• Korean Journal of Food Science and Technology
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• v.6 no.2
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• pp.75-78
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• 1974

An experiment has been carried out in order to analyze the main components of Korean Cattles' milk, and fractionate the milk protein by DEAE-cellulose column. The results obtained were summarized as follow. 1) The average values of specific gravity, pH and acidity of Korean Cattles milk which were negative in alcohol test were 1,036, 6.4 and 0.21, respectively. 2) The average values of total solids, solids-not-fat, protein, lactose and ash contents of Korean Cattles milk were 11.61%, 9.53%, 2.08%, 3.99%, 4.76% and 0.86%, respectively. 3) Distribution of casein, whey protein, N.P.N., protein precipitated in 12% TCA, lactoglobulin and lactalbumin contents of the milk were 3.07%, 1.13%, 0.10%, 4.06%, 0.34% and 0.66%, respectively. 4) Acid casein obtained from Korean Cattles milk was fractionated into four fractions on DEAE-cellulose column with 0.005M tris-citrate buffer containing 6M urea, pH 8.6, and the ratio of the fraction I, II, III and IV was 3.24%, 52.67%, 26.22% and 17.87%, respectively. 5) Whey protein obtained from Korean Cattles milk was also fractionated into four fractions on DEAE-cellulose column with 0.04M phosphate buffer, pH 5.8, and the ratio of the fraction I, II, III and IV was 41.74%, 10.17%, 1.50% and 46.59%, respectively.

• Current Research on Agriculture and Life Sciences
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• v.3
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• pp.166-173
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• 1985

Several enzyme immobilization methods has been compared for immobilization of pepsin. Carboxymethyl cellulose and diethylaminoethyl cellulose were activated with Hcl and with NaOH, and were used for immobilization of pepsin. Sepharose-4B was activated cyanogen bromide, and was used for immobilization of pepsin. Porous glass beads were derivatized with 3-aminopropyitrlethoxysilane and with succinicanhydride, and were used for immobilization of pepsin. The results abtained were summarized as follow, 1. 10 mg/gr. dry bead and 15mg/gr. dry bead of pepsin were absorbed to CM-cellulose and DEAE-cellulose, 20 mg/gr. dry bead and 27 mg/gr. dry bead were coupled to CM-cellulose and DEAE-cellulose with glutaraldehyde respectively. Enzyme yields were 22% and 24% of soluble pepsin. 2. 16 mg/gr. dry bead of pepsin was attached to cyanogen bromide activated sepharose-4B, 19mg/gr. dry bead was cross linked to the activated bead with glutaraldehyde. Immobilized enzyme activity was 23% of soluble pepsin. 3. 40 mg/gr. dry bead of pepsin was conjugated to the derivatized glass beads. Immobilized enzyme activity was 45% of soluble pepsin.

• Journal of Dairy Science and Biotechnology
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• v.18 no.1
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• pp.1-8
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• 2000

This experiment was carried out to study fractionation and physicochemical characteristics of caprine casein. Acid caseins obtained from caprine colostral and normal milk were analyzed by chymosin treatment and fractionated by DEAE-cellulose column chromatography with linear gradient and electrophoresis. Protein, fat and lactose of caprine normal milk were 2.70${\pm}$0.27%, 3.82${\pm}$0.51%, and 4.10${\pm}$0.29%, respectively. More non-protein nitrogen(NPN) was released by chymosin treatment from caprine colostral casein than normal casein. The electrophoretic pattern of caprine casein was not similar to that of bovine casein, Caprine normal casein was fractionated by DEAE-cellulose column chromatography with a 0.08${\sim}$0.18 M NaCl linear gradient into 5 pes with the proportion of 5.27%, 26.07%, 25.97%, 30.40% and 12.29%, respectively. In order to identify the pure fraction, the chymosin-treated caprine normal casein was fractionated by DEAE-cellulosecolumn chromatography with a 0.08${\sim}$0.18 M NaCl linear gradient into 6 peaks with the proportion of 17.06%, 9.10%, 17.85%, 20.11%, 27.03% and 8.85%, respectively.

• Journal of Microbiology and Biotechnology
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• v.18 no.3
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• pp.465-471
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• 2008

Highly active, stable, and magnetically separable immobilized enzymes were developed using carboxymethyl cellulose (CMC) and diethylaminoethyl cellulose DEAE-C; hereafter designated "DEAE" as supporting materials. Iron oxide nanoparticles penetrated the micropores of the supporting materials, rendering them magnetically separable. Lipase (LP) was immobilized on the surface of the supporting materials by using cross-linked enzyme aggregation (CLEA) by glutaraldehyde. The activity of enzyme aggregates coated on DEAE was approximately 2 times higher than that of enzyme aggregates coated on CMC. This is explained by the fact that enzyme aggregates with amine residues are more efficient than those with carboxyl residues. After a 96-h enantioselective ibuprofen esterification reaction, 6% ibuprofen propyl ester was produced from the racemic mixture of ibuprofen by using DEAE-LP, and 2.8% using CMC-LP.

• The Korean Journal of Food And Nutrition
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• v.10 no.4
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• pp.503-508
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• 1997

The extraction and separation methods of protein-bound polysaccharides from the mycelium and culture broth of L. edodes were investigated. The use 2% solution of surface active agent, Triton X-100 was effective for extraction of the protein-bound polysaccharide from the mycelium. The extraction of the protein-bound polysaccharides from mycelium with hot water was achieved by 4 hours extraction at 10$0^{\circ}C$. For the separation and partial purification of the protein bound polysaccharides the column chromatography using DEAE-Cellulose, DEAE-Sephadex and Sephadex proved to be effective.

• Journal of Microbiology and Biotechnology
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• v.25 no.8
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• pp.1291-1298
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• 2015

Five different polymer nanofibers, namely, polyaniline nanofiber (PANI), magnetically separable polyaniline nanofiber (PAMP), magnetically separable DEAE cellulose fiber (DEAE), magnetically separable CM cellulose fiber (CM), and polystyrene nanofiber (PSNF), have been used for the immobilization of lactase (E.C. 3.2.1.23). Except for CM and PSNF, three polymers showed great properties. The catalytic activities (k_cat) of the free, PANI, PAMP, and magnetic DEAE-cellulose were determined to be 4.0, 2.05, 0.59, and 0.042 mM/min·mg protein, respectively. The lactase immobilized on DEAE, PANI, and PAMP showed improved stability and recyclability. PANI- and PAMP-lactase showed only a 0-3% decrease in activity after 3 months of vigorous shaking conditions (200 rpm) and at room temperature (25℃). PANI-, PAMP-, and DEAE-lactase showed a high percentage of conversion (100%, 47%, and 12%) after a 1 h lactose hydrolysis reaction. The residual activities of PANI-, PAMP-, and DEAE-lactase after 10 times of recycling were 98%, 96%, and 97%, respectively.

• 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.

• Korean Journal of Veterinary Research
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• v.13 no.1
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• pp.47-52
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• 1973

An attempt was carried out to purify the cell components of Bordetella bronchiseptica by the mild procedures. From the supernatant of sonic treated colls, the K-agglutinogen, hemagglutinogen and skin necrotizing factor were separated by a successive use of DEAE-cellulose column chromatography and ammonium sulfate precipitation. The specific activity of purified K-agglutinogen was demonstrated by a gel-diffusion test and was also found to be free from other biologically active substances of B. bronchiseptica: namely hemagglutinin, skin-necrotizing factor and O-antigen.

• Journal of Life Science
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• v.22 no.4
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• pp.508-515
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• 2012

In this study, DEAE-cotton [derivatized by 2-(diethylamino)ethyl chloride hydrochloride (DEAE HCl)] was prepared as a carrier for immobilized $Pichia$ $stipitis$ for ethanol production. When cotton was derivatized with 0.5 M DEAE HCl, the yeast cell suspension was adsorbed at 100% of the initial cell $OD_{600}$. The adsorbed yeast cells were estimated to be 101.8 mg-dry cells/g-DEAE-cotton. In particular, when a flask culture using the immobilized yeast cells was conducted in a glucose and xylose-containing medium, the yeast cells on the DEAE-cotton gradually produced ethanol, according to glucose and xylose consumption; the ethanol yield was approximately 0.33 g-ethanol/g-monosaccharide. Because DEAE-cotton was successfully used as a carrier for ethanol production from a glucose and xylose-containing medium, we expect that this bioethanol production process may be used for the bioethanol production process from the hydrolysate of lignocellulosic biomass. All the results of DEAE-cotton were compared with those of DEAE-cellulose as a carrier for immobilization.

• Microbiology and Biotechnology Letters
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• v.17 no.6
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• pp.587-592
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• 1989

A strain of alkalophilic Bacillus sp. YS-309 capable of producing large amount of $\beta$-galactosidase has been isolated from soil sample. Intracellular $\beta$-galactosidase was purified 6.9 folds by procedures including ammonium sulfate precipitation, DEAE-cellulose chromatography, gel-filtration, DEAE-Sephadex A-50 chromatography with over-all yield of 17.8%. The molecular weight of native enzyme was 205, 000 by HPLC, and SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of 4 identical subunits with a molecular weight of 56, 000.