• Journal of Ginseng Research
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• v.39 no.3
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• pp.221-229
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• 2015

Background: Minor ginsenosides, those having low content in ginseng, have higher pharmacological activities. To obtain minor ginsenosides, the biotransformation of American ginseng protopanaxadiol (PPD)-ginsenoside was studied using special ginsenosidase type-I from Aspergillus niger g.848. Methods: DEAE (diethylaminoethyl)-cellulose and polyacrylamide gel electrophoresis were used in enzyme purification, thin-layer chromatography and high performance liquid chromatography (HPLC) were used in enzyme hydrolysis and kinetics; crude enzyme was used in minor ginsenoside preparation from PPD-ginsenoside; the products were separated with silica-gel-column, and recognized by HPLC and NMR (Nuclear Magnetic Resonance). Results: The enzyme molecular weight was 75 kDa; the enzyme firstly hydrolyzed the C-20 position 20-O-${\beta}$-D-Glc of ginsenoside Rb1, then the C-3 position 3-O-${\beta}$-D-Glc with the pathway $Rb1{\rightarrow}Rd{\rightarrow}F2{\rightarrow}C-K$. However, the enzyme firstly hydrolyzed C-3 position 3-O-${\beta}$-D-Glc of ginsenoside Rb2 and Rc, finally hydrolyzed 20-O-L-Ara with the pathway $Rb2{\rightarrow}C-O{\rightarrow}C-Y{\rightarrow}C-K$, and $Rc{\rightarrow}C-Mc1{\rightarrow}C-Mc{\rightarrow}C-K$. According to enzyme kinetics, $K_m$ and $V_{max}$ of Michaelis-Menten equation, the enzyme reaction velocities on ginsenosides were Rb1 > Rb2 > Rc > Rd. However, the pure enzyme yield was only 3.1%, so crude enzyme was used for minor ginsenoside preparation. When the crude enzyme was reacted in 3% American ginseng PPD-ginsenoside (containing Rb1, Rb2, Rc, and Rd) at $45^{\circ}C$ and pH 5.0 for 18 h, the main products were minor ginsenosides C-Mc, C-Y, F2, and C-K; average molar yields were 43.7% for C-Mc from Rc, 42.4% for C-Y from Rb2, and 69.5% for F2 and C-K from Rb1 and Rd. Conclusion: Four monomer minor ginsenosides were successfully produced (at low-cost) from the PPD-ginsenosides using crude enzyme.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.5
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• pp.832-836
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• 1994

This study was carried out to investigate several kinds of characteristics of pork sausage prepared by different cooking temperature and time (60, 90, 120, 150, 180 minutes in $58^{\circ}C$ and 25, 40, 55, 70, 85 minutes in $65^{\circ}C$). In case of color, L(bright), a (red) and b(yellow) value were 64.60-65.26, 9.14-9.94 and 8.68-9.34 in $58^{\circ}C$, and 65.16-66.68, 8.78-9.62 and 7.66-8.36 in $63^{\circ}C$, respectively. Gel strength showed high when cooking time was 120, 250 and 180 minute in $58^{\circ}C$ and 40 minute in $65^{\circ}C$. Residual nitrite concentration showed higher $58^{\circ}C$ than $65^{\circ}C$ and decreased gradually as cooking time elevated in all cooking temperature. Total plate count in 58$^{\circ}C$ was higher than $65^{\circ}C$, was wholly $8.7{\times}10^2~3.5{\times}10^3$.In case of free amino acid content, Asp, Glu and Lys were high and Cys, Met and Tyr low and was not different with $58^{\circ}C$ and $65^{\circ}C$. The result of sensory evaluation was not different (p<0.05) with $58^{\circ}C\;and\;65^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.24 no.3
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• pp.284-288
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• 1992

This study was undertaken to investigate the effect of pH and phytate level on the solubility of the protein due to binding between phytate and low-phytate rapeseed protein isolate by means of SDS-polyacrylamide gel electrophoresis. Results showed that the number of protein bands decreased by the increasing amount of phytate added to the soluble extract at pH 2.0 and 5.0 whereas there was no change at pH 11.5. Among 18 bands of rapeseed proteins at pH 2.0, seven bands (105.8, 52.3, 37.3, 34.8, 26.3, 21.3, 18.4 KDa) were removed by precipitation with 100 mg phytate addition and six bands (78.8, 46.5, 19.4, 16.8, 11.7, 8.5 KDa) further disappeared by 150 mg phytate addition. Among 15 bands at pH 5.0, only four bands disappeared by phytate addition. It is suggested that the functionality of rapeseed protein isolate can be improved by lowering the phytate content.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.28 no.2
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• pp.227-236
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• 1995

The objective of this research was to characterize fucoidans isolated from Laminaria religiosa and Undaria pinnatifida in Korea to obtain basic data for Production of soluble dietary fiber materials with biological functionality. Fucoidans were successively extracted 3 times at $65\%$ for 1hr with arid solution of pH 2.0, and cetylpyridinium chloride was used for partial purification. The yields of partially purified fucoidans were $2.71\%$ for L. religiosa, $6.65\%$ for sporophylls of U. pinnatifida and $0.40\%$ for blade of U. pinnatifida. The yield from sporophylls of U. pinnatifida was highest among the sample tested, whereas the yield from blade of U. pinnatifida was lowest. It appeared that the fuconidans content in different parts of U. pinnatifida varied. Partially purified fucoidans were separated into 3 fractions by DEAE-Sephadex A-25 ion exchange column and the maior fractions were refractionated with tractional precipitation with ethanol. $60-70\%$ ethanol precipitated fractions of 1. religiosa and sporophylls of U. pinnatifida turned out to be homogeneous by cellulose acetate electrophoresis and gel filteration chromatography. The molar ratios of fucose, galactose, and sulfate in the purified fucoidans(ethanol precipitated fractions) were 1 : 0.31 : 2.43 for L. religiosa and 1 : 0.97 : 1.99 for sporophylls of U. pinnatifida. The averaged molecular weights of the purified fucoidans from L. religiosa and sporophylls of U. pinnatifida were 31,000 and 38,000, respectively.

• BMB Reports
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• v.39 no.4
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• pp.432-440
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• 2006

A tuber lectin from Arisaema jacquemontii Blume belonging to family Araceae was purified by employing a single step affinity chromatography using column of asialofetuin-linked amino activated silica beads and the bound lectin was eluted with 100 mM glycine-HCl buffer pH 2.5. The purified A. jacquemontii lectin (AJL) showed a single protein band with an apparent molecular mass of 13.4 kDa when submitted to SDS-polyacrylamide gel electrophoresis under reducing as well as non-reducing conditions. The native molecular mass of AJL determined by gel filtration on a Biogel P-200 column was 52 kDa and its carbohydrate content was estimated to be 3.40%. Thus AJL is a tetrameric glycoprotein. The purified lectin agglutinated erythrocytes from rabbit but not from human. Its activity was not inhibited by any of the mono- and disaccharides tested except N-acetyl-D-lactosamine having minimal inhibitory sugar concentration (MIC) 25 mM. Among the glycoproteins tested only asialofetuin was found to be inhibitory (MIC $125\;{\mu}g/mL$). A single band was obtained in native PAGE at pH 4.5 while PAGE at pH 8.3 showed two bands. Isoelectric focusing of AJL gave multiple bands in the pI range of 4.6-5.5. When incorporated in artificial diet AJL significantly affected the development of Bactrocera cucurbitae (Coquillett) larvae indicating the possibility of using this lectin in a biotechnological strategy for insect management of cucurbits. Larvae fed on artificial diet containing sub-lethal dose of AJL showed a significant decrease in acid phosphatase and alkaline phosphatase activity while esterase activity markedly increased as compared to larvae fed on diet without lectin. Out of various human cancer cell lines employed in sulphorhodamine B (SRB) assay, this lectin was found to have appreciable inhibitory effect on the in vitro proliferation of HCT-15, HOP-62, SW-620, HT-29, IMR-32, SKOV-3, Colo-205, PC-3, HEP-2 and A-549 cancer cell lines by 82, 77, 73, 70, 41, 41, 37, 29, 21 and 21% respectively.

• The Korean Journal of Pesticide Science
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• v.12 no.4
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• pp.315-322
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• 2008

In this study, a simple, effective, and sensitive method has been developed for the quantitative residue analysis of cyhalofop-butyl and its metabolite cyhalofop acid in water and soil when kept under laboratory conditions. The content of cyholofop-butyl and cyhalofop acid in water and soil was analyzed by first purifying the compounds through liquid-liquid extraction and partitioning followed by Silica gel (adsorption) chromatography. Upon the completion of the purification step the residual levels were monitored through high-performance liquid chromatography (HPLC) using a UV absorbance detector. The recoveries of cyhalofop-butyl from three replicates spiked at two different concentrations ranged from 82.5 to 100.0% and from 66.7 to 97.9% in water and soil, respectively. The limit of detection and minimum detection level of cyhalofop-butyl in water and soil was 0.02 ppm and 10 ng, respectively. The recoveries of cyhalofop acid ranged from 80.7 to 104.8% in water and from 76.9 to 98.1 % in soil. The limit of detection of cyhalofop acid was 0.005 ppm in water and 0.01 ppm in soil, while the minimum detection level was 2 ng both in water and soil. The half-live of cyhalofop-butyl was 4.14 and 6.6 days in water and soil, respectively. The method was successfully applied to evaluate cyhalofop-butyl residues in water and soil applied aj. 30% emulsion, oil in water (EW) product.

• Korean Journal of Food Science and Technology
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• v.18 no.2
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• pp.158-162
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• 1986

Various cell wall polysaccharides such as ionically associated pectin (IAP), covalently bounded pectin (CBP),4N potassium hydroxide soluble hemicellulosic fraction (HF,) and 0-3N soluble hemicellulosic fraction (HF,) were fractionated from crude cell wall of the fresh and soft persimmon by chemical method. The changesin cell wall polysaccharides were studied by gel filteration chromatography . The content of crude cell wall remarkably decreased in the soft persimmon. The decreasing rates of IAP, CBP and $HF_2$ were 59, 60 and 74%, respectively, while $HF_1$ and cellulose changed only a little during softening. Sugar compositions of IAP and CBP were 72-84% uronic acid, 5-1% hexose and 11-16% pentose, and also the hemicellulose was composed of uronic acid besides hexose and pentose that was hemicellulosic components. The loss rate of pentose in IAP, of hexose in CBP, of hexose and uronic acid in $HF_2$, of pentose in $HF_1$ increased during softening. Though apparent average molecular freight of all polysaccharides shifted from high molecular freight to low molecular weight polymer, the shifting degree of CBP and $HF_2$ was especially remarkable during softening. It is suggested that the severe softening phenomenon of persimmon involved the degradation and dissolution of wall bound-CBP and $HF_2$ which were associated with each other.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.31-41
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• 1998

A carotenoprotein from the muscle of Ascidian (Halocynthia roretzi) was purified by ion exchange chromatography and gel filtration chromatography, and analyzed molecular weight, stability of pH and heat, effect of denaturing agents, amino acids and fatty acids composition. The purified carotenoprotein had absorption maxima of 463 nm and 439 nm. The carotenoprotein had an approxmimate molecular weight of 64.4 kDa in polyacrylamide gel electrophoresis. The amino acid compositions of carotenoprotein were mainly Gly (15.39%), Asn (11.31%), Gln (10.62%) and Ser (13.35%). The major fatty acids composition of carotenoprotein were $C_{16:1(n-7)}\;(15.4%)$, $C_{22:1(n-9)}\;(14.5%)$ and $C_{20:1(n-11)}\;(11.4%)$. The monounsaturated fatty acids (45.2%) contained abundant content compared to other saturated (38.1%) and polyunsaturated (11.7%) fatty acids.

• Applied Biological Chemistry
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• v.25 no.2
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• pp.67-74
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• 1982

Morphology, physicochemical properties, pasting properties in the presence of various anionic ions and aging of gels of Akibare (Japoica type) and Milyang 23 (Indica type) rice starch were studied, Both starches. were polygonal with length in the range of $3{\sim}6{\mu}m$. Starch granules of Akibare were somewhat smaller than those of Milyang 23. X-ray diffraction study demonstrated that peak shape and intensity were significantly different between the two starches. Akibare and Milyang 23 rice starch had amylose content of 18.5 and 19.5% and water binding capacity of 106 and 100%, respectively. Milyang 23 rice starch had a higher swelling power than Akibare starch. A relationship between percent solubility and swelling power implied that bonding forces within the granules of the both starches were different. The optical transmittance of 0.1% suspension of the two starches increased rapidly from $60^{\circ}C$. In the range of $60{\sim}90^{\circ}C$, the two starches showed a single gelatinization pattern. Amylograms of the two starches in the presence of various anionic ions showed that pasting temperature and peak temperature were progressively increased in the order of SCN-${SO_4}^=$. SCN- and I- ions increased the peak height of Akibare rice starch while only SCN- ion was effective for Milyang 23 rice starch. There were no differences in the rates of retrogradation of 45% gels of the two starches stored at $21^{\circ}C$.

• Journal of Sericultural and Entomological Science
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• v.31 no.2
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• pp.82-90
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• 1989

Antheraea yamamai vitellin was purified from matured eggs by polyacrylamide gel electrophoresis for characterization of its biochemical properties : molecular weight, sugar and lipid composition, amino acid composition and electron microscopic morphology, etc. 1. A yamamai vitellin was composed of two subunits, large and small, showing different mobility in SDS-polyacrylamide gel electrophoresis. 2. The molecular weight of the vitellin was estimated to be approximately 450,000 dalton and the large and small subunits were 174,000 dalton and 44,000 dalton, respectively. 3. The vitellin seemed to be a glycolipoprotein since it showed a positive reaction to coomassie brilliant blue, sudan black B and PAS staining. Both subunits were similiar in this aspect. 4. Lipid of the witellin reveraled several different types including saturated lipids. 5. When the vitellin was incubated at 7$0^{\circ}C$ for 60 minites its apoprotein still cross-reacted to the specific antiserum to the native vitellin. Its sugar components were also detected by PAS staining, but its lipid portion was not detected by sudan black B staining. 6. Its amino acid composition was similar to that of other insects, but its glycine content was peculiarly very high. 7. The vitellin molecule was spherical in shape with a diameter of 14$\pm$0.8nm by negatively.