• Korean Journal of Human Ecology
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• v.5 no.1
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• pp.48-61
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• 2002

This study was carried out to investigate the effects of four kinds of leavening agents on Jeung-Pyun fermantation. Milk-wine(M), fresh yeast(F), dry yeast(D), instant yeast(I) were used in Jeung-Pyun ingredients. The physicochemical properties, sensory evaluation were examined. The results of this study are summarized as follows: 1. Basic recipes for Jeung-Pyun by preliminary test were developed. 2. Specific volumes and expansion ratio of Jeung-Pyun was higher in the fresh yeast-added sample. 3. The pH of Jeung-Pyun was decreased significantly as the fermentation progressed 4. In the result comparing Jeung-Pyun extracting after 1st fermentation with Jeung-Pyun extracting 2nd fermentation by SEM, the former was widely distributed in stability of bubble and pore than the latter. 5. Standard recipe by Q.D.A. test added four kinds of leavening agents were as follows: (1)Jeung-Pyun added milk wine was 240min for 1st fermentation time, 60min for 2nd fermentation time, 35$^{\circ}C$ for fermentation temperature, 80% for fermentation humidity respectively. (2) Jeung-Pyun added fresh yeast was 90min for 1st fermentation time, 40min for 2nd fermentation time, 35$^{\circ}C$ for fermentation temperature, 80% for fermentation humidity respectively. (3)Jeung-Pyun added dry yeast was 90min for 1st fermentation time, 60min for 2nd fermentation time, 35$^{\circ}C$ for fermentation temperature, 60% for fermentation humidity respectively. (4)Jeung-Pyun added instant yeast was 90min for 1st fermentation time, 40min for 2nd fermentation time, 30$^{\circ}C$ for fermentation temperature, 60% for fermentation humidity respectively. 6.Based on sensory evaluation, Jeung-Pyun added fresh yeast was significantry higher than others in color, sweetness, moistness, softness, and overall quality. There was negative significance between milk wine flavor and astrigentness, and yeast flavor.

• YAKHAK HOEJI
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• v.41 no.5
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• pp.615-621
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• 1997

Dehydropeptidase-I (DHP-I) was solubilized from porcine kidney by treatment with n-butanol and partially purified 19.25 fold by $(NH_4)_2SO_4$ precipitation, DEAE-Sepharose CL-6B ion exchange chromatography and Sephacryl S-300 HR chromatography with an overall yield of 19.16. DHP-I showed its optimal activity at pH 7.5 and 25$^{\circ}C$. Its activity was stable under neutral and alkaline conditions, but was disappeared under acidic condition. And DHP-I was heat-labile and its activity remained at 45$^{\circ}C$ for 3hrs. The enzyme was not inhibited by dicationic ions, while its activity was increased by $Co^{2+}$(1mM) and $Zn^{2+}$ (0.1mM). The enzyme was inhibited by EDTA and N-ethylmaleimide. The relative molecular mass of DHP-I was estimated to be approximately 100kDa by gel filtration chromatography. The $K_m$ value of DHP-I for glycyldehydrophenylalanine (GDHP) was 1.98mM. DWP20418 [(1R, 5S, 6S)-6-[1-(R)-Hydroxyethyl]-1-methyl-2-[(2S, 4S)-2-(piperazinylcarbonyl)-1-(R)-hydroxyethyl)pyrrolidine-4-thio]carbapen-2-em-3-carboxylic acid], compared with meropenem (MEPM), was rather easily hydrolized by DHP-I, while it was four times more resistant than imipenem (IPM) to DHP-I.

• YAKHAK HOEJI
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• v.45 no.1
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• pp.46-54
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• 2001

Protein carboxyl Ο-methylation is a kind of enzymatic reaction producing carboxyl methylester catalyzed by protein carboxyl Ο-methyltransferases at the carboxyl group of amino acid residues in polypeptide. Since the finding of carboxyl methylesterl many studies have been focused on the under-standing of biological functions in eukaryotes but still not clear except for roles in Ras attachment to membrane and protein repair. In this study, we investigated the protein carboxyl methylation in porcine liver and testis in respect of identification and characterization of carboxyl methylesters and natural proteinous substrates using pH stability of the esters and electrophoresis under acidic and basic conditions. We detected several kinds of methyl esters, 3 kinds each in cytosolic fractions from liver and testis. Under the treatment of strong acid and base, the ratio between base-stable substrates and unstable ones in liver (4 : 6) was different from the ratio obtained in testis (6 : 4). The methyl accepting capacities were affected by enzymatic proteolysis between the range of 55 to 65% in liver and of 35 to 45% in testis. Separation of the methylated proteins by acidic electrophoresis in the presence of urea and SDS revealed distinctively natural substrates of 26, 33 and 80 kD in the cytosol from liver and of 14, 25, 32 and 86 kD from testis. Most of the labelling, however were lost following electrophoresis under moderate alkaline condition, except for molecules of newly detected 7 and 17 kD in livers and 15, 29, 40 and 80 kD in testis. From these results, it was proposed that protein carboxyl Ο-methylation in each organs may be catalyzed by different classes of protein carboxyl Ο-methyltransferases. In addition, it is suggested that the protein carboxyl methylation in liver and testis may have different patterns in respect of natural substrates.

• Bulletin of the Korean Chemical Society
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• v.34 no.11
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• pp.3307-3311
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• 2013

A new fiber optical sensor was developed for the determination of 2,4-dichlorophenol (DCP). The sensor was based on DCP oxidation by oxygen with the catalysis of iron(III) tetrasulfophthalocyanine (Fe(III)PcTs). The optical oxygen sensing film with $Ru(bpy)_3Cl_2$ as the fluorescence indicator was used to determine the consumption of oxygen in solution. A lock-in amplifier was used for detecting the lifetime of the oxygen sensing film by measuring the phase delay change of the sensor head. The different variables affecting the sensor performance were evaluated and optimized. Under the optimal conditions (i.e. pH 6.0, $25^{\circ}C$, Fe(III)PcTs concentration of 0.62 mg/mL), the linear detection range and response time of the sensor are $1.0{\times}10^{-6}-9.0{\times}10^{-6}$ mol/L and 250 s, respectively. The sensor displays high selectivity, good repeatability and stability, and can be used as an effective tool in analyzing DCP concentration in practical samples.

• The Korean Journal of Food And Nutrition
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• v.16 no.4
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• pp.334-339
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• 2003

To increase the utilization of citron, citron juice that is by-product of citron tea was spray dried and freeze dried. Cyclodextrin(CD) was used as wall material to stabilize during drying. The physiochemical properties of citron juice were as follows: water content of 82.3%, pH of 2.45, and there were little different in two kinds of drying or CD added in different ratio. Citric acid, malic acid, succinic acid and lactic acid were detected in all of the samples. Spray and freeze-drying increased markedly yellowness compared to that of citron juice. Heat stability was reduced by both of two kinds of drying, and CD 15% was more decreased than CD 10%. Water uptake by freeze-drying was somewhat higher than that of spray-drying. When sensory properties of original citron juice was compared with those of spray and freeze dried, freeze drying with 10% of cyclodextrin was evaluated as superior to citron juice or other drying conditions.

• Food Science of Animal Resources
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• v.35 no.5
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• pp.630-637
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• 2015

In the dairy industry, natural plant-based powders are widely used to develop flavor and functionality. However, most of these ingredients are water-insoluble; therefore, emulsification is essential. In this study, the efficacy of high pressure homogenization (HPH) on natural plant (chocolate or vanilla)-based model emulsions was investigated. The particle size, electrical conductivity, Brix, pH, and color were analyzed after HPH. HPH significantly decreased the particle size of chocolate-based emulsions as a function of elevated pressures (20-100 MPa). HPH decreased the mean particle size of chocolate-based emulsions from 29.01 μm to 5.12 μm, and that of vanilla-based emulsions from 4.18 μm to 2.44 μm. Electrical conductivity increased as a function of the elevated pressures after HPH, for both chocolate- and vanilla-based model emulsions. HPH at 100 MPa increased the electrical conductivity of chocolate-based model emulsions from 0.570 S/m to 0.680 S/m, and that of vanilla-based model emulsions from 0.573 S/m to 0.601 S/m. Increased electrical conductivity would be attributed to colloidal phase modification and dispersion of oil globules. Brix of both chocolate- and vanilla-based model emulsions gradually increased as a function of the HPH pressure. Thus, HPH increased the solubility of plant-based powders by decreasing the particle size. This study demonstrated the potential use of HPH for enhancing the emulsification process and stability of the natural plant powders for applications with dairy products.

• Journal of Pharmaceutical Investigation
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• v.37 no.1
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• pp.45-49
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• 2007

Dextran-5-aminosalicylic acid conjugate (dextran-5-ASA) was in vitro-evaluated as a polymeric colon-spe-cific prodrug of 5-aminosalicylic acid (5-ASA). Chemical stability of dextran-5-ASA in the pH 1.2 or 6.8 buffer solutions was investigated at 37 for 6 hrs. The dextran backbone was not degraded and no 5-ASA release was detected. Moreover, dextran-5-ASA neither liberated 5-ASA in the homogenates of the small intestine of rats nor was transported across Caco-2 cell monolayers, suggesting no significant loss of dextran-5-ASA during transit through the upper intestine. Furthermore, incubation of dextran-5-ASA in 10% cecal contents of rats released about 37% and 55% of 5-ASA bound to dextran in 8 hr and 24 hr, respectively. While that with either esterase or dextranase failed to liberate 5-ASA from the polymeric prodrug, incubation of dextran-5-ASA with both esterases and dextranse released 5-ASA up to about 24% of 5-ASA bound to dextran. These results suggest that, after oral administration of dextran-5-ASA, the polymeric prodrug is delivered specifically to and releases 5-ASA in the large intestine, and reveal that the 5-ASA release by cleavage of the ester bond requires precedent depolymerization of the dextran backbone.

• Journal of Pharmaceutical Investigation
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• v.37 no.1
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• pp.7-13
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• 2007

To produce stable polymer coating layer using the interaction between metal stent and polymer layer, Ahx-HSAB was synthesized by coupling 6-aminoheanoic acid (Ahx) with N-Hydroxy succinimidyl 4-azidobenzonate (HSAB) containing photo reactive group. Then, Ahx-HSAB was applied to self·assembled monolayer (SAM) on $TiO_2$-coated surface, since one end of Ahx-HSAB was carboxyl acid which was known to be able to interact with $TiO_2$ surface. That SAM layer was incubated in 1% polycaprolacton (PCL) solution and photoreacted by ultraviolet light (254 nm) to produce the chemical bond between SAM and polymer layer, followed by PCL polymer coating ({\sim}5\;{\mu}m$) by the method of spray coating. The surface change was investigated by measuring of contact angle of the surface. The contact angle values of stainless steel (SS) surface, $TiO_2$-coated surface, SAM layer by Ahx-HSAB, photoreacted surface with PCL and PCL layer by spray coating were 70.48${\pm}$1.89, 38.57${\pm}$3.31, 60.14${\pm}$2.21, 54.91${\pm}$2.70 and 56.47${\pm}$2.12, respectively. The stability of polymer layers was tested by incubation of PCL-coated plates in 0.1M PBS buffer (pH 7.4, 0.05%, Tween 80) with vigorous shaking (200 rpm). While the poiymer layer prepared by these processes showed the intact surface morphology over 3 days, the polymer layers prepared by spray coating of PCL onto SS plate (control 1) and $TiO_2$-coated SS plate (control 2) were Peeled off in 3 days. Thus, the polymer coating method using SAM and photoreaction seems to be a effective method to obtain the stable polymer layer onto SS surface.

• Journal of Microbiology and Biotechnology
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• v.20 no.12
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• pp.1653-1663
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• 2010

The first gene (${\alpha}$-gal1) encoding an extracellular ${\alpha}$-Dgalactosidase from the thermophilic fungus Talaromyces emersonii was cloned and characterized. The ${\alpha}$-gal1 gene consisted of an open reading frame of 1,792 base pairs interrupted by six introns that encoded a mature protein of 452 amino acids, including a 24 amino acid secretory signal sequence. The translated protein had highest identity with other fungal ${\alpha}$-galactosidases belonging to glycosyl hydrolase family 27. The ${\alpha}$-gal1 gene was overexpressed as a secretory protein with an N-terminal histidine tag in the methylotrophic yeast Pichia pastoris. Recombinant ${\alpha}$-Gal1 was secreted into the culture medium as a monomeric glycoprotein with a maximal yield of 10.75 mg/l and purified to homogeneity using Hisbinding nickel-agarose affinity chromatography. The purified enzyme was maximally active at $70^{\circ}C$, pH 4.5, and lost no activity over 10 days at $50^{\circ}C$. ${\alpha}$-Gal1 followed Michaelis-Menten kinetics ($V_{max}\;of\;240.3{\mu}M/min/mg,\;K_m\;of\;0.294 mM$) and was inhibited competitively by galactose ($K_m{^{obs}}$ of 0.57 mM, $K_i$ of 2.77 mM). The recombinant T. emersonii ${\alpha}$-galactosidase displayed broad substrate preference, being active on both oligo- and polymeric substrates, yet had strict specificity for the ${\alpha}$-galactosidic linkage. Owing to its substrate preference and noteworthy stability, ${\alpha}$-Gal1 is of particular interest for possible biotechnological applications involving the processing of plant materials.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.49 no.6
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• pp.772-778
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• 2016

To develop a value-added product from individually quick-frozen oysters Crassostrea gigas (IQFO), we prepared a retort pouched oyster soup (RPOS) from IQFOs and characterized its processing conditions and quality metrics. We found that the most appropriate manufacturing process for the RPOS consisted of half-thawing and washing raw IQF oysters, blanching, adding them to the retort pouch along with other ingredients (base soup stock, IQF oyster extract, radish, bean sprouts, garlic, and red pepper), sealing, retort sterilization ($120^{\circ}$, F0-value 10 min.), cooling, and packaging inspection. The moisture, crude protein, pH and salinity of the RPOS were 91.0%, 2.8%, 6.20 and 0.9%, respectively. The total amino acid content of the RPOS was 2,163.8 mg/100 g, and the main amino acids were glutamic acid, aspartic acid, leucine, proline, lysine and arginine. The primary inorganic ions were Na, K, S and Zn. In taste compounds, total free amino acid content was 313.4 mg/100 g, and the main free amino acids were glutamic acid, taurine, proline, hydroxyproline, aspartic acid, glycine, alanine, valine, lysine and arginine. This RPOS has good storage stability and organoleptic qualities compared with commercial retort pouched shellfish soup, and is suitable for commercialization as a value-added instant seafood soup.