 및 배양학적 특성)

  • Yun, Hye-Ju;Lee, You-Jung;Yeo, Soo-Hwan;Choi, Hye-Sun;Park, Hye-Young;Park, Heui-Dong;Baek, Seong-Yeol
    • Microbiology and Biotechnology Letters
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    • v.40 no.2
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    • pp.98-103
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    • 2012
  • For screening of useful enzymes producing microorganisms from Meju, we isolated high lipase producing strains and their lipolytic enzyme activities were then tested. The lipolytic enzyme activities of isolated microorganisms were therefore tested on the Y124 strain. The gene sequence analysis of ITS from Y124 strain revealed Yarrowia lipolytica. Lipase production by the Y124 strain was studied in media containing various carbon sources. The Y124 strain drastically increased lipolytic enzyme activity in YPO media containing olive oil, as well as in YPDO media containing both olive oil and glucose. Maximal lipase production was achieved in YPD (yeast extract-peptone-D-glucose) media containing 0.7% olive oil when cultured at $30^{\circ}C$ for 8 hrs. The lipase produced from the Y124 strain showed the highest activity in p-NPO (p-nitrophenyl octanoate ($C_8$)), amongst the various p-nitrophenyl esters.

Isolation and Optimized Culture Conditions of Fibrinolytic Enzyme Producing Strain Isolated from Korean Traditional Soybean Sauce (간장 유래 혈전분해 효소 생산 균주의 분리 및 배양학적 특성)

  • Baek, Seong-Yeol;Yun, Hye-Ju;Park, Heui-Dong;Yeo, Soo-Hwan
    • Microbiology and Biotechnology Letters
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    • v.39 no.4
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    • pp.330-336
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    • 2011
  • Bacterial strains exhibiting fibrinolytic activity were screened from traditional Korean soybean sauce. The Fibrinolytic activities of the various isolated microorganism were further examined and the superior strain YJ11-21 was selected for further analyses. Gene sequence analysis of 16S rDNA of the YJ11-21 strain revealed Bacillus licheniformis. Optimal culture conditions were investigated in order to maximize the production of the fibrinolytic enzyme by YJ11-21. Amongst the carbon sources tested, glucose was the most effective for enzyme production and amongst the nitrogen sources tested, yeast extract was seen to be the most effective. A one percent addition of NaCl to the medium resulted in the highest fibrinolytic activity. Interestingly, a 10% addition of NaCl resulted in a high activity together with a high cell growth rate. Therefore, YJ11-21 is speculated of being a halotolerant. The optimum pH and temperature for enzyme production were a pH of 9.0 and $30^{\circ}C$, respectively.

Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Recombinant E. coli (재조합 대장균으로부터 항고혈압 Angiotensin I-Converting Enzyme 저해제의 특성연구)

  • Kim, Jae-Ho;Jeong, Seung-Chan;Lee, Dae-Hyong;Lee, Jong-Soo
    • The Journal of Natural Sciences
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    • v.16 no.1
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    • pp.1-13
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    • 2005
  • The angiotensin I-converting enzyme (ACE) inhibitor has anti-hypertensive effects and has long been used as prevention or remedy of hypertension. This study were carried out to produce and purify a new ACE inhibitor from recombinant E. coli and further elucidate its structure-function relationship. Recombinant pGEX-4T-3 containing ACE inhibitory peptide gene of Saccharomyces cerevisiae was transformed into E. coli BL21(DE3). Glutathione-S transferase (GST) fusion protein from E. Coli BL21(DE3) harboring the recombination pGEX-4T-3 was obtained and the ACE inhibitory peptide was purified with Sephadex G-25 column chromatography. The purified ACE inhibitory peptide was a novel decapeptide with sequence Tyr-Asp-Gly-Gly-Val-Phe -Arg-Val-Tyr-Thr which shows very low similarity to the other ACE inhibitory peptide sequence. The purified ACE inhibitor competitively inhibited ACE.

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Transformation of Ginsenoside Rd to Ginsenoside F2 by Enzymes of Leuconostoc fallax LH3 (Leuconostoc fallax LH3이 생산하는 효소에 의한 Ginsenoside Rd의 Ginsenoside F2로의 전환)

  • Quan, Lin-Hu;Cheng, Le-Qin;Na, Ju-Ryun;Kim, Ho-Bin;Park, Min-Ju;Kim, Se-Hwa;Kim, Myung-Kyum;Yang, Deok-Chun
    • Korean Journal of Medicinal Crop Science
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    • v.16 no.3
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    • pp.155-160
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    • 2008
  • Ginsenosides have been regarded as the principal components, responsible for the pharmacological and biological activities of ginseng. Absorption of major ginsenosides at the gastrointestinal tract was extremely low, when ginseng taken orally. In order to improve the absorption and bioavailability, transformation of major ginsenosides into more active and valuable minor ginsenoside is much required. In this present study, We isolated a lactic acid bacteria Leuconostoc fallax LH3 from the Korean fermented food Kimchi, which have higher ${\beta}$-glucosidase activity. Using the ethanol precipitated curd enzyme of Leuconostoc fallax LH3, we investigated the biotransformation of ginsenoside Rd at different experimental condition to increase transformation. The maximum convertion was supported at 30 $^{\circ}C$ and decreased when temperatures increased. In order to optimize the effect of pH, the curd enzyme was mixed 20 mM sodium phosphate buffer (pH 3.5 to pH 8.0). Ginsenoside Rd was almost hydrolyzed between pH 7.0 and pH 9.0, but not hydrolyzed above pH 10.0. Ginsenoside Rd was hydrolyzed after 24 hrs incubation, but whereas the ginsenoside F2 was appeared from 36 hrs, and all ginsenoside Rd was transformed to F2 after the 60 hrs incubation. Based on this study, the curd enzyme of Leuconostoc fallax LH3 transformed the ginsenoside Rd at the 30$^{\circ}C$ and the pH optimum of 7.0 to 9.0 after the 60 hrs incubation time.