• Applied Biological Chemistry
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• 제32권4호
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• pp.321-326
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• 1989

탈지들깨종자박의 질소용해도는 $pH\;4.0{\sim}5.0$에서 최저수준을 보였으며, pH11.0에서는 92.3%로 최고용해도를 나타내었다. Phytate의 용해도는 pH 4.8에서 최고수준을 나타내었으며 $pH\;8.0{\sim}11.0$에서는 $9.4{\sim}8.3%$로 낮은 값을 나타내었다. 원심력이 추출액 중의 질소량의 변화에 미치는 영향는 미미하였으나 phytate의 양과 혼탁도는 원심력의 증가에 따라 감소하다가 8,000 rpm 이상에서 거의 일정수준을 유지하였다. 추출온도의 상승$(5{\sim}60^{\circ}C)$에 따라 종자박의 졸소 및 phytate의 용해도는 증가하였으나 증가폭은 미미하였다. pH 0.5에서 $CaCl_2$의 첨가는 phytate의 용해도를 크게 감소시켰는데 $50mM\;CaCl_2$ 용액에서는 거의 0%에 가까운 용해도를 나타내었다. 들깨종자 분리단백질의 질소 및 phytate의 용해도는 pH의 상승에 따라 모두 증가하는 경향을 보였다. 그러나 pH 11.1에서 10mM $CaCl_2$ 첨가는 phytate의 용해도를 80.5%에서 약 10%로 감소시켰다. 탈지들깨종자박의 조단백질과 phytate 함량은 각각 60.1%와 5.0%였으며, 분리단백질은 각각 89.6%와 1.1%였다.

• Preventive Nutrition and Food Science
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• 제12권2호
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• pp.103-110
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• 2007

The protein profiles among Korean rice cultivars were assessed by total protein determination, solubility fractionation, SDS-PAGE analysis and scanning densitometry. In the extraction of protein, the SDS/urea system at a neutral pH was more efficient than that at alkaline pH. The determination of total protein showed that the protein content was similar among cultivars, ranging from 87.9 to 92.7 mg/g dry weight. Additionally, the water/NaCl-soluble protein fraction, containing 14${\sim}$16 kDa albumin and 22 kDa globulin ${\alpha}$-globulin, was also similar among cultivars, with a range of 9.94 to 11.98 mg/g dry weight. The SDS-PAGE/densitometry of total protein showed that there was no discernable difference in proteins of higher molecular weights among various cultivars, whereas the amount of lower molecular weight proteins (14${\sim}$16 kDa) is somewhat variable among cultivars. Furthermore, SDS-PAGE analysis of water/NaCl-soluble and propanol-soluble fractions indicates that there is a discernible change in the content of albumin, globulin or prolamin among cultivars. Thus, the PAGE/densitometry method, preceded by solubility fractionation, is useful for examining differences in protein profiles of rice cultivars.

• 한국식품과학회지
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• 제19권2호
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• pp.89-96
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• 1987

방어와 갈색띠 매물고둥에서 myosin과 paramyosin 을 추출하고, 이들 단백질의 가열중에 일어나는 변성기구를 아미노산 잔기와 SH기의 변화 및 단백질간의 상호작용 등을 측정하므로서 분석하였다. 각 단백질을 이루는 구성아미노산의 측쇄중 소수성 잔기의 유리정도는 가열온도 $65^{\circ}C$까지는 증가하였으나, 그 이상의 가열온도에서는 감소하는 경향을 보였다. 유리 소수성 잔기가 증가하여 감에 따라, 단백질간 상호작용도 활발하여 갔으며, 소수성 잔기의 유리정도가 감소하는 가열온도$65^{\circ}C$부터는 단백질의 응집이 일어나기 시작 하였다. 단백질간의 상호작용을 탁도로써 분석하여 Arrhenius식으로 해석한 결과, 방어 myosin은 3단계이상의 변성과정으로 구분할 수 있었으며, 갈색띠 매물고둥 paramyos은 2단계의 변성과정으로 구분할 수 있었다. 이들 두 단백질 소수성, 용해도, 유리 SH기의 수 및 단백질간의 상호작용 등은 온도함수와 밀접한 상관관계를 보였다.

• 한국식품조리과학회지
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• 제7권3호
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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 $100^{\circ}C$.

• 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.

• 한국자원식물학회지
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• 제11권3호
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• pp.272-278
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• 1998

This study was carried out to investigate the functional properties such as nitrogen solubility, emulsifying property , foaming capapcity , water and oil absorption of Camellia (Camellia japonica .) seed protein isolate in condition of distilled water and 0.5M NaCl solution at pH 2.0∼10.0. Nitrogen solubility of Camellia protein isolate in distilled water showed the minimum value at pH 4.0 and increased at pH lower or higher than the isoelectric point(pH 4.0). It was 90.0 %at pH 10.0 Nitrogen solubility of 0.5M NaCl solution showed a similar pattern with that of distrille dwater but was higher than that of distilled water except pH 2.0 and pH 10.0. Emulsifying activity of Camellia seed protein islate showed the minimum value at pH 4.0, but was higher at ether value of pH. Emulsifying stability of protein isolate was stable by heat treatment for 30min, at 80℃ and increased in 0.5M NaCl solution more than that of distille dwater. Foaming capacity of Camellia seed protein isolate in distill3ed water showed the minimum value near the isoelectric point, While it changed little at other values of pH. Foaming stability slowly decreased as, but didn't make a significant difference as time was delayed . Oil absorption was 1.4ml per a sample of 1g and water absorption was 0.9ml per a sample of 1g. The former was higher than the latter . The content of total amino acid of Camellia protein isolate was 43.67% and the major total amino acid of Camellia protein isolate was 43.67% and the major total amino acid was in the order of glutamic acid , arginine, aspartic acid, and leucine.

• 한국식품조리과학회지
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• 제7권2호
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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.

• Applied Biological Chemistry
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• 제36권2호
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• pp.121-126
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• 1993

참깨박에 함유되어 있는 불용성 형태의 단백질을 가용성 형태의 단백질로 용출시키기 위하여 Bacillus sp. CW-1121이 생성하는 효소를 작용시켰다. 이때 참깨박의 단백질 용출을 위한 최적 pH는 7.5였으며, 최적 온도는 $40^{\circ}C$였고 최적 조건하에서 2시간의 소화로 약 60%의 용해도를 보였다. 단백질의 용해도는 참깨 단백질이 pH4.5에서 가장 낮아 등전점을 보였고, pH3.0과 pH6.0 이상에서는 크게 증가하였다. 효소처리 참깨박 단백질을 전기영동한 결과 수용성 단백질은 4개, 염용성 단백질은 2개의 밴드가 관찰되었다. 분리 단백의 아미노산 조성은 수용성 단백질의 경우 serine이 17.24 mg/g, 염용성 단백질은 glutamic acid가 10.77 mg/g, 유리아미노산은 glutamic acid가 6.55 mg/g으로 가장 많이 함유되어 있었으며 특히 필수아미노산의 조성도 상당히 좋은 편이었다.

• 한국식품영양과학회지
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• 제24권4호
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• pp.619-624
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• 1995

Sesame protein concentrate(SPC) was prepared from defatted sesame flour(DSF) at several different pH(2.0, 7.0, 9.0, 11.0) for protein extraction. Some of their functional properties were determined in order to compare the effects of pH during preparation of concentrates. Compared with DSF, nitrogen solubility was markedly improved in all SPC, and SPC extracted at pH 11.0 showed the highest solubility at all pH leaves examined. Fatabsorption was increased in all SPC prepared, but water absorption was decreased as the extraction pH of protein increased. The emulsifying properteis and foaming properties of SPC were remarkably higher than DSF. As the extraction pH of protein was increased, the emulsion activity was also increased, but emulsion stability was decreased. SPC extracted at pH 7.0 showed the highest foaming capacity on the other hand, the highest foaming stability was shown in SPC extracted at pH 2.0. As the protein extraction pH increased, the viscosity of the protein solution was increased. SPC extracted at pH 11.0 showed highest viscosity at all protein concentrations tested.

• 한국식품과학회지
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• 제19권1호
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• pp.61-65
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• 1987

k-casein은 유단백질 분획으로 GMP를 포함하고있으떠 GMP는 sialic acid를 포함하고 있으므로 k-casein index로 sialic acid 가 사용될 수 있다. 탈지분유 분리 단백질 용해도는 칼슘카페인 보다 일반적으로 낮으므로 용매처리시 야기되는 k-casein의 손실과 저용해도와의 관계를 규명하고자 하였다. 특히 용매처리시 주요 stabilizing fraction k-casein의 손실 혹은 손상을 고려해야만 한다. 용매처리시 sialic acid 는 제1차 추출용매에 16.5%, 제2차 추출용매에 4.0%손실되어 전체 20.5%가 용매처리시 손실되었다. 또 사용한 메탄올의 농도가 증가할수록 sialic acid손실이 감소하여 sialic acid 손실은 메탄을분획보다 물분획에따라 좌우된 것 같다. 따라서 sialic acid를 함유한 분말 extracted solid의 feed back 실험 결과 10%첨 가시최대 용해도를 나타냈으며 유당은 용해도 변화에 기여하지 못하였다 결론적으로 탈지분유 단백의 저용해도 헌상은 용매처리시 k-casein의 가용성 물질 손실에도 일부 기인한 것으로 사료된다.