• 한국식품과학회지
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• 제22권3호
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• pp.343-349
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• 1990

pH를 달리한 수용액 및 농도를 달리한 염류수용액에서 들깨종실의 단백질과 phytate의 용해도를 측정하여 단백질로부터 phytate를 제거할 수 있는 조건을 검토하였다. 들깨종실단백질의 용해도는 pH4.0에서 가장 낮은 9.5%로 등전점을 보였고, 그보다 산성 또는 알칼리성쪽으로 갈수록 증가되었다. 반면에 phytate의 용해도는 pH5.0에서 가장 높았으며 그보다 산성 또는 알칼리성쪽으로 갈수록 감소되었다. NaCl 수용액을 처리하였을 때 단백질의 용해도는 pH $3.0{\sim}4.0$ 범위에서 가장 낮았고 pH 6.0 이상에서는 현저히 증가되었다. Phytate의 용해도는 pH$2.0{\sim}5.0$ 범위에서는 약 90%내외로 높았으나 pH6.0 이상에서는 급격히 감소되었다. $Na_2SO_3$ 수용액처리에서는 단백질 용해도가 $pH2.0{\sim}3.0$ 범위에서 가장 낮았고 phytate의 용해도는 $pH5.0{\sim}6.0$에서 최대치를 보였고, 3%의 경우는 전 pH 구간에 걸쳐서 낮았으나 5%와 7%에서는 전 구간에서 높았다. $CaCl_2$ 수용액처리에서는 단백질 용해도가 3% 수용액에서는 전 pH 구간에서 낮았으나 5%와 7%에서는 $pH5.0{\sim}10.0$에서 높은 값을 보였으며 phytate의 용해도는 $pH2.0{\sim}3.0$ 사이에서 최대값을 나타내고 pH4.0이상에서는 급격히 감소하였다. 이상의 결과에서 3% NaCl 용액을 사용하여 pH9.0에서 단백질을 추출하고 pH4.0에서 침전시켰을 때 단백질 수율이 좋고 phytate 잔존량이 가장 적어, 저(低)phytate 분리단백질을 만드는 가장 좋은 조건이었다..

• Bulletin of the Korean Chemical Society
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• 제29권2호
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• pp.347-351
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• 2008

Acetyl-CoA carboxylase (ACC) is an excellent candidate for antibiotics drug target, which mediates malonyl-CoA synthesis from acetyl-CoA through acetylation process. It is also involved in the committed step of fatty acid synthesis which is essential for living organisms. We have determined the three dimensional structure of C terminal domain of HP0371, biotin-carboxyl carrier protein of H. pyroli, in solution state using heteronuclear multi-dimensional NMR spectroscopy. The structure of HP0371 shows a flatten b-sheet fold which is similar with that of E. coli. However, the sequence and structure of protruding thumb are different with that of E. coli and the thumb shows different basis of structural rigidity based on backbone dynamics data.

• 한국자기공명학회논문지
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• 제9권2호
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• pp.74-92
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• 2005

The high resolution solution structure of MCP-3 was determined using multinuclear, multidimensional NMR spectroscopy with an expressed and $^{13}C-\;and\;^{15}N-labeled$ protein. The MCP-3 has a typical chemokine fold including 3 anti-parallel $\beta-sheets$, and a C-terminal helix, but it exists as a monomer in solution under the conditions where the structure was determined (2 mM, pH 5.1 at $30^{\circ}C$). Based on the structure and the amino acid sequence compared to other chemokines we propose that Ile20 and Leu25 in MCP-3 play key roles in the formation of N-loop (residues between the $2^{nd}$ cysteine and the I sheet) which has been implicated as a determinant of chemokine specificity. Additional receptor binding surface is supplied by the 40s loop (residues between the 2 and the 3 sheet) and the binding interface of the acidic N-terminal region of chemokine receptor to MCP-3 would resemble the dimerization interface of CC type dimer.

• 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.

• Journal of Animal Science and Technology
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• 제58권8호
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• pp.31.1-31.8
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• 2016

Background: Plasma protein hydrolysates have been shown to possess antioxidant activity. However, no report has yet to examine the antioxidant effects of injection of plasma protein hydrolysates on meat quality. Therefore, in this study, the effects of injection of hydrolysis plasma protein solution on meat quality and storability were investigated in porcine M. longissimus lumborum. Methods: Twelve pigs were randomly selected at a commercial slaughter plant and harvested. Dissected loins were injected with one of five solutions: C- control (untreated), T1- 10 mM phosphate buffer solution (PBS), T2- 10 mM PBS with 0.01 % butylated hydroxytoluene, T3- 10 mM PBS with 5 % plasma proteins, and T4- 10 mM PBS with 5 % hydrolysis plasma proteins. Results: T3 and T4 induced greater reduction in protein content of the loin muscle than other treatments. T2 resulted in the lowest pH as well as highest cooking loss. After a storage period of 3-7 days, both lightness and redness of meat were unaffected by all injection treatments. However, yellowness was significantly elevated by treatment with T4 relative to the control. T4 also resulted in the lowest shear force (a measure of meat toughness), suggesting improvement of texture or tenderness. Further, T4 resulted in the most stable TBARS values during storage, indicating that this treatment might retard rancidity in meat. Conclusion: Injection of porcine M. longissimus lumborum with hydrolysis plasma protein solution could improve overall pork quality, including tenderness and storability.

• Journal of Chest Surgery
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• 제23권6호
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• pp.1084-1089
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• 1990

Plasma protein concentration, plasma albumin concentration, hematocrit, and arterial blood gas tension were measured in 15 mongrel dogs undergoing heart transplantation with cardiopulmonary bypass. The hemodilution due to priming solution resulted in a 49% decrease in plasma protein concentration, a 57% decrease in plasma albumin concentration, a 46%a decrease in hematocrit. The measurements had returned to preperfusion values 1 hour after the end of cardiopulmonary bypass. The intraoperative changes in plasma protein and albumin concentration did not correlate with changes in alveolar-arterial oxygen tension gradients[D[A\ulcorner PO2]]. It is concluded that, in the absence of an increase in left atrial pressure, marked decrease in plasma protein concentration can be tolerated without the occurrence of pulmonary edema. And further study should be done to determine how to prepare an ideal priming solution.

• 한국자기공명학회논문지
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• 제23권1호
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• pp.33-39
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• 2019

Studies on the interactions of proteins with partner molecules at the atomic resolution are essential for understanding the biological function of proteins in cells and for developing drug molecules. Solution NMR spectroscopy has shown remarkably useful capability for investigating properties on the weak to strong intermolecular interactions in both diluted and crowded solution such as cell lysates. Of note, the state-of-the-art in-cell NMR method has made it possible to obtain atomistic information on natures of intermolecular interactions between target proteins with partner molecules in living cells. In this mini-review, we comprehensively describe the several technological advances and developments in the in-cell NMR spectroscopy.

• Biotechnology and Bioprocess Engineering:BBE
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• 제7권1호
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• pp.26-30
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• 2002

A droplet fractionation method was previously developed to concentrate a dilute nonfoaming protein solution. In that earlier study with invertase, it was demonstrated that droplets created by ultrasonic energy waves could be enriched up to 8 times that of the initial dilute invertase solution. In this study, a mixture of bromelain (a foaming protein) and invertase (a nonfoaming protein) is investigated as a preliminary step to determine if droplet fractionation can also be used to separate a non-foaming protein from foaming proteins. The foaming mixture containing bromelain is first removed by bubbling the binary mixture with air. After the foam is removed, the protein rich air-water interfacial layer is skimmed off (prior to droplet fractionation) so as not to interfere with the subsequent droplet production from the remaining bulk liquid, rich in non-foaming protein. Finally, sonic energy waves are then applied to this residual bulk liquid to recover droplets containing the non-foaming protein, presumed to be invertase. The primary control variable used in this droplet fractionation process is the pH, which ranged for separate experiments between 2 and 9. It was observed that the maximum overall protein partition coefficients of 5 and 4 were achieved at pH 2 and 4, respectively, for the initial foaming experiment followed by the post foaming droplet fractionation experiment.

• KSBB Journal
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• 제17권6호
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• pp.515-519
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• 2002

발아현미를 생산하기 위하여 현미를 물에 침지, 키토산을 젖산에 용해하여 침지, 키토산을 글루탐산에 용해하여 침지 하였으며, 발아시키지 않은 현미와 아미노산 및 총 단백질 함량을 비교 분석하였다. 키토산을 50 ppm 되게 5 mM glutamic acid에 용해하여 침지액으로 사용한 경우 가장 높은 alanine, serine, lysine, isoleucine, methionine 함량의 증진과 총 유리아미노산 함량의 증진을 보였다. 또한 total soluble protein의 함량은 발아하지 않은 현미에 비하여 발아한 현미가 모두 낮았다. 특히 CG구는 물발아나 CL 발아시 현저히 감소되던 serine의 함량을 오히려 증진시겼다. 모든 발아구에서 aspartic acid 함량은 현저히 감소하였다. 이는 발아 과정에 의해 aspartic acid가 alanine, lysine, isoleucine, methionine 등으로 전환된 것에 기인된 것이라 여겨진다. 이상의 결과를 종합하면 현미발아시 키토산을 글루탐산에 용해하여 침지액으로 사용하면 유용한 아미노산인 alanine, serine 및 필수아미노산인 lysine, isoleucine, methionine 함량을 현저히 증진시킬 수 있어 영양성이 보강된 발아현미를 얻을 수 있을 것으로 기대된다.

• 한국가금학회:학술대회논문집
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• 한국가금학회 2006년도 제23차 정기총회 및 학술발표회
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• pp.69-72
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• 2006

To investigate the manufacturing methods of surimi-like materials (SLM) from breast muscle of spent hen, the muscles were diced, chopped and washed with distilled water or sodium chloride solution at 0.1, 0.5 and 1% level and then washed with distilled water to extract myofibrillar protein. When used only distilled water to extract myofibrillar protein, washing was repeated 3 times followed by homogenization and centrifugation of breast muscle after each washing (CM; conventional method). Whereas, to extract myofibrillar protein using sodium chloride solution had sufficient to do 2 times washing by distilled water after 1 time washing by sodium chloride followed by homogenization and centrifugation of breast muscle after each washing (NM; new method). The both batter and cooked SLM gel from NM had significantly (p<0.05) lower redness compared with CM. Again, SDS-PAGE with sarcoplasmic protein fractions showed that the bands of phosphorylase had increased staining intensity in NM compared with CM. These results indicated that the brightness was related to sarcoplasmic protein fractions. SDS-PAGE with myofibrillar protein showed that the bands of myosin had increased staining intensity in NM compared with CM. Data implied that myofibrillar protein extraction with sodium chloride solution had the better adaptability for the breast muscle of spent hen then the commonly used distilled water method.