• Membrane Journal
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• v.4 no.3
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• pp.163-170
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• 1994

The separation of inorganic salt from amino acid solution using was performed electrodialysis. In order to review the availability of electrodialysis using isoelectric point of amino acid as a bio-separation technique, electrodialysis stacks were designed using ion exchange membrane. Separation of NaCl from amino acid solution was performed in the condition similar to amino acid fermentation process. To obtain otimum conditions of separation, leakage of amino acid depending of pH and limiting current density were measured. On the basis of optimum condition, removal of NaCl and leakage of amino acid were investigated quantitatively in batch and continuous process, and current efficiencies were also obtained. As a result of batch experiment for 11 hours each amino acid solution, removal efficiencies of NaCl were in the ranges of 96.1~96.2%. Amino acid leakage rate of glycine, methionine, alanine were 2.5, 1.7, 2.0% respectively. Current efficiencies were in the ranges of 44.5~44.6%. As a result of continuous experiment in various flow rate of each amino acid solution, it took 120 ~ 150 min to reach to steady state. Removal efficiency of NaCl was increased as the flow rate was decreased, but current efficiency was decreased. At the steady states, there were no leakage of amino acid.

• Korean journal of applied entomology
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• v.56 no.1
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• pp.61-67
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• 2017

Two major sex pheromone components (Z-8-dodecenyl acetate and E-8-dodecenyl acetate) are known in the peach fruit moth, Grapholita molesta. From a putative biosynthetic pathway of these sex pheromone components, delta 10 desaturase ($10{\Delta}$ DES) has been proposed to play a crucial role in synthesizing a species-specific stereoisomer of the double bond. However, its molecular identity was not known. This study determined a putative desaturase (Gm-comp1575) as a $10{\Delta}$ DES candidate from G. molesta transcriptome constructed from the sex pheromone gland. Its open reading frame encodes 370 amino acid sequence with a predicted molecular weight at 43.2 kDa and isoelectric point at 8.77. It was predicted to have four transmembrane domains and six glycosylation sites at N-terminal or cytosolic domains. A phylogenetic analysis with its predicted amino acid sequence indicated that Gm-comp1575 is closely related with known $10{\Delta}$ DES genes of other insects. Gm-comp1575 transcript was detected in female adults at sex pheromone gland and other abdominal tissues. RNA interference of Gm-comp1575 significantly reduced attractiveness of virgin females in apple orchard compared to control females. These results suggest that Gm-comp1575 is associated with sex pheromone biosynthesis of G. molesta.

• BMB Reports
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• v.39 no.5
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• pp.502-510
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• 2006

2C-methyl-D-erythritol 2, 4-cyclodiphosphate synthase (MECPS, EC: 4.6.1.12) is the fifth enzyme of the non-mevalonate terpenoid pathway for isopentenyl diphosphate biosynthesis and is involved in the methylerythritol phosphate (MEP) pathway for ginkgolide biosynthesis. The full-length mecps cDNA sequence (designated as Gbmecps) was cloned and characterized for the first time from gymnosperm plant species, Ginkgo biloba, using RACE (rapid amplification of cDNA ends) technique. The full-length cDNA of Gbmecps was 874 bp containing a 720 bp open reading frame (ORF) encoding a peptide of 239 amino acids with a calculated molecular mass of 26.03 kDa and an isoelectric point of 8.83. Comparative and bioinformatic analyses revealed that GbMECPS showed extensive homology with MECPSs from other species and contained conserved residues owned by the MECPS protein family. Phylogenetic analysis indicated that GbMECPS was more ancient than other plant MECPSs. Tissue expression pattern analysis indicated that GbMECPS expressed the highest in roots, followed by in leaves, and the lowest in seeds. The color complementation assay indicated that GbMECPS could accelerate the accumulation of $\beta$-carotene. The cloning, characterization and functional analysis of GbMECPS will be helpful to understand more about the role of MECPS involved in the ginkgolides biosynthesis at the molecular level.

• Korean journal of food and cookery science
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• v.7 no.2
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• pp.97-104
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• 1991

This study was carried out in order to study the protein functionality such as foaming and emulsifying properties by succinylation of peanut protein isolates. Succinylated and unsuccinylated peanut protein isolate was tested for to find out the effect of pH, heat treatment and sodium chloride concentration on the solubility, foam expansion, foam stability, emulsion capacity and emulsion stability. The results are summarized as follows; 1. Succinylation enhanced the solubility of peanut protein isotate (PPI). The solubility of succinylated PPI markedly increased at pH 4.5. When the protein solutions was heated, the solubility of succinylated PPI greatly increased than PPI at pH 3. With addition of NaCl, solubility of succinylated PPI increased at pH 7 and pH 9. 2. The foam expansion of PPI and succinylated PPI on pH was no difference between both proteins. Addition of NaCl and heat treatment caused steeply increased in foam expansion at pH 3. 3. The foam stability of PPI and succinylated PPI showed the lowest value at pH 4.5. When PPI and succinylated PPI was heated, foam stability of two proteins incensed at pH 3 and showed similar aspects between PPI and succinylated PPI. However, at pH 9 stability of succinylated PPI decreased by heat treatment over $60^{\circ}C$. 4. Emulsion capacity of succinylated PPI on pH was markedly increased and showed the highest value at pH 11. At pH 4.5 which is isoelectric point of PPI, emulsion capacity of PPI by succinylation improved than that of PPI. When succinylated PPI was heated, emulsion capacity was greatly increased at pH 2 and pH 7. With NaCl was added, emulsion capacity of succinylated PPI increased than that of PPI. 5. Emulsion stability of PPI and succinylated PPI was affected by pH and showed its highest value at pH 11. At pH 4.5, emulsion stability of succinylated PPI increased than that of PPI. Addition of NaCl and heat treatment caused slightly increased in emulsion stability of succinylated PPI.

• Korean Journal of Food Science and Technology
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• v.25 no.1
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• pp.39-45
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• 1993

The effects of enzymatic modification with pepsin and actinidin was studied on molecular weight distributions and functional properties of hydrolysates from soy protein isolate (SPI) differing in degree of hydrolysis. The hydrolyzed SPI by pepsin showed 41.5% degree of hydrolysis after 5 min, and maximum hydrolysis was obtained after 2 hours. Actinidin hydrolyzed SPI 26.71% degree after 1 hour. On SDS-PAGE, native SPI showed 9 distinguishable bands on SDS-PAGE gel. Pepsin treated SPI showed one broad band in the lower part of gel. This band was shifted further to the bottom of the gel and became faint as hydrolysis time increased. While actinidin treated SPI showed different SDS-PAGE pattern from pepsin. However PAGE patterns were similar with pepsin and actinidin treated groups. With pepsin treatment, solubility of SPI distinctively increased around isoelectric point(pI). Emulsifying activity (EA) and emulsifying stability (ES) showed marked increase over pH range of $3.0{\sim}8.0$. 5 min modified group had most excellent foam expansion (FE). Foam stability (FS) was increased as pepsin treatment time increased at pI. With actinidin treatment, solubility was increased. 60 min modified SPI had the most effective EA at pH 4.5. However ES was not effected by actinidin treatment. 5 min modified group was most effect in FE. FS was higher at alkaline pH.

• Applied Chemistry for Engineering
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• v.5 no.3
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• pp.547-559
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• 1994

To effectively utilize fish skin wastes from marine manufactory, the optimal extraction conditions to prepare gelatin from fish skins of Alaska pollack, cod and yellowfin sole were investigated. In addition, the physical properties of the fish skin gelatins prepared under the optimal extraction conditions were compared with the commercial animal skin gelatin. The conditions for extraction of gelatins from fish skins were as follows ; The skins were limed with 1.0~1.5%(w/v) calcium hydroxide solution. The fish skin gelatins were extracted with 6~7 volumes of water(pH 6.0~7.0) for 5hrs at $40{\sim}50^{\circ}C$, and the yield of Alaska pollack skin gelatin extracted under the above conditions was higher than those of cod and yellowfin sole skins. The heavy metal contents, jelly strength and electric conductivities of fish skin gelatins were lower than those of a commercial gelatin(bovine skin), but the viscosity and isoelectric point were higher. The amount of amino acid in fish skin, such as gelatin, glutamic acid, serine, threonine, methionine and cysteine, were higher than those in pig and ox skin. However, the contents of hydroxyproline and proline were lower.

• Korean Journal of Microbiology
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• v.45 no.2
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• pp.200-207
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• 2009

In this study, the characterization of purified erythritol 4-phosphate dehydrogenase, key enzyme of erythritol biosynthesis, produced by Penicillium sp. KJ81 was investigated. Optimum production conditions of erythritol 4-phosphate dehydrogenase was 1 vvm areration, 200 rpm agitation, at $37^{\circ}C$ for 8 days in the medium containing 30% sucrose, 0.5% yeast extract, 0.5% $(NH_4)_2SO_4$, 0.1% $KH_2PO_4$, and 0.05%$MgCl_2$. Erythritol 4-phosphate dehydrogenase was purified through ultrafiltration and preparative gel electrophoresis from cell extract of Penicillium sp. KJ81. This enzyme was especially active on erythrose 4-phosphate with 1.07 mM of Km value. It gave a single band on native polyacrylamide gel electrophoresis and an isoelectric point of 4.6. The enzyme had an optimal activity at pH 7.0 and $30^{\circ}C$. It was stable between pH 4.0 and 9.0, and also below $30^{\circ}C$. The enzyme activity was completely inhibited by 1mM $Cu^{2+}$ and 1 mM $Zn^{2+}$, but was not significantly affected by other cations tested. This enzyme was inactivated by treatment of tyrosine specific reagent, iodine and tryptophan specific reagent, N-bromosuccinimide. The substrate of the enzyme, erythrose 4-phosphate showed protective effect on the inactivation of the enzyme by both reagents. These results suggest that tryptophan and tyrosine residues are probably located at or near active site of the enzyme.

• Journal of Life Science
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• v.18 no.6
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• pp.845-851
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• 2008

${\beta}-Lactamase$, secreted from Bacillus sp. J105 strain was purified to a single band on SDS-PAGE by ammonium sulfate precipitation, ion exchange column chromatography and gel-filtration. The molecular weight of the purified enzyme was 31 kDa on SDS-PAGE and its isoelectric point was 7.35. Optimal pH and temperature for enzymatic reaction were 5 and $40^{\circ}C$, respectively. As a result of total amino acid composition analysis of the purified enzyme, Gly and Ala were occupied 14.1 and 13.3 mole %, respectively. Km and Vmax value of purified enzyme were 1.33 mM and 0.36 mM/ml using ampicillin as a substrate, respectively.

• Korean Journal of Food Science and Technology
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• v.21 no.3
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• pp.338-344
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• 1989

This study was conducted to investigate the mechanism involved with gelation of soybean proteins, 7S and 11S. For the preparations of soybean gels, calsium coagulation and isoelectric point precipitation through the lactic acid fermentation were employed. The textural properties and microstructure of soybean curds were examined by Instron Universal Testing Machine and Scanning Electron Microscope(SEM), respectively. Soybean cheeses were also prepared from soyprotein curds. The characteristics of prepared soybean cheeses were studied by Instron and Sensory evaluation. Microstructure of soybean curds demonstrated by SEM differed markely, postulating that molecular interaction occured in the curds varied with type of protein and coagulative conditions. Textural parameter measured by Instron demonstrated that the curds and the cheeses made through lactic acid fermentation showed higher values in hardness, gumminess and chewiness than those coagulated with $CaCl_2$ 11S PRF could give the curds with higher values in hardness, cohesiveness, springiness, gumminess and chewiness than SPI and 7S PRF Sensory evaluation results showed that soybean cheese made from 11S PRF scored higher values in taste, chewiness, and hardness. However, panels preferred soybean cheese prepared from SPI in color, chewiness and brittleness.

• Plant Biotechnology Reports
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• v.3 no.2
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• pp.147-155
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• 2009

Oryza grandiglumis Chitinase IVa (OgChitIVa) cDNA encoding a class IV chitinase was cloned from wild rice (Oryza grandiglumis). OgChitIVa cDNA contains an open reading frame of 867 nucleotides encoding 288 amino acid residues with a predicted molecular weight of 30.4 kDa and isoelectric point of 8.48. Deduced amino acid sequences of OgChitIVa include the signal peptide and chitin-binding domain in the N-terminal domain and conserved catalytic domain. OgChitIVa showed significant similarity at the amino acid level with related monocotyledonous rice and maize chitinase, but low similarity with dicotyledoneous chitinase. Southern blot analysis showed that OgChitIVa genes are present as two copies in the wild rice genome. It was shown that RNA expression of OgChitIVa was induced by defense/stress signaling chemicals, such as jasmonic acid, salicylic acid, and ethephon or cantharidin and endothall or wounding, and yeast extract. It was demonstrated that overexpression of OgChitIVa in Arabidopsis resulted in mild resistance against the fungal pathogen, Botrytis cinerea, by lowering disease rate and necrosis size. RT-PCR analysis showed that PR-1 and PR-2 RNA expression was induced in the transgenic lines. Here, we suggest that a novel OgChitIVa gene may play a role in signal transduction process in defense response against B. cinerea in plants.