• Korean Journal of Food Science and Technology
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• v.5 no.2
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• pp.78-83
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• 1973

The naringin hydrolyzing enzyme has been purified from the culture filtrate of the mold Aspergillus S-1 which selected to remove the bitter test of the orange or citrus fruits industrily. In a view of purity naringinase was more effectively purified in order of molecular sieving on Sephadeex G-200, starach gel electrophoresis, chromatography or a DEAE-Cellulose column and fractional precipitation by ammonium sulfate. The purified enzyme is homogeneous in paper electrophoresis from a culture filtrate by treatment fractional precipitation with ammonium sulfate, DEAE-Cellulose treatment and Sephadex-200 column chromatography and it hydrolyse only naringin to purunin.

• Applied Biological Chemistry
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• v.38 no.2
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• pp.147-150
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• 1995

Effects of gelation conditions on physical properties of dover sole skin gelatin prepared by fractional precipitation with ethanol were investigated. The physical properties such as gel strength, melting point and gelling point of both ethanol treated and non-ethanoltreated gelatins were improved as concentration of gelatin was increased. The physical property of 10% ethanol treated gelatin sol reached maximum at pH 6.0, whereas non-treated one showed maximum at pH 5.0. Both ethanol treated and non-treated gelatin gel showed the higher gel strength and melting point at lower temperatures and longer period of time. Generally, the physical properties of ethanol treated gelatin gel was better than those of non-ethanol treated gel.

• Resources Recycling
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• v.17 no.5
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• pp.3-10
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• 2008

We researched recycle of mixed waste acids including HF, $CH_{3}COOH$, $HNO_3$ produced during semiconductor wafer process. At first, we recovered HF in form of $Na_{2}SiF_6$ by precipitation using $NaNO_3$ and $Na_{2}SiO_3$. Concentration of HF was made down from 110 g/L, initial concectration, to 0.5 g/L and Recovery rate of HF was 99.5%. After recovery of HF, concentration of $HNO_3$ and $CH_{3}COOH$ is 498 g/L, 265 g/L respectively. From that mixed acid, we recovered $CH_{3}COOH$ using 2 stages of fractional distillation. In first stage, $CH_{3}COOH$ was distilled for separation from $HNO_3$. And in second stage, we recoverd refined $CH_{3}COOH$ by using fractional distillation for removing a little amount of $HNO_3$ in $CH_{3}COOH$ vapor. The concentration of recovered $CH_{3}COOH$ in second stage is 20% and finally recovery rate of $CH_{3}COOH$ is about 87.5%.

• Journal of the Korean Chemical Society
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• v.4 no.1
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• pp.44-50
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• 1957

Fibrous cellulose triacetate prepared from purified cotton under various temperatures was dissolved in the solution of 70%, monochloroacetic acid and it was fractionated using water as a precipitant. Eight fractions were obtained through the stepwise precipitation. Degree of polymerization and molecular weight of each fraction were measured viscometrically. Integral and differential molecular weight distribution curve were drawn for each sample prepared under various temperatures and were carefully observed. On this experimental study, following conclusions were obtained: Fractional precipitation can be carried out for fibrous cellulose triacetate in the solution of 70% monochloroacetic acid using water as a precipitant. The differences on the shapes of molecular weight distribution curve were occured on account of the various acetylation temperatures. At the relatively higher acetylation temperatures, the cellulose was randomly degraded and the portion of low degree of polymerization was increased. Commercial acetate, therefore, may not be prepared at above 40$^{\circ}C$ according to the molecular weight distribution curve regardless of higher viscosity and average degree of polymerization. It was concluded that the optimum acetylation temperature for commercial acetate was approximately 30$^{\circ}C$.

• YAKHAK HOEJI
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• v.6 no.2
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• pp.18-22
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• 1962

Purified preparation of .betha.-amylase is obtained from radish root by the means of fractional precipitation with ammonium sulfate. Purified preparation saccharifies the starch, .betha.-maltose being formed. Dextrinization in the true sense does not take place. Hydrolysis ceases when approximately 50% of the theoretical yield of maltose is obtained and there remains a substance (to be .betha.-limit dextrin) which gives a blue-violet with iodine, no glucose being formed. Stability of preparation is optimal at pH 4-9 and more completely inactivated at 65.deg. in fifteen minutes. .betha.-Amylase of radish exhibits optimal activity at and near pH 5.0, which varied depending upon the buffer. Calcium and chloride ions do not effect the activities of enzyme. The results of experiments with oxidizing, alkylating and mercaptide-forming reagents which have been reported to be specific for sulfhydryl groups confirm that free sulfhydryl groups are essential to the activity of .betha.-amylase from radish.

• Korean Chemical Engineering Research
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• v.54 no.1
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• pp.89-93
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• 2016

In this study, we investigated the separation behavior of the anticancer agent paclitaxel and its semi-synthetic precursor 10-deacetylpaclitaxel (10-DAP) from plant cell cultures. As a result of sequential separation/purification performed by biomass extraction with solvent, liquid-liquid extraction, adsorbent treatment, hexane precipitation, and fractional precipitation, the adsorbent treatment was found to be the most effective in separating and recovering 10-DAP from paclitaxel. The optimal adsorbent type, crude extract/adsorbent ratio, and adsorbent treatment temperature were sylopute, 1:1.5 (w/w), and $20^{\circ}C$, respectively. The separation/recovery of 10-DAP from paclitaxel was 74.1% in adsorbent treatment process under optimal conditions.

• BMB Reports
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• v.28 no.2
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• pp.149-154
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• 1995

Protein methylase II (S-adenosyl-L-methionine : protein O-methyl-transferase, EC 2.1.1.24; PM II) was purified approximately 1250-fold from porcine testis by fractional precipitation and DEAE-cellulose chromatography, followed by gel filtration on a Sephadex G-75 column and HPLC on a Protein Pak 125 column. The molecular weight of the enzyme was estimated to be 33,000 daltons by SDS-PAGE, which agreed with the value determined by gel filtration. Isoelectric focusing of purified PM II showed a single protein species with an isoelectric point of 6.2. The optimum pH for the reaction was 6.0. The $K_m$ value of the enzyme was $1{\times}10^{-5}M$ with a $V_{max}$ value of 769 pmol/min/mg of enzyme. S-adenosyl-L-homocysteine is a competitive inhibitor of PM II with a $K_i$ value of $1.38{\times}10^{-6}M$.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.332-339
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• 2010

The lipase from Mucor racemosus NRRL 3631 was partially purified by fractional precipitation using 60% ammonium sulfate, which resulted in a 8.33-fold purification. The partially purified lipase was then immobilized using different immobilization techniques: physical adsorption, ionic binding, and entrapment. Entrapment in a 4% agar proved to be the most suitable technique (82% yield), as the immobilized lipase was more stable at acidic and alkaline pHs than the free enzyme, plus 100% of the original activity was retained owing to the thermal stability of the immobilized enzyme after heat treatment for 60 min at $45^{\circ}C$. The calculated half-lives (472.5, 433.12, and 268.5 min at 50, 55, and $60^{\circ}C$, respectively) and the activation energy (9.85 kcal/mol) for the immobilized enzyme were higher than those for the free enzyme. Under the selected conditions, the immobilized enzyme had a higher $K_m$ (11.11 mM) and lower $V_{max}$ (105.26 U/mg protein) when compared with the free enzyme (8.33 mM and 125.0 U/mg protein, respectively). The operational stability of the biocatalyst was tested for both the hydrolysis of triglycerides and esterification of fatty acids with glycerol. After 4 cycles, the immobilized lipase retained approximately 50% and 80% of its original activity in the hydrolysis and esterification reactions, respectively.

• The Korean Journal of Mycology
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• v.17 no.3
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• pp.145-148
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• 1989

An acid-stable ${\alpha}-amylase$ produced by Aspergillus niger K-25 strain was purified by fractional precipitation with ammonium sulfate, ethacridine and acetone. The final preparation was homogeneous in cellulose acetate electrophoresis. The enzyme retained 91 % of its oringinal activity at pH 3.0, 8.7% at pH 2.4. The optimum pH of the enzyme was around pH 4. The purified-enzyme with optimum temperature of $40^{\circ}C$ was more heat-stable than the commercial product. The enzyme retained 80% of its original activity when heated to $60^{\circ}C$ for 30 minutes while the commercial amylase lost its acitivity completely within 30 minutes at $50^{\circ}C$.

• Journal of Applied Biological Chemistry
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• v.43 no.4
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• pp.235-239
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• 2000

A polysaccharide with antithrombin activity in Manda$^{(R)}& (PAM) was purified via procedures comprising three major steps, i.e. fractional precipitation with ethanol, anion exchange chromatography, and gel permeation chromatography. PAM showed a symmetrical peak on size exclusion HPLC, as assessed by refractive index, and behaved as a single band on cellulose acetate electrophoresis. The average molecular mass was estimated to be 222 kDa by gel filtration. PAM was found to be a sulfated heteropolysaccharide that contains sulfate group (20.5%, w/w) and uronic acid moiety (7.1 %, w/w) in addition to neutral sugar consisting of fucose, xylose, mannose, galactose, and glucose in a molar ratio of 1.00 : 0.35 : 0.28: 0.22 : 0.15. This polysaccharide appeared to inhibit blood coagulation via the intrinsic pathway in a dose-dependent pattern. The clotting of fibrinogen by thrombin was also significantly mitigated by the presence of PAM.