• Korean Journal of Food Science and Technology
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• v.37 no.2
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• pp.164-170
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• 2005

To improve functional properties of food proteins, homologous or heterologous ${\beta}-casein$ and 11S globulin(glycinin) from animal and vegetable proteins, respectively, were bio-hybridized using transglutaminase(MTGase). Susceptibility was confirmed by SDS-PAGE, particle size analyzed, and emulsion stability tested using Reddy and Fogler method, To determine how bio-hybridized protein influences emulsion stability, protein bound on oil droplet was investigated using Scanning Electron Microscopy (SEM). formation of bio-hybridized protein band was detected among homologous and heterologous proteins, with heterologous protein forming weak band in oligomer form. Homologous ${\beta}-casein$ protein showed high emulsion stability, while homologous glycinin showed almost no stability. Stability of heterologous ${\beta}-casein$ and glycinin protein was higher than that of glycinin. SEM photographs showed even distribution of bio-hybridized proteins on oil droplet improved stability.

• Korean journal of food and cookery science
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• v.7 no.3
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• pp.53-59
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• 1991

This study was carried out in order to investigate the change of protein functionalities such as foaming and emulsifying properties by succinylation of protein isolates. Succinylated and unsuccinylated munghean protein isolates were tested for finding out the effects of pH, heat treatment and sodium chloride concentration on the solubility, emulsion capacity, emulsion stability, foaming capacity, and foam stability. The results are summarized as follows: 1. Succinylation enhanced the solubility of MPI except at pH 4.5. When heated, succinylation greatly increased the solubility of succinylated MPI above $60^{\circ}C$. With the addition of NaCl, succinylation increased the solubility of MPI at acidic condition. 2. Emulsion capacity of succinylated MPI showed the lowest value at pH 7 and higher values at acidic and alkaine condition. when succinylated MPI was heated, emulsion capacity showed the highest at $80^{\circ}C$. With NaCl was added, emulsion capacity of succinylated MPI lincreased at pH 7, 9 or 11 decreased at pH 3 except addition of 1.0M NaCl. 3. Emulsion stability of MPI and succinylated MPI showed the highest at pH 4.5. Succinylation enhanced the emulsion stability of MPI at acidic condition. 4. The foaming capacity of MPI was increased at pH 3, 7 or 9 by succinylation. 5. When heated, foam stability of MPI and succinylated MPI showed the highest at pH 4.5 and at pH 11, respectively. When heated, both proteins showed the highest stability at $100^{\circ}C$.

• Korean Journal of Food Science and Technology
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• v.28 no.6
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• pp.1009-1013
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• 1996

This study was carried to investigate the emulsion stability of microcrystalline chitins (MCC) prepared from chitins of different molecular sizes and different degrees of phosphorylation in a model fatty food system. Chitins of low, medium and high molecular size prepared from crabshells were phosphorylated to 30-50% to make MCC. MCC prepared from chitin of medium molecular size revealed a high emulsion stability. The best emulsion stability was observed in MCC prepared from medium size chitin with 40% phosphorylation (M-40-MCC). The fat binding capacity of MCC was not significantly different among the samples. MCC with 50% phosphorylation had more fat binding capacity, ranging from 650-690%. When 2.46% of M-40-MCC was applied to a coconutoil-water system as an emulsifier, emulsion separation was observed from 10 min after emulsification, indicating that it could not be used as a sole emulsifier. When 50% of emulsifier (Span-60 &Tween-60) in a liquid coffee creamer, selected as a model fatty foods, was replaced by M-40-MCC, emulsion stability was as good as control. Consistency of liquid creamer was decreased and L value increased as the amount of MCC repacement increased. A liquid creamer with 50% emulsifier replaced by MCC had sensory characteristics equivalent to control.

• Food Science of Animal Resources
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• v.35 no.2
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• pp.258-264
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• 2015

This study was conducted to evaluate emulsion mapping between emulsion stability and cooking yields, apparent viscosity, and hardness of reduced-fat pork emulsion systems. The reduced-fat emulsion systems were supplemented with different lipid types and brown rice bran fiber (BRF) concentrations. Compared to the control with 30% back fat, lower emulsion stability and higher cooking yield of meat emulsion systems were observed in T1 (30% back fat+1% BRF), T2 (30% back fat+2% BRF), T3 (30% back fat+3% BRF), T4 (30% back fat+6% BRF), and T15 (10% back fat+10% canola oil+2% BRF). Lower emulsion stability and higher apparent viscosity were observed in T1, T2, T3, T4, and T8 (20% back fat+3% BRF) compared to the control. Lower emulsion stability and higher hardness was detected in all treatments compared with the control, except T5 (20% back fat), T10 (10% back fat+10% canola oil+2% BRF), T11 (10% back fat+10% olive oil+2% BRF), T12 (10% back fat+10% grape seed oil+2% BRF), and T13 (10% back fat+10% soybean oil+2% BRF). This approach has been found particularly useful for highlighting differences among the emulsified properties in emulsion meat products. Thus, the results obtained with emulsion mapping are useful in making emulsified meat products of desired quality characteristics, partially replacing pork back fat with a mix of 10% back fat, 10% canola oil and 2% BRF was most similar to the control with 30% pork back fat.

• Korean journal of food and cookery science
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• v.6 no.4 s.13
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• pp.9-14
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• 1990

The emlsifying properties of small red bean protein isoates were evaluated through their emulsion capacity and stability of the resulting emulsions. The influence of pH, Sodium Chloride and heat treatment on the efficiency of small red bean protein isolates as emulsifying agents was studied. The surface hydrophobicity (So) of small red bean protein islates also examined. The results were obtained as follows; 1. The emusion capacity of small red bean protein isolates was high at pH 11, low at pH 3 and decreased by heat treament. With addition of NaCl, emulsion capacity decreased steadily and showed lowest value when 0.2M NaCl was added. 2. The emulsion stability at pH 4.5 and heat treatment over $60^{\circ}C$ decreased emulsion stability at pH 4.5. When NaCl was added, emulsion stability was generally increased. 3. The surface hydrophobicity of small red bean protein isolates showed the highest value at pH 3 and lowest at pH 11 and increased as the heating temperature increased When 0.2 M NaCl was added, surface hydrophobicity also increased at pH 4.5.

• Journal of the Korean Applied Science and Technology
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• v.26 no.2
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• pp.117-123
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• 2009

Caprylic/Capric triglyceride-in-water emulsions stabilized by Nikkol HCO-60 and HCO-10 were prepared using emulsion inversion point method at different HLB values. Emulsions with various droplet sizes were formed, and emulsion inversion point was detected by electrical conductivity. The change in emulsion droplet sizes and long term stability were monitored using laser scattering method and visual method. The droplet sizes and stability of emulsions were affected by HLB of surfactant. At emulsion inversion point, the water volume fraction increased as the HLB of surfactants decreased. According to our analysis, this resulted from a tendency of forming the W/O (water-in-oil) emulsion as the HLB of surfactants was decreased. The emulsion inversion point was clearly detected by the microscope and the electric conductivity meter. Nanometer-sized emulsion was obtained at the optimum HLB by using emulsion inversion point method. The main pattern of instability of emulsions in HLB 12 and 13 systems was Ostwald ripening. However, The patterns of instability of emulsions below 11 of HLB systems were Ostwald ripening and coalescence. All emulsions produced with surfactants in the range of HLB 8-13, creaming caused by density difference between water phase and oil phase.

• The Korea Journal of Herbology
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• v.25 no.4
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• pp.145-149
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• 2010

Objectives : Since cosmetics have been one of the help of life, unlike medicine, natural products have been used for cosmetics, generally giving the image of safety and relief compared to synthetic products. Among them, Houttuynia cordata has been known as a useful herbal medicine with antibiotic, anti-inflammatory and anti-oxidative activities. In this study, we were to use Houttuynia cordata extract on formulation of cosmetic emulsions. Methods : The effects of Houttuynia cordata extract on emulsion stability and viscoelastic properties of emulsion were measured using turbiscan and rheometer. And we assessed the anti-oxidative and antibiotic activities of Houttuynia cordata extract. Results : 1. The results of this investigation for emulsion stability showed that the stability emulsion containing Houttuynia cordata extract was decreased depending on concentration of Houttuynia cordata extract. 2. Super oxide dismutase activity was strongly dependents on concentration of Houttuynia cordata extract. 3. Houttuynia cordata extract showed good anti-microbial activity against Staphylococcus aureus. Conclusions : Houttuynia cordata extract can be effectively used in cosmetic emulsions when the relation between natural product extracts and formulation of cosmetics is elucidated.

• 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.

• Journal of Pharmaceutical Investigation
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• v.27 no.4
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• pp.287-293
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• 1997

To make a stable o/w emulsion, the effects of egg lecithin as an emulsifier and polyvinylpyrrolidone (PVP) as an auxiliary emulsifier on the physical stability of emulsion were investigated. The oil-in-water emulsion system was manufactured by microfluidizer and evaluated the physical stability. Average particle size and size distribution of emulsion was measured by dynamic light scattering analyzer and interfacial tension was measured. From the interfacial tension tested, critical micelle concentration of the egg lecithin was 0.1 %w/v and optimal concentration for the preparation of emulsion was 1.0 %w/v. The mean particle size was about $0.2\;{\mu}m$ which was suitable for injections. The short-term accelerated stability studies were conducted by centrifugation, freeze-thaw method and shaking of the emulsion samples. The addition of PVP was caused the reduction in the particle size and improved the physical stability of emulsion. These results suggested that a mixed interfacial film comprising the egg lecithin and PVP was formed at the o/w interface and it was effective in preventing phase separation under thermic or mechanical stress. We used antineoplaston A10 (A10) as a model drug which is peptide and amino acid derivative having a action to the living organism against the development of neoplastic growth by a nonimmunological progress. It has a poor solubility in water and there may be a difficulty in formulation of A10. Emulsion formulation study about A10 was performed. Solubility of A10 in emulsion was about five times as high as that in water. From the results of solubility and partition coefficient, almost A10 molecules in o/w emulsion exist in the interface between oil and water.

• Preventive Nutrition and Food Science
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• v.3 no.2
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• pp.133-142
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• 1998

Effects of protein heat treatment and surfactant additionoo the orthokindetic stability of $\beta$-lactoglobulin-stabilized emulsions have been investigated under turbulent flow conditions. In studies on protein-stabilized emulsions, samples which had been subjected to heat treatment(i.e. the protein solution orthe emulsion) have been found to be more prone to orthokinetic coalescene than the untreated ones. The emulsions stabilized with protein heated above the denaturation temperature(i.e. 7$0^{\circ}C$) showed the bigger initial average droplet size, which resulted in an increased orthokinetic coalescenece rate. The storage of the protein-stabilized emulsion at high temperature prior to the shearing experiment also made the emulsion less stable in the shear field. Interestingly. the addition of DATEM has been found to produce a substantial increase in orthokinetic stability of the heat-denatured protein-stabilized emulsion system, although Tween 20 is the opposite case.