• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.1
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• pp.57-63
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• 2000

To extract insoluble proteins from abolished soybean meal, the meal was treatesd with phytase and protease produced by Aspergillus sp. SM-15 and Aspergillus sp. MS-18. The extraction of insoluble soybean protein was increased at alkaline range more than pH 5 in case of phytase, pH 7 to 11 in case of protease and pH 5 to 12 in case of the mixed enzyme of phytase and protease. The optimum extraction temperature of insoluble protein was 5$0^{\circ}C$ for phytase and the mixed enzyme of phytase and protease, and 6$0^{\circ}C$ for protease. The optimum treatment time for extraction of protein was 9 hrs for phytase, 11 hrs for protease and the mixed enzyme of phytase and protease and optimum unit of enzyme for extraction of protein was 600 unit, 40 unit and 900 unit＋60 unit in case of phytase, protease, phytase and protease, respectively. The treatment of mixed enzyme showed higher extracton rate of protein than single enzyme treatment. The foaming capacity, foaming stability, emulsion capacity, and emulsion stability of soybean meal protein by the treatment of the enzymes increased at all pH range. Further more oil absorption as well as water absorption capacities by the treatment of the enzymes were also increased. The functional properteis of the soybean meal protein treated by the mixed enzyme were higher than those of soybean meal protein treated by the single enzyme.

• Korean Journal of Food Science and Technology
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• v.30 no.3
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• pp.557-561
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• 1998

This study was conducted to investigate the functionality of soybean protein isolates extracted in acidic range (pH 2.0 and 3.0), neutral range (pH 7.0) and alkaline range (pH 10.0 and 12.0). The protein content of soybean protein isolates extracted at pH 3.0 was maximum (93.31%), but that of pH 7.0 was minimum (73.93%). The extraction yield of soybean protein isolates extracted at pH 3.0 was minimum (0.36%), but that of pH 12.0 was maximum (47.54%). The functionality (solubility, water absorption, oil absorption, foam capacity, foam stability, emulsion capacity and gelation) of soybean protein isolates was significantly influenced by pH of extraction medium. The soybean protein isolates extracted at pH 2.0 and 3.0 were more soluble at acidic ranges and those of pH 3.0 and 7.0 were more soluble at neutral ranges, but those of pH 2.0, 3.0, 7.0, 10.0 and 12.0 were more soluble at alkaline ranges than other ranges. The soybean protein isolates extracted at pH 2.0 and pH 12.0 gave greater water absorption, oil absorption and foam capacity than those extracted at pH 3.0, pH 7.0 and pH 10.0. And the emulsion capacity of soybean protein isolates was increased by the increase of extraction pH.

• Journal of Environmental Science International
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• v.26 no.5
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• pp.563-572
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• 2017

The Electrocoagulation-Flotation (ECF) process has great potential in wastewater treatment. ECF technology is effective in the removal of colloidal particles, oil-water emulsion, organic pollutants such as microalgae, and heavy metals. Numerous studies have been conducted on ECF; however, many of them used a conventional plate-type aluminum anode. In this study, we determined the effect of changing operational parameters such as power supply time, applied current, NaCl concentration, and pH on the turbidity removal efficiency of kaoline. We also determined the effects of different electrolyte types (NaCl, $MgSO_4$, $CaCl_2$, $Na_2SO_4$, and tap water), as well as the differences caused by using a plate-type and mesh-type aluminum anode, on the turbidity removal efficiency. The results showed that the optimal values of ECF time, applied current, NaCl concentration, and pH were 5 min, 0.35 A, 0.4 g/L NaCl in distilled water, and pH 7, respectively. The results also revealed that the turbidity removal efficiency of kaoline in different electrolytes decreased in the following sequence, given the same conductivity: tap water > $CaCl_2$ > $MgSO_4$ > NaCl > $Na_2SO_4$. The turbidity removal efficiency of the mesh-type aluminum anode was significantly greater than the plate-type aluminum anode.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.5
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• pp.519-524
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• 1992

purified rapeseed(Brassica napus var. Youngsan) protein was hydrolyzed by pronase. The hyrolysate protein was investigated for the some physicochemical and functional properties. UV and intrinsic fluorescence spectra of the hydrolysate showed the maximum absorption at 274nm and 360nm respectively. Intensity of yellow color decreased in the process of hydrolysis and the surface hydrophobicity decreased up to fourfold. The main bands of hydrolysate by sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) were observed at 14,000 to 12,000 dalton molecular weight. Solubilities of hydrolyzed protein increased by 10~15% compared to those of unhydrolyzed protein at acidic pH. In the hydrolysate, while absorption of both water and oil, foam expansion and emulsion stability were increased, absolute viscosity, heat coagulation, calcium coagulation, foam stability and emulsion activity were decreased.

• 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.

• Applied Biological Chemistry
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• v.47 no.2
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• pp.170-175
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• 2004

In this paper we studied about Bacillus sp. TBM40-3 producing biosurfactants. The strains were isolated from Taeback Mountain soil and identified as Bacillus sp. by l6S rDNA nucleotides sequence analysis. The TBM40-3 was gram-positive and rod-shaped as observed by field emission scanning microscopy. After the cultivation TBM40-3 in LB broth for 90 h and the surface tension of supernatant was decreased to 29 mN/m. Emulsification activity and stability of crude biosurfactant was measured by using water-immiscible hydrocarbons and oil as substrate. Maximum emulsification activity and stability was obtained from soybean oil. Also, we confirmed that the TBM40-3 producing biosurfactant had an effect on crude oil while showing a superior effect as compared to chemically synthesized surfactants (SDS, Span85, Tween40, Triton X-100). As a result, the Bacillus sp. TBM40-3 producing biosurfactant had potent properties as an emulsifying agent and an emulsion stabilizing agent.

• Applied Biological Chemistry
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• v.49 no.4
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• pp.304-308
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• 2006

To extract insoluble proteins from silkworm pupa meal, the meal was treated with pretense produced by Bacillus sp. JH-209. The extraction of insoluble silkworm pupa protein was enhanced at alkaline pHs ranged from 7 to 11 by treatment with the protease. The optimum extraction temperature was $40^{\circ}C$ for in soluble protein treated with pretense. The optimum protease treatment time for extraction of protein was 11 hrs and optimum amount of enzyme treated for extraction of protein was 60 Unit, respectively. The treatment of enzyme extracted more protein than ordinary extraction method without pretense. The foaming capacity, foaming stability, emulsion capacity, and emulsion stability of silkworm pupa meal protein extracted by the treatment of the enzymes increased at all pH ranges. Further more oil absorption as well as water absorption capacities of the protein extracted by the treatment of the enzymes were also increased.

• Archives of Pharmacal Research
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• v.29 no.7
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• pp.598-604
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• 2006

In many conventional drug delivery systems in vogue, failure to deliver efficient drug delivery at the target site/organs; is evident as a result, less efficacious pharmacological response is elicited. Microspheres can be derived a remedial measure which can improve site-specific drug delivery to a considerable extent. As an application, Lung-targeting Ofloxacin-loaded gelatin microspheres (GLOME) were prepared by water in oil emulsion method. The Central Composite Design (CCD) was used to optimize the process of preparation, the appearance and size distribution were examined by scanning electron microscopy, the aspects such as in vitro release characteristics, stability, drug loading, loading efficiency, pharmacokinetics and tissue distribution in albino mice were studied. The experimental results showed that the microspheres in the range of $0.32-22\;{\mu}m$. The drug loading and loading efficiency were 61.05 and 91.55% respectively. The in vitro release profile of the microspheres matched the korsmeyer’s peppas release pattern, and release at 1h was 42%, while for the original drug, ofloxacin under the same conditions 90.02% released in the first half an hour. After i.v. administration (15 min), the drug concentration of microspheres group in lung in albino mice was $1048\;{\mu}g/g$, while that of controlled group was $6.77\;{\mu}g/g$. GLOME found to release the drug to a maximum extent in the target tissue, lungs.

• Food Science of Animal Resources
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• v.42 no.5
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• pp.849-860
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• 2022

The myofibril protein (MP) isolate-saccharide graft reactions was prepared using the Maillard reaction with saccharides. The effects of various saccharides on protein functionality and quality of the Maillard reaction were investigated and compared with those of MP. The grafting degree of the MP isolate-saccharide graft reaction was significantly higher in the reducing sugar-treated groups (lactose, glucose, fructose, and palatinose). The browning intensity of the MP isolate-saccharide graft reaction with fructose, sucrose, and erythitol was higher than that observed in the control reaction (p<0.05). MP that reacted with reducing sugars (glucose, fructose, palatinose, and lactose) had fainter bands than MP that reacted with non-reducing sugars (sucrose, erythitol, trehalose, sorbitol, and xylitol). MPs conjugated with glucose exhibited higher protein solubility. The palatinose and lactose treatments were maximum in water binding capacity, though no significant difference in oil binding capacity among the saccharide treatments was observed. The emulsion stability of the MP isolate-saccharide graft reaction with palatinose and erythitol was higher than that of the control reaction. Therefore, reducing sugars have good protein functionality in the MP isolate-saccharides graft reaction.

• Journal of the Korean Chemical Society
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• v.57 no.4
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• pp.439-446
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• 2013

Chitosan (CS) and hydroxypropylmethyl cellulose (HPMC) blend microspheres were prepared by water-in-oil emulsion technique and were loaded with an anti-cancer drug 5-fluorouracil (5-FU). CS-HPMC microspheres were characterized by Fourier transform infrared spectroscopy to confirm the cross-linking reaction. Scanning electron microscopy (SEM) was also used to assess the surface morphology of particles prepared. The quantity of release of 5-FU from the microspheres have been studied in terms of blend composition and amount of cross-linking agent. Differential scanning calorimetry and X-ray diffraction techniques indicated a uniform distribution of 5-FU particles in microspheres, whereas SEM suggested the spherical structure of the microspheres with slight rough surface. The in vitro drug release indicated that the particle size and release kinetics depend upon blend composition, amount of cross-linking agent used and amount of 5-FU present in the microspheres.