• Journal of Microbiology and Biotechnology
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• v.6 no.3
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• pp.184-188
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• 1996

The Acinetobacter sp. BE-254 isolated from soil sources produced a bioemulsifier in the medium supplemented with n-hexadecane. This bioemulsifier was purified by the procedures of fractionation (ammonium sulfate and chilled acetone), extraction by hexane, and column chromatography on silica gel 60. The results from various color reactions indicated that the bioemulsifier was a glycolipid. The purified emulsifier was very stable at pHs ranging from 4 to 10 and under heat treatment at $100^{\circ}C$ for 30 min. Emulsification activity was also hardly influenced by pH. The critical micelle concentration (CMC) and surface tension at the point ($\gamma_{cmc}$) of the bioemulsifier were approximately 35 mg/l and 30 mN/m, respectively. The bioemulsifier showed a fairly good emulsification activity and stability in comparison with other commercial emulsifiers in the basic formula composed of emulsifier, oil, and water.

• Preventive Nutrition and Food Science
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• v.21 no.4
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• pp.338-347
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• 2016

The present study investigated the volatile compound, physicochemical, and antioxidant properties of beany flavor-removed soy protein isolate (SPI) hydrolyzates produced by combined high temperature pre-treatment and enzymatic hydrolysis. Without remarkable changes in amino acid composition, reductions of residual lipoxygenase activity and beany flavor-causing volatile compounds such as hexanol, hexanal, and pentanol in SPI were observed after combined heating and enzymatic treatments. The degree of hydrolysis, emulsion capacity and stability, 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity, and superoxide radical scavenging activity of SPI were significantly increased, but the magnitudes of apparent viscosity, consistency index, and dynamic moduli (G', G") of SPI were significantly decreased after the combined heating and enzymatic treatments. Based on these results, it was suggested that the enzymatic hydrolysis in combination with high temperature pre-treatment may allow for the production of beany flavor-removed SPI hydrolyzates with superior emulsifying and antioxidant functionalities.

• Asian-Australasian Journal of Animal Sciences
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• v.4 no.4
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• pp.407-410
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• 1991

The relationship between the possible structural change due to chemical modifications and functionality changes was studied in pigskin collagen. Amino groups in collagen were modified by succinylation and reductive alkylation. Carboxyl groups were modified using carbodiimide. Thermal denaturation temperature of collagen increased remarkably by carboxyl groups modification whereas decreased by succinylation and reductive alkylation. Emulsifying capacity was improved by reductive alkylation and carboxyl groups modification while emulsion stability was improved by succinylation. Chemical modifications increased solubility whereas decreased the foaming capacity of collagen. Viscosity of collagen at various pH varied with methods of modification.

• Preventive Nutrition and Food Science
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• v.2 no.1
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• pp.17-22
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• 1997

Casein was chemically modified with acetic, succinic, and maleic anhydride and changes in functional pro-perties were evaluated as affected by the degree of modification. Chemical modification resulted in casein with unique functional properties depending upon the type of anhydrid used and the degree of modification. It was possible to control heat coagulation, calcium precipitability, forming and emulsion capacity and stability. At pH 4.5 heat coagulation was 0% in the case 74.1% acetylated casein; on the contrary, succinylation and maleyation resulted in highly heat sensitive protein. Foaming properties were improved markedly by suc-cinylation and maleylation at pH 4.5. However, emulsifying properties were enhanced only by maleylation.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06a
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• pp.146-148
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• 2001

The objective of this study was to investigate the behavior of ribonuclease A (RNase) at the water/methylene chloride interface. It was aimed at better understanding the denaturation of proteins upon emulsification. RNase was vulnerable to the interface-induced aggregation reactions that led to formation of water-insoluble aggregates upon emulsification. Biochemical analyses demonstrated that intermolecular covalent linkages might have been involved in the aggregation reactions. The protein instability observed with emulsification was traced to consequences of protein adsorption and conformational rearrangements at the interface. These results indicated that emulsifying aqueous protein solutions in organic solvents should be handled with care, since emulsification could bring denaturation and aggregation to proteins.

• Journal of environmental and Sanitary engineering
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• v.11 no.3
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• pp.69-77
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• 1996

The result of isolated and selected to the strain having the emulsifying activity from soil's strain the strain was identified as Candida genus. The strain was investigated with culture condition at pH culture temperature, flow rate of air, strring rate etc., and physicochemical properties of the biosurfactant were examined. The optimum composition of medium for a strain cultivation were obtained as follow : glucose ; 100g/L, yeast extract ; 10g/L, urea ; 1.0g/L, KH$_{2}$PO$_{4}$ ; 50mg/L, MgSO$_{4}$ ; 500mg/L, and the op condition of cultivation was as follow : pH ; 3.0, temperatlue ; 24$\circ $C, strring rate ; 40rpm. The maximum yield of biosurfactant was obtained by pH ; 3.0-3.5, and temperature ; 25$\circ $C. The degree of emulsification of syntesized biosurfactant was increased clearly by increasing concentration of biosurfactant and it's stability was maintained for a long time. The surface tension of biosurfactant was varied with pH, especially it was showed that the surface tension was high at acidic pH.

• Preventive Nutrition and Food Science
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• v.3 no.2
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• pp.175-179
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• 1998

Some functional properties and nutritive value were determined for the protein concentrated fractionated from chrysanthemum flower in orer to renew interest in the flowers as food. Proximate components of chrysanthemum flower protein concentration (FPC) showed 61.2% protein, 2.0% fat and 35.2% carbhydrate on a dry basis. In amino acid composition of FPC, glutamic acid was the highest in the content, follwoed by aspartic acid, leucine and lysine. The ratio of essential/ total amino acids(E/T) was 0.42, showing a higher level of essential amino acids compared to the FAO reference protein. Digestibility of chrysanthemum FPC by pepsin and trypsin was lwoer than that of casein and was negatively correlative to both water and fat absorptions. Similar characteristics were determined between chrysanthemum FPC and milk casein in their emulsifying activity and emulsion stability. This results indicate that flowers or petals of chrysanthemum might be developed as a good source of protein.

• Journal of the Korean Applied Science and Technology
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• v.36 no.1
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• pp.174-188
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• 2019

The present study was carried out to investigate the emulsifying properties of heat-treated octenyl succinic anhydride(OSA) starch and the interfacial structure at oil droplet surface in emulsions stabilized by heat-treated OSA starch. First, the aqueous suspensions of OSA starch were heated at $80^{\circ}C$ for 30 min. Oil-in-water emulsions were then prepared with the heat-treated OSA starch suspension as sole emulsifier and their physicochemical properties such as fat globule size, surface load, zeta-potential, dispersion stability, confocal laser scanning microscopic image(CLSM) were determined. It was found that fat globule size decreased as the concentration of OSA starch in emulsions increased, showing a lower limit value ($d_{32}:0.31{\mu}m$) at ${\geq}0.2wt%$. Surface load increased steadily with increasing OSA starch concentration in emulsions, possibly forming multiple layers. In addition, fat globule sizes were also influenced by pH: they were increased in acidic conditions and these results were interpreted in view of the change in zeta potentials. The dispersion stability by Turbiscan showed that it was more unstable in emulsions at acidic condition. Heat-treated OSA starch found to adsorb at the oil droplet surface as some forms of membrane (not starch granules), which might be indicative of stabilizing mechanism of OSA starch emulsions to be steric forces.

• Journal of the Korean Applied Science and Technology
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• v.30 no.4
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• pp.635-648
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• 2013

This study was carried out to investigate the emulsifying properties of surface-active substances from defatted rapeseed cake by supercritical $CO_2$ extraction. Based on the interfacial tension data, a supercritical fluid extract (SFE) with the lowest value of 14.16 mN/m was chosen for evaluation which was obtained from No. 2 extraction condition (150 bar, $65^{\circ}C$, 250 g). For emulsions with SFE, some physicochemical properties (i.e., fat globule size, creaming stability, zeta potential etc) were investigated according to changes in SFE concentration, pH, and NaCl addition in an emulsion. It was found that fat globule size was decreased with increasing SFE concentration in emulsion, with showing a critical value at 0.5 wt%, thereby resulting in less susceptibility to creaming behavior. The SFE emulsion also showed instability at acidic conditions (pH<7.0) as well as by NaCl addition. This was coincided with zeta potential data of emulsion. In addition, SSL (sodium stearoyl lactylate) found to be suitable as a co-surfactant, as it helped considerably in decreasing fat globule size in emulsions and its optimum concentration to be over 0.03 wt%, based on 0.1 wt% SFE in emulsion.

• 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.