• 한국식품영양과학회지
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• 제45권9호
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• pp.1285-1292
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• 2016

분리콩단백질(SPI, soy protein isolate) 농도, pH, 전해질의 종류와 농도, alginates의 농도와 분자량이 SPI의 표면소수성에 미치는 영향을 조사한 결과는 다음과 같다. SPI 농도가 증가할수록 표면소수성은 감소하였다. SPI의 표면소수성이 pH 7.0에서 최대값을 나타내었다가 pH가 7.0을 기준으로 증가 혹은 감소함에 따라 표면소수성이 감소하는 경향을 나타내었다. SPI의 표면소수성은 NaCl의 농도가 100 mM까지 증가함에 따라 급격히 증가하지만 더 이상의 농도에서는 변화가 없었다. $CaCl_2$와 $MgCl_2$의 농도가 각각 50 mM과 30 mM까지 증가할수록 SPI의 표면소수성이 급격히 감소하였지만, 그 이상의 농도에서는 큰 변화가 없었다. Na-alginate의 농도와 분자량의 증가함에 따라 SPI의 표면소수성이 감소한 것으로 나타났다. Na-alginate의 분자량이 증가함에 따라 표면소수성의 증가속도가 감소하였다.

• 한국수산과학회지
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• 제54권4호
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• pp.543-551
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• 2021

Changes in gluten surface hydrophobicity, which play an important role in the functional characteristics of protein, were measured according to various protein concentrations, pH levels, electrolytes concentrations, and alginate molecular weights using 8-anilino-1-naphthalene sulfonic acid (ANS) as a fluorescent probe. Gluten surface hydrophobicity decreased as gluten concentration increased, reaching a maximum pH of 7.0. The effects of alginate molecular weights and alginate concentration on the surface hydrophobicity, emulsifying activity index (EAI), and emulsion stability index (ESI) of gluten-sodium alginate dispersion (GAD) were measured. Gluten surface hydrophobicity rapidly increased the asl NaCl concentration of gluten solution up to 300 mM and showed no significant increase above 300 mM. However, gluten surface hydrophobicity notably decreased until the concentration of CaCl₂ and MgCl₂ reached 30 mM, indicating no significant variations above 30 mM. GAD surface hydrophobicity increased as the concentration and molecular weight of sodium alginate increased, however, gluten concentration increased as the GAD surface hydrophobicity decreased. The EAI and ESI of GAD increased as both molecular weight and concentration of sodium alginate increased.

• 한국식품과학회지
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• 제25권5호
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• pp.571-575
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• 1993

대두 펩타이드의 표면소수도가 혈청 콜레스테롤의 농도에 미치는 영향을 조사하기 위하여, 대두 단백질(ISP), 카세인(CNP), 이들 단백질을 펩신으로 가수분해하여 pH에 따른 펩타이드 침전 획분들(SHT, SH8, SH6, SH4, CHT, CH6, CH5, CH4)을 흰쥐에 섭취시키고 혈청 콜레스테롤 농도 및 분변 스테로이드이 배설량을 측정하였다. 그리고 각 펩타이드의 표면소수도를 ANS 형광법 및 SDS 결합법으로 측정하여, 이들의 상관관계를 분석한 결과, 펩타이드의 ANS 표면소수도가 높아질수록 분변으로 배설된 스테로이드량은 증가하였으며(r=0.81), 혈청 콜레스테롤 농도는 낮아졌다.(r=-0.868). 그러나 SDS 표면소수도는 그들과 상관관계가 없었다. 또한 대두 단백질은 가수분해에 의하여 ANS 표면소수도가 증가하였다. 이상의 결과는 흰쥐의 담즙염이, 소화중 생성된 높은 표면소수도의 펩타이드와 결합하여 체외로 배출되므로서 대두단백질의 섭취에 의한 혈청 콜레스테롤 농도가 낮아짐을 시사하였다.

• 한국식품조리과학회지
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• 제6권3호통권12호
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• pp.9-15
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• 1990

Peanut prptein isolate was tested for the purpose of finding out the effect of pH, Sodium Chloride concentration and heat treatment on the solubility, surface hydrophobicity, foam expansion and foam stability. The solubility of peanut protein isolate was affected by pH and showed the lowest value at pH 4.5. When the peanut protein isolate was heated, the solubility decreased at pH 3 and pH 7 but at pH 9 solubility increased. At all pH range, solubility decreased as NaCl was added. The surface hydrophobicity of peanut protein isolate showed the highest value at pH 1.5. Generally, at acidic pH range the surface hydrophobicity was high, but at alkaline region, the surface hydrophobicity increased as the temperature increased. And when NaCl was added, the surface hydrophobicity was also increased. Foam expansion of peanut protein isolate was no significant difference among the values about pH. When the peanut protein was heated and NaCl was added, foam expansion was increased at pH 7. Foam stability was significantly low at pH 4.5 and foam stability was increased at acidic pH region below pH 4.5. At pH 7 and pH 9, heat treatment above $60^{\circ}C$ increased foam stability. When NaCl was added, foam stability was significantly increased at pH 3 and pH 7.

• Applied Biological Chemistry
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• 제33권1호
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• pp.52-61
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• 1990

단백질의 기능성을 높이고자 acetic anhydride(AA), succinic anhydride (SA) 및 maleic anhydride(MA)로 단백질을 acyl화 시켜 소수성과 기능성 변화를 측정하여 기능 특성과 소수성의 관계를 고찰한 결과, 단백질의 아미노산 잔기인 amino기와 sulfhydryl기의 acyl화에는 AA에 의한 수식율이 가장 높아 amino기의 89.5 % sulfhydryl기의 72.2 %가 수식되었으며 amino기가 sulfhydryl기 보다 쉽게 acyl화 되었다. Succinyl화 및 maleyl화에 의해 어류 단백질의 소수성은 감소 하였으나 acetyl화는 단백질의 소수성이 근육 단백질보다 높다. AA, SA 및 MA로 acyl화 되면 단백질의 용해도, 유화특성, 포말특성, 수분 흡수력 및 지방 흡수력이 크게 향상되었으며 근육 단백질이 농축 단백질보다 기능적 특성이 좋았다. 단백질의 소수성 감소와 용해도 증가는 높은 상관을 보였고 유화특성 및 포말특성은 단백질의 용해도와 깊은 관련이 있었으며 단백질의 소수성도 중요하였다. 단백질의 수분 흡수력은 용해도와 상관이 크나 소수성과는 큰 관계가 없었으며 지방 흡수력은 단백질의 용해도 보다는 소수성에 더 큰 영향을 받는다.

• BMB Reports
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• 제38권4호
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• pp.407-413
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• 2005

Calcium and zinc binding protein, calprotectin is a multifunctional protein with broad spectrum antimicrobial and antitumoural activity. It was purified from human neutrophil, using a two-step ion exchange chromatography. Since surface hydrophobicity of calprotectin may be important in membrane anchoring, membrane penetration, subunits oligomerization and some biological roles of protein, in this study attempted to explore the effect of calcium in physiological range on the calprotectin lipophilicity. Incubation of human calprotectin ($50\;{\mu}g/ml$) with different calcium concentrations showed that 1-anilino-8-naphthalene sulfonic acid (ANS) fluorescence intensity of the protein significantly elevates with calcium in a dose dependent manner, suggesting an increase in calprotectin surface hydrophobicity upon calcium binding. Our study also indicates that calcium at higher concentrations (6, 8 and 10 mM) induces aggregation of human calprotectin. Our finding demonstrates that the starting time and the rate constant of calprotectin aggregation depend on the calcium concentration.

• 한국식품조리과학회지
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• 제6권4호통권13호
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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.

• 한국식품조리과학회지
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• 제9권1호
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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 $80^{\circ}C$.

• 약학회지
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• 제35권6호
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• pp.461-465
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• 1991

Silica-based gel filtration chromatography has been used to characterize molecular weight of proteins. However, the molecular weight measured by this method was distorted by protein-silica interactions like hydrophobic and electrostatic forces. Therefore, we characterized protein-silica interaction using two forms of phytochrome (124 kDa) having different hydrophobicity and surface charge. PH and ionic strength affected the retention time of phytochrome suggesting that electrostatic force is the major interaction between protein and silica surface.

• 한국식품영양학회지
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• 제24권4호
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• pp.740-745
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• 2011

Ohmic heating uses electric resistance heat which occurs equally and rapidly inside food when an electrical current is passed throught. In this study, we observed the physical & chemical characteristics changes which occurs in soybean protein during heating denaturation by using ohmic and conventional heating. After the ohmic heating process, we could not find any change of the primary protein structure in the denaturated soy protein samples. However, the rate of imbibed water(RIW) of the ohmic samples was 2 times faster than that of the conventional samples. Also the ANS-surface hydrophobicity was decreased, which is very closely related to RIW. In the differential scanning calorimeter(DSC) analysis result, all 7S soyprotein fraction samples were completely denaturated by ohmic and conventional heating. However, the 11S samples were completely denatured only by ohmic heating. According to the DSC result, we decided that soyprotein was damaged by temperature and electrical current during ohmic heating. The damage of electrical current was a cause of the characteristic changes.