• Title/Summary/Keyword: alkali-heat treatment

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Reviews on an Improvement and Measurement of the Hydrophobicity for Carbon Materials (탄소재료의 소수성 향상 방법 및 측정 방법에 대한 고찰)

  • Kang, Yu-Jin;Kim, Yu-Jin;Jang, Min-Hyeok;Jo, Hyung-Kun;Yoon, Seong-Jin;Han, Gyoung-Jae;Cho, Hye-Ryeong;Seo, Dong-Jin;Park, Joo-Il
    • Journal of the Korea Organic Resources Recycling Association
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    • v.30 no.4
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    • pp.41-50
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    • 2022
  • Recently, research on carbon adsorbents has been active as an interest in improving the environment such as indoor and outdoor air quality. Considering that causative substances deteriorate the air quality are basically volatile organic compounds, it is important to improve the hydrophobicity of the carbon materials for better removal efficiency. This study presents a method for improving hydrophobicity of carbon and a measurement of the hydrophobicity. Generally, methods of improving the hydrophobicity of carbon materials are heat treatment, acid/alkali treatment, coating and immersion with hydrophobic materials. However, it collapses the pore structure and reduces the adsorption capacity. Therefore, this study briefly introduce not only the general method for improving carbon materials' hydrophobicity but also the method for converting the precursor of the material is briefly introduced. Futhermore, this study introduces a analytical technique used to determine hydrophobic modification or not, and aims to enhance the understanding of carbon materials.

Electrical Properties of YMnO3 Thin Film by Sol-gel Process (졸-겔 공정에 의한 YMnO3 박막의 전기적 특성)

  • Kim, Eung-Soo;Kim, Beng-Gu;Kim, Yoo-Taek
    • Journal of the Korean Ceramic Society
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    • v.39 no.5
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    • pp.511-516
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    • 2002
  • Hexagonal $YMnO_3$ thin films were prepared from $Y(NO_3)_3{\cdot}5H_2O$ and $Mn(CH_3CO_2)_2{\cdot}4H_2O$ as starting materials on the Si(100) substrates by the sol-gel method. The crystal structure and the electrical properties of the $YMnO_3$ thin films were investigated as a function of heat treatment temperature, the amount of water(Rw) of hydrolysis and the addition of catalysis. The crystallization of the $YMnO_3$ thin film began at 700${\circ}C$ and completed at 800${\circ}C$ for 1 h. The c-axis (0001) preferred orientation of hexagonal $YMnO_3$ was detected for the $YMnO_3$ thin films with Rw=6 and that was decreased for the $YMnO_3$ thin films with Rw=1 and Rw=12. The crystallinity and preferred orientation of the $YMnO_3$ thin films were depended on the addition of acid and/or alkali catalysis, which, in turn, the preferred orientation of c-axis was decreased and the orthorhombic phase of $YMnO_3$ was detected to the specimens with the addition of catalysis. The $YMnO_3$ thin film with Rw=6 showed good leakage current density of $1.2{\times}10-8 A/cm^2$ at the applied voltage of 0.2V and the leakage current density was not changed drastically with applied voltage.

Inhibitory Substance Produced by Aspergillus sp. on the Snake Venom Proteinase - Isolation of Microorganism and Biological Activities of the Inhibitor - (Aspergillus 속 균주가 생성되는 사독 Proteinase에 대한 저해물질 - 균의 분리 및 저해물질의 생물학적 작용상 -)

  • Hyun, Nam-Joo;Seu, Jung-Hwn
    • Microbiology and Biotechnology Letters
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    • v.15 no.2
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    • pp.129-134
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    • 1987
  • Aspergillus sp. (MK-24) producing a biological active substance that inhibited the venom proteinase activity was isolated from soil. The substance also inhibited the activity of trypsin and coagulation of blood, but did not inhibit papain, $\alpha$-chymotrypsin and pepsin. The substance was partially purified from culture filtrate by precipitaion with acetone, and by chromatography of DEAE-Sepadex A-50 column and Amberlite IRC-50 ion exchange. The inhibitory substance was stable in the wide pH range from 2.0 to 12.0 at 37$^{\circ}C$, but not stable at $65^{\circ}C$ in the alkaline pH. Only 12% of the activity was decreased by the heat treatment at 10$0^{\circ}C$ for two hours. The inhibition on venom proteinase (Agkistrodon bromohoffi brevicaudus) was a mixed type. The inhibitory activity depended on the preincubation time and completely depressed by cupric, zinc and cobalt ions. The inhibition on the venom proteinase was appeared strongly on casein but not on ovalbumin or hemoglobin as a substrate.

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Antimicrobial Activity of Korean Wild Tea Extract According to the Degree of Fermentation (발효정도에 따른 국내산 야생차 추출물의 항균활성)

  • Choi, Ok-Ja;Rhee, Haeng-Jae;Choi, Kyeong-Hee
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.34 no.2
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    • pp.148-157
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    • 2005
  • This study was investigated to determine antimicrobial activity of the water and ethanol extracts of Korean wild green tea, semi-fermented tea, and fermented tea. Antimicrobial activity was examined against 8 kinds of several microorganisms. The minimum inhibitory concentration (MIC) of the water and ethanol extracts of green tea showed the most active antimicrobial activity against B. subtilis 0.2 mg/mL in Gram positive bacteria and P. fluorescens 0.3∼0.5 mg/mL in Gram negative bacteria. But the extracts did not show antimicrobial activity against lactic acid bacteria and yeast at the level of less than 1 mg/mL. Antimicrobial activity got lower as tea got more fermented. Antimicrobial activity of ethanol extracts from green tea, semifermented tea, and fermented tea was stronger than that of water extracts. Antimicrobial activity of the water and ethanol extracts of green tea, semi-fermented tea, and fermented tea was not destroyed at 50∼121$^{\circ}C$, and pH 3∼11, which proved to be very stable when given over heat, acid & alkali treatment. The ethanol extract of green tea, semi-fermented tea, and fermented tea was fractionated in the order of hexane, diethyl ether, ethyl acetate and water fraction. The highest antimicrobial activity was found in the water fraction, but not found in hexane fraction, while antimicrobial activity of fermented tea was not found in ether fraction.

Functional Properties of Soy Protein Isolates Prepared from Defatted Soybean Meal (탈지대두박(脫脂大豆粕)에서 추출(抽出)한 분리대두단백(分離大豆蛋白)의 식품학적(食品學的) 성질(性質))

  • Byun, Si-Myung;Kim, Chul-Jin
    • Korean Journal of Food Science and Technology
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    • v.9 no.2
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    • pp.123-130
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    • 1977
  • A laboratory study was made to develop a simple and economic model method for the systematic determination of functional properties of 'Soy Protein Isolates (SPI)' prepared from defatted soybean meal. These are required to evaluate and to predict how SPI may behave in specific systems and such proteins can be used to simulate or replace conventional proteins. Data concerning the effects of pH, salt concentration, temperature, and protein concentration on the functional properties which include solubility, heat denaturation, gel forming capacity, emulsifying capacity, and foaming capacity are presented. The results are as follows: 1) The yield of SPI from defatted soybean meal increased to 83.9 % as the soybean meal was extracted with 0.02 N NaOH. 2) The suitable viscocity of a dope solution for spinning fiber was found to be 60 Poises by using syringe needle (0.3 mm) with 15 % SPI in 0.6 % NaOH. 3) Heat caused thickening and gelation in concentration of 8 % with a temperature threshold of $70^{\circ}C$. At $8{\sim}12\;%$ protein concentration, gel was formed within $10{\sim}30\;min$ at $70{\sim}100\;^{\circ}C$. It was, however, disrupted rapidly at $125\;^{\circ}C$ of overheat treatment. The gel was firm, resilient and self-supporting at protein concentration of 14 % and less susceptible to disruption of overheating. 4) The emulsifying capacity (EC) of SPI was correlated positively to the solubility of protein at ${\mu}=0$. At pH of the isoelectric point of SPI (pH 4.6), EC increased as concentration of sodium chloride increased. Using model system$(mixing\;speed:\;12,000\;r.p.m.,\;oil\;addition\;rate:\;0.9\;ml/sec,\;and\;temperature\;:\;20{\pm}1\;^{\circ}C)$, the maximum EC of SPI was found to be 47.2 ml of oil/100 mg protein, at the condition of pH 8.7 and ${\mu}=0.6$. The milk casein had greater EC than SPI at lower ionic strength while the EC of SPI was the same as milk casein at higher ionic strength. 5) The shaking test was used in determining the foam-ability of proteins. Progressively increasing SPI concentration up to 5 % indicated that the maximum protein concentration for foaming capacity was 2 %. Sucrose reduced foam expansion slightly but enhanced foam stability. The results of comparing milk casein and egg albumin were that foaming properties of SPI were the same as egg albumin, and better than milk casein, particularly in foam stability.

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