• Korean journal of food and cookery science
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• v.9 no.1
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• pp.43-51
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• 1993

Buckwheat protein isolate was tested for the effects of pH, addition of sodium chloride and heat treatment on solubility, emulsion capacities, emulsion stability, surface hydrophobicity, foam capacities and foam stability. The solubility of buckwheat protein isolate was affected by pH and showed the lowest value at pH 4.5, the isoelectric point of buckwheat protein isolate. The solubility significantly as the pH value reached closer to either ends of the pH, i.e., pH 1.0 and 11.0. The effects of NaCl concentration on solubility were as follows; at pH 2.0, the solubility significantly decreased when NaCl was added; at pH 4.5, it increased above 0.6 M; at pH 7.0 it increased; and at pH 9.0 it decreased. The solubility increased above $80^{\circ}C$, at all pH ranges. The emulsion capacity was the lowest at pH 4.5. It significantly increased as the pH approached higher acidic or alkalic regions. At pH 2.0, when NaCl was added, the emulsion capacity decreased, but it increased at pH 4.5 and showed the maximum value at pH 7.0 and 9.0 with 0.6 M and 0.8 M NaCl concentrations. Upon heating, the emulsion capacity decreased at acidic pH's but was maximised at pH 7.0 and 9.0 on $60^{\circ}C$ heat treatment. The emulsion stability was the lowest at pH 4.5 but increased with heat treatment. At acidic pH, the emulsion stability increased with the increase in NaCl concentration but decreased at pH 7.0 and 9.0. Generally, at other pH ranges, the emulsion stability was decreased with increased heating temperature. The surface hydrophobicity showed the highest value at pH 2.0 and the lowest value at pH 11.0. As NaCl concentrationed, the surface hydrophobicity decreased at acidic pH. The NaCl concentration had no significant effects on surface hydrophobicity at pH 7.0, 9.0 except for the highest value observed at 0.8 M and 0.4 M. At all pH ranges, the surface hydrophobicity was increased, when the temperature increased. The foam capacity decreased, with increased in pH value. At acidic pH, the foam capacity was decreased with the increased in NaCl concentration. The highest value was observed upon adding 0.2 M or 0.4 M NaCl at pH 7.0 and 9.0. Heat treatments of $60^{\circ}C$ and $40^{\circ}C$ showed the highest foam capacity values at pH 2.0 and 4.5, respectively. At pH 7.0 and 9.0, the foam capacity decreased with the increased in temperature. The foam stability was not significantly related to different pH values. The addition of 0.4 M NaCl at pH 2.0, 7.0 and 9.0 showed the highest stability and the addition of 1.0 M at pH 4.5 showed the lowest. The higher the heating temperature, the lower the foam stability at pH 2.0 and 9.0. However, the foam stability increased at pH 4.5 and 7.0 before reaching $80^{\circ}C$.

• 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.

• 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.37 no.3
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• pp.345-351
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• 2005

Physicochemical properties and functionalities of sodium caseinate, whey protein, skim milk, and whole milk with or without transglutaminase (TGase, 200 : 1) at $38^{\circ}C$ were determined. After crosslinking by TGase, whey protein was effective in improving heat stability compared to native protein at over $70^{\circ}C$. Whole milk was stable with lower turbidity compared to native solution. Whey protein showed low hydrolysis degree, fewer than sodium caseinate, during early activation time and increased slightly thereafter Emulsifying activities of sodium caseinate at pH 2 and 8, and whey protein at pH 7 and 8 improved. Emulsion stability of sodium caseinate improved at entire pH range studied. Foam expansion and foam stability of samples improved with TGase-treatment. Viscosities of TGase-treated samples were higher than those of untreated ones.

• Korean Journal of Food Science and Technology
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• v.19 no.5
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• pp.409-413
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• 1987

Microcrystalline collagen was manufactured from raw pigskins and its functional properties were measured. It showed a thixotropic behavior. The maximum viscosity was obtained at pH 3.5 and the viscosity increased with the increase of concentration in a nonlinear manner. The increase in temperature decreadsed the viscosity while the effect of temperature was greater at pH below 4.5. Foaming capacity was similar to that of gelatin but superior to that of egg white at 1%. The foam stability was inferior to that of egg white. Emulsifying capacity was lower than that of pork. Values from physical and chemical analysis were somewhat different from those of medical-grade microcrystalline collagen made from bovine cerium collagen.

• Korean Journal of Food Science and Technology
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• v.9 no.2
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• pp.123-130
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• 1977

A laboratory study was made to develop a simple and economic model method for the systematic determination of functional properties of 'Soy Protein Isolates (SPI)' prepared from defatted soybean meal. These are required to evaluate and to predict how SPI may behave in specific systems and such proteins can be used to simulate or replace conventional proteins. Data concerning the effects of pH, salt concentration, temperature, and protein concentration on the functional properties which include solubility, heat denaturation, gel forming capacity, emulsifying capacity, and foaming capacity are presented. The results are as follows: 1) The yield of SPI from defatted soybean meal increased to 83.9 % as the soybean meal was extracted with 0.02 N NaOH. 2) The suitable viscocity of a dope solution for spinning fiber was found to be 60 Poises by using syringe needle (0.3 mm) with 15 % SPI in 0.6 % NaOH. 3) Heat caused thickening and gelation in concentration of 8 % with a temperature threshold of $70^{\circ}C$. At $8{\sim}12\;%$ protein concentration, gel was formed within $10{\sim}30\;min$ at $70{\sim}100\;^{\circ}C$. It was, however, disrupted rapidly at $125\;^{\circ}C$ of overheat treatment. The gel was firm, resilient and self-supporting at protein concentration of 14 % and less susceptible to disruption of overheating. 4) The emulsifying capacity (EC) of SPI was correlated positively to the solubility of protein at ${\mu}=0$. At pH of the isoelectric point of SPI (pH 4.6), EC increased as concentration of sodium chloride increased. Using model system$(mixing\;speed:\;12,000\;r.p.m.,\;oil\;addition\;rate:\;0.9\;ml/sec,\;and\;temperature\;:\;20{\pm}1\;^{\circ}C)$, the maximum EC of SPI was found to be 47.2 ml of oil/100 mg protein, at the condition of pH 8.7 and ${\mu}=0.6$. The milk casein had greater EC than SPI at lower ionic strength while the EC of SPI was the same as milk casein at higher ionic strength. 5) The shaking test was used in determining the foam-ability of proteins. Progressively increasing SPI concentration up to 5 % indicated that the maximum protein concentration for foaming capacity was 2 %. Sucrose reduced foam expansion slightly but enhanced foam stability. The results of comparing milk casein and egg albumin were that foaming properties of SPI were the same as egg albumin, and better than milk casein, particularly in foam stability.

• Journal of the Korean Applied Science and Technology
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• v.3 no.1
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• pp.65-71
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• 1986

Four amphoteric surfactants, 1-(N-alkyl-N,N-dimethyl ammonio)-4-naphthalene sulfonates, were prepared by the alkylation of 1-(N,N-dimethylamino)-4,naphthalene sulfonic acid with chloroalkanes such as 1-decylchloride, 1-tetradecyl chloride and 1-hexadecyl chloride. These quaternary ammonium compounds such as 1-(N-decyl-N, N-dimethylammonio)-4-naphthalene sulfonate, 1-(N-dodecyl-N,N-dimethylammonio)-4-naphthalene sulfonate, 1-(N-tetradecyl-N,N-dimethylammonio)-4-naphthalene sulfonate and 1-(N-hexadecyl-N,N-dimethylammonio)-4-naphthalene sulfonate could be separated by means of thin layes chromatography and column chromatography. The surface chemical properties such as surface tension, foaming power, foam stability, wetting efficiency and solubilizing effect for these four compounds were measured. Also critical micelle concentration and hydrophilic-lipophilic balance(HLB) were evaluated. These compounds showed good surface as O/W type emulsifying agent and detergent.

• Korean Journal of Food Science and Technology
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• v.26 no.2
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• pp.110-116
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• 1994

In order to study the effects of enzyme modification on the physico-chemical and functional properties of myofibrillar protein prepared from the frozen sardine, Sardinops melanostica, the protein was hydrolyzed with pepsin under the enzyme-substrate ratio 1:100 at $37^{\circ}C$ and pH 1.65 for 1, 4, 8, 12, and 24 hr, respectively. The properties of pepsin-modified sardine myofibriliar protein were determined. The extents of proteolysis with pepsin as a fuction of time was showed a typical enzyme hydorlysis curve with an initial region of 4 hour period followed by plateau region. The SDS-acrylamide slab gel electrophoresis patterns of pepsin-modified proteins showed mainly disappearances of minor protein bands, but no changes of main protein bands. The gel filtration patterns through Sephadex G-75 of sardine myofibrillar protein showed two big peaks and three small peaks. All the small peaks were disappearanced by proteolysis with pepsin in one hour. and during the period of proteolysis the fast big peak became gradually smaller and the late big peak eluted more slowly. By proteolysis, the emulsifying activity and emulsifying capacity of sardine myofibrillar protein were all decreased. The effects of pepsin-modification on emulsifying capacity were greater than those on emulsifying activity of protein. The aeration capacity of the protein was increased about 1.9 folds and the foam stability decreased to 0.6 folds of control by pepsin-modification. The pepsin-modified sardine myofibrillar proteins showed about 0.6 folds of heat coagulation and 1.4 folds of viscosity of control. The pH dependence of solubilities of sardine myofibrillar protein showed two isoelectric areas of pH 5 and 9. The pepsin-modified protein showed more clear pH dependences at the early stage but not at the late stage of proteolysis.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.5
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• pp.542-549
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• 1999

The hydrothermal extracts were produced from fish head and their functional properties were investigated. The extracts exhibited an antioxidative effect and synergistic effect with $\alpha$-tocopherol by measuring peroxide values. The $5\%$ solution showed more antioxidative effect than $1\%$ solution. The extracts showed cryopropective effect, but the effect was less than sucrose. The solubility of the extracts was over $70\%$ in the all range of pH, and its lowest solubility was shown in pH 3.0. The extracts exhibited an emulsifying activity less than sugar ester (EAI=34.72) and little higher than or similiar to egg white (EAI= 14.69). The extracts showed a relatively high foam activity. The osmolality of the hydrothermal extracts at $1.0\%$ concentration were 23$\~$31 mOsmole which were much lower than 317 mOsmole at $1\%$ NaCl.