• Title/Summary/Keyword: 가수분해 침전

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Titanium Dioxide Recovery from Soda-roasted Spent SCR Catalysts through Sulphuric Acid Leaching and Hydrolysis Precipitation (소다배소 처리된 탈질 폐촉매로부터 황산침출과 가수분해 침전반응에 의한 TiO2의 회수)

  • Kim, Seunghyun;Trinh, Ha Bich;Lee, Jaeryeong
    • Resources Recycling
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    • v.29 no.5
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    • pp.48-54
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    • 2020
  • Sulphuric acid (H2SO4) leaching and hydrolysis were experimented for the recovery of titanum dioxide (TiO2) from the water-leached residue followed by soda-roasting spent SCR catalysts. Sulphuric acid leaching of Ti was carried out with leachate concentration (4~8 M) and the others were fixed (temp.: 70 ℃, leaching time: 3 hrs, slurry density: 100 g/L, stirring speed: 500 rpm). For recovering of Ti from the leaching solution, hydrolysis precipitation was conducted at 100 ℃ for 2 hours in various mixing ratio (leached solution:distilled water) of 1:9 to 5:5. The maximum leachability was reached to 95.2 % in 6 M H2SO4 leachate. on the other hand, the leachability of Si decreased dramatically 91.7 to 3.0 % with an increase of H2SO4 concentration. Hydrolysis precipitation of Ti was proceeded with leaching solution of 8 M H2SO4 with the lowest content of Si. The yield of precipitation increased proportionally with a dilution ratio of leaching solution. Moreover, it increased generally by adding 0.2 g TiO2 as a precipitation seed to the diluted leaching solution. Ultimately, 99.8 % of TiO2 can be recovered with the purity of 99.46 % from the 1:9 diluted solution.

Enzymatic Modification of Sardine Protein Concentrate (정어리 분말(粉末) 단백질(蛋白質)의 효소적(酵素的) 수식(修飾))

  • Kim, Se-Kwon;Lee, Eung-Ho
    • Applied Biological Chemistry
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    • v.30 no.3
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    • pp.234-241
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    • 1987
  • Conditions necessary for optimal plastein productivity from sardine protein hydrolysate using papain and pepsin were established. Sardine protein concentrate was hydrolyzed with pepsin yielding an approximate degree of hydrolysis of 77.2%. Enzyme induced plastein was optimized at: pH 6 for papain and pH 4 for pepsin; substrate concentrate, 50%(w/v) for papain and 40%(w/v) for pepsin; time of incubation, 24hr; enzyme/substrate ratio, 1 : 100(w/w). Plastein yields of 49.5% and 45.3% were found for papain and pepsin, respectively, when 10% trichloroacetic acid (TCA) was used as the precipitating agent. However, when plastein was precipitated by 50% ethanol, the yield was found to be 43.6% and 41.0% for papain and pepsin, respectively. Ethanol-precipitated plastein did not contain lipid and contained approximately 1.3% ash and 91.0% protein. In comparison, the TCA-precipitated plastein contained 74.2% protein, 0.5% lipid and 15.3% ash.

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Solubility Studies of Uranyl Hydrolysis Precipitates (우라닐 가수분해물의 용해도 연구)

  • Park, Yong-Joon;Pyo, Hyung-Ryul;Kim, Won-Ho;Chun, Kwan-Sik
    • Journal of the Korean Chemical Society
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    • v.40 no.9
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    • pp.599-606
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    • 1996
  • The effects of chemical species in groundwater on the solubility of the uranyl hydrolysis precipitates formed at pH 6.4 and 9.7 were investigated. Based on the chemical composition of the groundwater, the synthetic groundwater was prepared. The colloid-free (separated) groundwater was also prepared by removal of both organic and inorganic colloids from the sampled groundwater. Solubilities of precipitates formed in the hydrolysis of uranyl ion in groundwater, separated groundwater, synthetic groundwater and 0.1 M NaCl solution were measured over neutral to alkaline pH range, and especially, the effect of the anions and cations found in groundwater on the solubility was investigated. Solubility in groundwater was approximately two orders of magnitude greater than that in 0.1 M NaCl solution. Soubililties of uranyl hydrolysis precipitates formed at pH 9.7 and 6.4 were compared in groundwater and synthetic groundwater. Solubilities of the precipitates formed at different pH were found to be in the same order of magnitude in groundwater and synthetic groundwater, however the uranyl hydolysis precipitates formed at higher pH values showed a tendency of higher solubility.

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Immobilization Study of Inorganic Priority Pollutants in Soil with Amino Acids from Hydrolyzed Waste (재활용 아미노산을 이용한 토양 중의 무기 Priority Pollutants의 안정화 연구)

  • Bang, Jeong Hwan;Kim, Nam Jeong;Moon, Byoung Seok
    • Journal of Korean Society of societal Security
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    • v.4 no.2
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    • pp.49-56
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    • 2011
  • The hydroxide precipitation method is appropriate to distinguish free metal ions with complexed metal ions with amino acids. Optimum pH conditions of hydroxide precipitation were investigated using mixed amino acids which have similar composition ratio with hydrolyzed amino acids. When applied to soil samples immobilities of Hg, Cr, and Cu ion with mixed and hydrolyzed amino acids were reasonable. But those of Cd and Zn were not sufficient.

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미생물 효소처리로 얻은 대두 펩타이드의 기능성

  • Park, Yang-Won
    • 한국생물공학회:학술대회논문집
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    • 2000.11a
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    • pp.447-450
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    • 2000
  • Microorganism, including some bacteria isolated from soil, were found to secrete an extracellular soymilk-clotting enzyme. Using this bacterial enzyme experiments were carried out to optimize the hydrolyzing conditions for the production of soy peptides. The soy peptides produced by hydrolyzing 11S globulin with enzyme treatment at $65^{\circ}C$, pH 6.1, for 1hr were found to have a accessible possibility. The obtained coagulum by enzymatic reaction was very flocculation with fine structural formation. Properties of peptide Y and W of the enzyme hydrolysates at pH 6.1 were superior to that of isoelectric precipitation because these peptides were miscible with water in all proportions.

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Preparation of Soluble Silk Peptides by Food-grade Proteinases (효소 분해에 의한 가용성 실크 펩타이드의 제조)

  • Ha Jae-Seok;Song Jae-Jun;Cho Hyoung-Kwon;Lee Seung-Goo
    • Microbiology and Biotechnology Letters
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    • v.34 no.2
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    • pp.115-120
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    • 2006
  • Enzymatic hydrolysis of silk fibers were investigated for the preparation of soluble silk peptides by ten food-grade proteases from Bacillus, Aspergilius, and plant sources. Silk fibers were dissolved for 1 hr in a 2:1 cosolvent (50% $CaCl_2$: ethanol) by heating at $90^{\circ}C$. The silk solution was filtered to remove Impurity particles and desalted for 50 hours by a dialysis process to remove the used cosolvent. When the silk hydrolysis was performed at $45^{\circ}C$ for 2 hours, most proteases from Bacillus and Aspergillus generated large amounts of insoluble aggregates. On the contrary, proteases from plant sources produced much less aggregates during prolonged incubations and also exhibited high hydrolysis activities. In regards of the solubility and broad molecular sizes of produced silk peptides, Bromelain was finally selected and applied for the enzymatic hydrolysis of silk fibers.

Study on Proteolysis of Glucagon .3-Interleukin-2 {G.3-IL-2} Using Enterokinase (Enterokinase에 의한 Glucagon.3-Interleukin-2 {G.3-IL-2} 의 단백질 분해 연구)

  • 이운영;이지원;김인호
    • KSBB Journal
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    • v.15 no.3
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    • pp.238-242
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    • 2000
  • A fusion protein of human interleukin-2(hiL-2) and glucagon which was expressed in Escherichia coli. was digested with enterokinase for recovery of hIL-2 from the fused protein. To obtain hIL-2 of optimum recovery hydrolysis reaction were performed under various conditions of urea additives and reaction time. hIL-2 was finally purified by RP-HPLC(reversed phase-HPLC) to remove cleaved G3 fusion partner and residual uncleaved G3-IL-2 HIL-2 was eluted in a single peak at 100% acetonitrile at 28 min. Optimum urea concentration was found to be 0.5 M and 24 h reaction time was sufficient without any additive such as CaCl2 and Tween-20.

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Sugars in Korean and Japanese Beer - 2. Enzymatic Analysis - (한국 및 일본산 맥주의 당에 관한 연구 - 2. 효소적 분석 -)

  • 안용근
    • The Korean Journal of Food And Nutrition
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    • v.11 no.2
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    • pp.150-158
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    • 1998
  • Limit dextrin of Korean beer(3 brands) and Japanese beer(21 brands) were separated by ethanol fractionation. Limit dextrin of Korean and Japanese beer was estimated to be 1.1%. 1H-NMR analysis revealed that the limit dextrin showed both signal of $\alpha$-1, 4- and $\alpha$-1, 6- glucosidic linkage with its estimation ratio of average 5.5:1. Limit dextrin was hydrolyzed to glucose with the yield of 57.22% by Aspergillus awamori $\alpha$-glucosidase(24.7 unit) plus human salivay $\alpha$-amylase(2.4 unit) in 100${mu}ell$ of 0.043M acetate buffer at 37$^{\circ}C$ for 5 hour. Among them, limit dextrin of Korean beer showed the highest hydrolysis rate of 76%. Small size sugars (64.8%) removed by ethanol fractionation and limit dextrin(21.4%) hydrolyzed by amylases that is digestable sugar. Non hydrolyzed limit dextrin(13.8%) by the amylases which can be a growth factor of Bifidobacterium in human intestine.

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Recovery of High Purity TiO2 Powder from Ilmenite by Hydrochloric Acid Leaching (타이타늄 철석으로부터 염산 침출에 의한 고순도 이산화 타이타늄 회수)

  • Ahn, Hyeong Hun;Lee, Man Seung
    • Resources Recycling
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    • v.28 no.5
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    • pp.68-73
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    • 2019
  • Ilmenite is one of the principal ores for the production of titanium dioxide. To produce titanium dioxide with purity higher than 99.9% from ilmenite, Ti(IV) should be separated from the dissolved impurities such as Fe(III), Si(IV), and Mn(II) present in ilmenite. In this work, a hydrometallurgical process was investigated to recover pure titanium dioxide from ilmenite by HCl leaching followed by separation and hydrolysis of Ti(IV). An optimum leaching condition was obtained by investigating the effect of HCl concentration, pulp density, and leaching time on the leaching percentage of Ti(IV), Fe(III), Si(IV), and Mn(II). Ammonium hydroxide and sodium hydroxide solutions were employed as neutralizing agents to hydrolyze Ti(IV) from the stripping solution of Ti(IV). Titanium dioxide of the anatase phase was obtained by calcination of the hydrolyzed precipitates with $NH_4OH$ solution. A hydrometallurgical process can be developed to produce pure $TiO_2$ powders from ilmenite.

Further Characterization of Protein Sulfotransferase(s) of Rat Brain by Alkaline Hydrolysis of Sulfated Proteins (황산화 단백질의 알칼리 가수분해에 의한 쥐 뇌의 단백질 황산기전달효소의 추가특성 연구)

  • 유재욱;최명언
    • The Korean Journal of Zoology
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    • v.33 no.4
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    • pp.468-475
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    • 1990
  • An In vitro protein sulfation in the soluble fraction of rat brain was charaderized further by an improved method of alkaline hydrolysis and thin layer ceflulose electrophoresis TLE) The protein sulfation was carried out in a reaction system containing [35 S] 3'-phosphoadenosine-5'-phosphosulfate (PAPS), Tris-maleate buffer (pH 8), MgCI$_2$, and soluble proteins from rat brain. The sulfated proteins were precipitated by acetone and alkaline hydrolysis was performed to obtain sulfated amino acids. The hydrolysate was separated further by TLE and the separated residues were identified by fluorography. The Iluorography of one-dimensional The showed at least nine sulfated residues including tryosine-O-sulfate. The other spots were not identified yet positively. General properties of protein sulfotransferases (PST) using this method were re-examined such as effects of concentrations of PAPS, pH, incubation temperature and $Mg^2$+. These results suggest a possible occurrence of several PST corresponding to each sulfated residue in rat brain and that the sulfation can occur not only in tyrosine but also in other residues as well.

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