• Title/Summary/Keyword: 활성시간

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Preparation of activated carbon from waste tire char (폐타이어 열분해 잔류물로부터 활성탄 제조)

  • Kim, Jin-Uk;Lim, Ki-Hyuk;Shon, Byung-Hyun
    • Proceedings of the KAIS Fall Conference
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    • 2011.12a
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    • pp.266-268
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    • 2011
  • 본 논문은 폐타이어 열분해 잔류물인 char를 이용하여 수증기 활성화법으로 활성탄을 제조하였다. 활성화 온도가 증가할수록 비표면적은 증가하였으나 활성화 시간에 따른 비표면적은 3시간에서 최대를 보인 후 시간이 지속되면 비표면적은 감소하였다. 본 연구결과, 타이어열분해 잔류물 char를 이용한 활성탄 제조에 있어 최적의 실험조건은 활성화 온도 $850^{\circ}C$, 활성화 시간 3시간, 승온속도 $5^{\circ}C/min$이었으며 이 조건에서 제조한 활성탄의 비표면적은 $517.6m^2/g$으로 나타났다.

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Analysis of the Coagulation Factors of Donated Plasma for Effective Utilization (헌혈혈장의 효율적 활용을 위한 혈액응고인자 활성도 분석)

  • Jee, Yong-Hun;Kim, Myung-Han;Kwon, So-Yong;Cho, Nam-Sun;Cho, Youn-Jung;Choi, Kyoung-Young
    • The Korean Journal of Blood Transfusion
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    • v.23 no.2
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    • pp.145-151
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    • 2012
  • 배경: 채혈 후 제제 경과시간에 따른 동결혈장의 혈액응고인자의 활성도와 이에 영향을 미치는 요인을 분석하여, 혈액응고인자제제의 원료혈장의 사용범위를 확장 가능한지 확인하고자 동결혈장의 채혈시간과 응고인자 특성을 측정하였다. 방법: ALT 부적격 혈장을 채혈 후 동결시간의 특성에 따라 4단계로 구분하였고, 6종류의 혈액 응고인자 활성도와 혈액형을 검사하였고, SAS 9.2 프로그램을 사용하여 통계처리 하였다. 결과: 혈액제제간 FVIII 활성도를 분석한 결과 PL-A>FFP>FP(8-24)${\approx}$FP(24-72) 순으로 유의하게 낮아졌고 혈액형에 따라서는 AB형이 제일 높고, O형이 제일 낮았다. 대한적십자사의 원료혈장에 대한 FVIII 활성 품질기준을 적용할 경우 PL-A, FFP와 FP24는 각각 85.0%와 82.5%로 적합하였다. 캐나다 퀘백 주처럼 FP24의 FVIII 활성이 0.52 IU/mL 이상을 적용할 경우 PL-A, FFP와 FP24는 각각 95.0%, 96.3%, 82.6%로 적합하였다. 또한 FP(8-24)의 A형과 AB형, FP(24-72)의 경우 AB형이 각각 82.1%, 83.3%, 100%로 적합하였다. 결론: 혈액응고인자제제용 원료혈장의 범위는 외국의 기준에 비추어 채혈 후 24시간 내에 동결된 혈장(FP24)으로 확대 사용이 가능하다. 이를 위해서는 채혈 후 동결시간과 혈액응고인자에 대한 품질기준을 유럽약전 또는 WHO 가이드라인과 비교하여 완화하는 것이 필요하다.

Production Condition of Alkaline Pretense by V. parahaemolyticus ATCC 17802(II) (V. parahaemolyticus ATCC 17802에 의한 Alkaline Pretense 생산조건(II))

  • 양지영;양지영;강현록;황미경;이재우;차재호
    • Journal of Food Hygiene and Safety
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    • v.16 no.1
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    • pp.33-36
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    • 2001
  • V. parahaemolyticus possessed an extracellular alkaline protease activity during the stationary growth phase. Various factors such as initial pH of medium, incubation temperature and shaking rate were investigated far optimizing the production of alkaline protease from V. parahaemolyticus ATCC 17802. Maximal activity of the protease was obtained when the bacteria were grown in 2% skim milk medium in 0.1M tris/HCl buffer (pH 7.6). Maximal activity of the protease was obtained when the bacteria were growls at initial pH of 7.6, incubation temperature 37$^{\circ}C$ and shaking rate of 250 rpm.

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Manufacturing Method for Traditional Doenjang and Screening of High Fibrin Clotting Inhibitory Samples (전통된장의 제조방법 조사 및 혈액응고 저해활성이 높은 된장의 스크리닝)

  • Jang, In-Hwan;In, Man-Jin;Chae, Hee-Jeong
    • Applied Biological Chemistry
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    • v.47 no.1
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    • pp.149-153
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    • 2004
  • 전통된장 제조방법으로서 원료 혼합비, 메주의 건조시간 및 온도, 메주와 된장의 발효 시간 및 온도, 된장 간장의 분리 여부, 된장 숙성(aging) 시간을 조사하였다. 혈액응고 저해 활성(anticoagulant activity)을 fibrin clotting assay법으로 분석하여 혈액응고 저해활성과 제법간의 상관 관계를 검토하였다. 숙성 기간이 길수록 혈액응고 저해활성이 높게 나타나는 경향을 보였으나 선형적인 상관관계보다는 비선형적으로 양의 상관관계를 갖는 것으로 판단되었다. 이상의 결과를 토대로 혈액응고 저해활성이 높은 2종의 된장시료를 선발하였으며 숙성기간이 180일 이상일 경우 전통된장의 혈액응고 저해활성이 높은 것으로 판단되었다.

Changes in cultural characteristics and biological activities of amaranth during fermentation (발효시간에 따른 아마란스 발효물의 배양특성 및 생리활성)

  • Lee, Rea-Hyun;Yang, Su-Jin;Hong, Joo-Heon
    • Food Science and Preservation
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    • v.23 no.4
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    • pp.568-575
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    • 2016
  • Bacillus amyloliquefaciens CGD3 was used as a starter for fermentation of amaranth and cultural characteristics and biological activities of amaranth were investigated. The viable cells in fermented amaranth was 4.54~8.01 log CFU/mL during 96 hr of fermentation period. Protease activities of amaranth showed the highest by 36.7 unit/mL after 72 hr of fermentation. The total phenolic and flavonoid contents of amaranth increased with fermentation time while its total sugar content decreased. The total protein content was the highest in amaranth fermented for 96 hr (0.25 mg/g). The DPPH scavenging activities, FRAP (ferric reducing antioxidant power), and reducing power of amaranth were highest in amaranth fermented for 72 hr, showing 84.46%, $551.91{\mu}M$, and 2.74, respectively. ACE (angiotensin converting enzyme) and ${\alpha}$-Glucosidase inhibition rates increased with fermentation time and showed the highest after 72 hr.

Evaluation of Radical Scavenging and α-Glucosidase Inhibitory Effects of Gallic Acid Reactants Using Polyphenol Oxidase (폴리페놀산화효소를 활용한 Gallic Acid 반응물의 라디칼 소거 및 α-Glucosidase 저해 활성 평가)

  • Jeong, Yun Hee;Kim, Tae Hoon
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.45 no.9
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    • pp.1385-1390
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    • 2016
  • Gallic acid is a representative hydroxybenzoic acid and is found in free form in several plants and in various esterified forms as a part of hydolyzable tannins. Convenient enzymatic transformation of trihydroxylated gallic acid with polyphenol oxidase originating from pear was evaluated to investigate whether polyphenol oxidase can be used as a valuable compound to improve the biological activity of gallic acid. Enzymatic oxidation processing of gallic acid using polyphenol oxidase was carried out for five different reaction times. The antioxidant effects of transformed gallic acid for different reaction times were evaluated via radical scavenging assays using 1,1-diphenyl-2-picrylhydrazyl and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radicals. In addition, the anti-diabetic property of the transformed gallic acid was measured based on ${\alpha}$-glucosidase. Gallic acid reacted for 5 h showed significantly higher antioxidant and ${\alpha}$-glucosidase inhibitory activities compared to the tested positive control substances. Biotransformation of simple gallic acid induced by polyphenol oxidase might be responsible for enhancing the biological activity of gallic acid.

한우에서 추출한 Myosin B의 Pepsin 가수분해물의 Ultrafilteration에 의한 Angiotensin Converting Enzyme(ACE) 저해 활성 분석

  • Kim, Yeong-Ju;Choe, Dam-Mi;Jin, Gu-Bok
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.10a
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    • pp.168-171
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    • 2005
  • 한우의 Myosin B 단백질을 단백질 가수분해 효소인 pepsin으로 처리한 다음 단백질의 함량과 혈압상승 펩티드 생성효소인 angiotensin-I converting enzyme(ACE)에 대한 저해활성을 측정하였다. 등심이 우둔에 비해 단백질의 함량이 높았으며, 가수분해 처리 후 우둔과 다르게 등심은 3시간 가수분해 처리구에서 단백질의 함량이 높게 나타났다. ACE 저해활성은 등심에서는 3시간, 우둔에서는 6시간동안 가수분해시켰을 때 ACE 저해율이 유의적으로 가장 높게 나타났으며, 3, 6시간동안 가수분해시켰을 경우 부위 별로 유의적인 차가 있었으나(p<0.05), 0, 1시간동안 가수분해 시켰을 때는 부위간의 유의적인 차는 없었다(p>0.05). ACE 저해율이 가장 좋은 가수분해 처리구를 ultrafiltration시킨 결과, 저분자 peptide 상태의 가수분해물이 고분자에 비하여 ACE 저해율이 높은 것으로 나타났다. 차후 ACE 억제활성도가 높은 단백질을 분리하여 가장 우수한 분획을 찾아 아미노산 염기서열을 밝혀 고혈압 억제제로 합성 개발하는 연구를 추진할 예정이다.

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Effects of Condiments upon Enzyme Activity (1) - Effects of Condiments upon Proteinase Activity of Pancreatin - (식품첨가물(食品添加物)이 소화효소(消化酵素)의 활성(活性)에 미치는 영향(影響)(1) - 식품첨가물(食品添加物)이 Pancreatin의 Proteinase Activity에 미치는 영향(影響) -)

  • Suh, Myung-Jah
    • Journal of Nutrition and Health
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    • v.6 no.4
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    • pp.55-60
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    • 1973
  • To determine the effects of condiments upon Proteinase Activity, condiments such as welsh onion, garlic, ginger, black pepper, red pepper, mi-won (glutamic acid natrium), sugar, mustard and horse-radish were ground by a homogenizer, and each of them was dosed by 0%, 1%, 5% and 10% into Pancreatin Solution of 0.2% for storage at the temperature of 15 degrees Cels. The Enzyme Solution thus obtained then was measured at a certain interval of time by the Fuld Gross Method, and the following results were obtained. 1) The condiments that kept Proteinase Action of Pancreatin checked below 75% were mustard, horse-radish, red pepper and welsh onion. The centrol power of welsh onion, in particular, became stronger as storage time became longer. 2) The condiments that kept Proteinase Action of Pancreatin checked below 50% were sugar, black pepper and ginger. 3) Mi-won and garlic showed a strong checking powor over Proteinase Action at an early stage of storage, but as time passed, their control power gradually diminished to naught. In short, it may be concluded that ail of the condiments used in this experiment demonstrated their checking power over Proteinase Action.

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Increased Alcohol Decomposition Efficacy of Hoveina dulcis Extract by Carbohydrate-Hydrolyzing Enzymes (당 분해 효소를 이용한 헛개나무 열매 추출물이 알코올 분해에 미치는 영향)

  • Lee, Kyung-Seok;Kim, Ae-Jung;Lee, Ki-Young
    • Journal of the East Asian Society of Dietary Life
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    • v.22 no.4
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    • pp.473-479
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    • 2012
  • In this study, increased alcohol decomposition efficacy (ADH) of Hoveina dulcis extract by Carbohydrate-Hydrolyzing Enzymes was investigated. Carbohydrate decomposition enzymes such as Maxinvert (Invertase), Optidex L-400 (Glucoamylase) and Rohament CL (Cellulase & Pectinase) were added to Hoveina dulcis extract at different concentrations (0.01, 0.05, 0.1, 0.5 and 1%) for 48 hrs, after which samples were taken every 6 hrs for determination of ADH activity. As the enzyme concentration became higher, ADH activity also increased. Especially, the addition of 1% Rohament CL increased enzyme activity to 76% at 30 hrs incubation, after which the increase in activity stopped. In the rat and human body experiment, enzymatic decomposition of Hovenia dulcis extract by addition of 1% Rohament CL was also effective in decreasing serum alcohol concentration and respiration. Especially, in the early stage after alcohol consumption, the efficacy of enzyme treatment of Hovenia dulcis extract was more effective. These results show that if the glycoside forms of active compounds such as flavonols in Hovenia dulcis extract are converted into aglycone forms, alcohol decomposition capability can be enhanced.

Characterization of Bacteriocin-Like Substances Produced by Bacillus subtilis MJP1 (Bacillus subtilis MJP1이 생산하는 Bacteriocin-Like Substances)

  • Yang, Eun-Ju;Chang, Hae-Choon
    • Microbiology and Biotechnology Letters
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    • v.35 no.4
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    • pp.339-346
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    • 2007
  • The MJP1 bacterial strain, which possesses antifungal activity, was isolated from meju and identified as Bacillus subtilis based on its morphological and biochemical properties, as well as its 16S rRNA sequence. Antimicrobial activity was found against various species of Gram-positive bacteria, yeasts, and molds, including food-spoilage microorganisms. The antifungal activity was found to be stable after heat and proteolytic enzyme treatment, and in the pH range of $6.0{\sim}10.0$. The antibacterial activity was stable in the pH range of $6.0{\sim}10.0$, but about 50% of the activity was lost after 24 hr at $30^{\circ}C$. The antibacterial compound was also inactivated by proteolytic enzyme treatment, indicating its proteinaceous nature. The apparent molecular masses of the partially purified antifungal and antibacterial compounds, as indicated by using the direct detection method in Tricine-SDS-PAGE, were approximately 2.4 kDa and 4.5 kDa, respectively. These studies suggest that B. subtilis MJP1 produces two bacteriocin-like substances with antifungal and antibacterial activities.