• Proceedings of the Korea Information Processing Society Conference
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• 2005.11a
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• pp.513-516
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• 2005

단백질 2DE 이미지 분석의 주요작업은 스팟 매칭에 의한 동일한 종류의 단백질 그룹인 패어링 클래스를 구성하는 것으로서 단백질간의 상호 작용, 질병에 관련한 단백질의 변화 등을 관찰할 수 있다. 하지만 2DE 실험의 여러 가지 문제점으로 인하여 패어링 클래스는 먼지, 공기방울 등 에러를 포함하게 되며 이런 에러들은 왜곡된 분석결과를 초래한다. 따라서 본 논문에서는 동일한 조직에서 같은 종류의 단백질은 발현량이 비슷하다는 특성을 이용하여 패어링 클래스의 개개의 스팟을 참조 스팟 속성으로 나눈 값을 유사도로 정의하고, 스팟의 유사도가 사용자에 의하여 선택되는 필터링 배수에 의한 범위를 벗어날 때 에러 스팟으로 간주하여 제거되는 에러 필터링 기법을 제안한다. 실험에서는 정확도(Precision), 재현율(Recall) 및 조화평균(Harmonic-mean) 값을 사용하여 제안된 필터링 기법의 타당성을 보여준다.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.2
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• pp.165-169
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• 1999

Experiments were conducted to evaluate a experimental model developed for the protein removal by foam separation. The foam separator was operated in well-mixed tank which would be considered as a completely mixed condition. The feasibility of foam separation to remove protein from sea water was investigated. Protein removal characteristics of the foam separator were obtained by batch experiments. To find the effect of the operating parameter to protein removal rate, the foam separation was carried with variation of initial protein concentration and superficial air velocity. The result indicated that the protein removal efficiency was increased with increasing protein concentration and superficial air velocity. The relationship between operation parameters and protein removal rate were evaluated by non-linear regression as the form of exponential function, Using both relationships, the simplified model was determined. The simplified foam separator operation model was verified by the batch operation. The simulation results showed a good relationship with the experimental data.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.10a
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• pp.380-383
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• 2004

본 연구는 원유에서 지방을 제거한 탈지유의 pH를 5.5, 7.0, 8.5로 조정한 다음 TGase를 첨가하여 0, 1, 2, 4, 8시간 반응시킨 다음 단백질 입자들을 동결건조하여 조직의 성상에 대해 주사 전자 현미경을 이용해 관찰, 비교하였다. pH와 TGase를 처리하지 않은 원유의 탈지유는 단백질 입자들이 규칙적으로 회합해 있었다. 그러나 pH 조정 후 TGase를 처리한 다음 반응시간을 달리한 시료에서는 pH를 5.5로 조정한 시료에서 현저한 변화가 있었는데 그 변화 양상은 단백질 입자들이 0시간에서 조각을 이루워 회합되어 있다가 1시간 반응시킨 경우 단백질 입자들이 서로 결합하여 넓게 회합을 하였다. 2시간 반응시킨 경우 단백질 입자들이 다시 뭉쳐서 회합하였으며 4시간 반응시킨 경우 뭉쳐져 있던 단백질 입자들이 조그만한 구형 성상으로 넓게 회합하였다. 8시간 반응시킨 시료는 구형 성상으로 회합되어 있던 단백질 입자들이 사라지면서 다시 넓게 회합하는 것을 관찰할 수 있었다. pH 7.0과 8.5 조건하에서는 단백질 입자들이 조각 형태를 이루고 있었으며 반응시간이 증가할수록 입자들이 넓게 확대되는 현상을 나타냈다. 이와 같은 단백질들의 변화 양상은 pH와 TGase처리 그리고 반응시간에 영향을 받고 있는 것으로 사료된다.

• Korean Journal of Food Science and Technology
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• v.10 no.2
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• pp.162-172
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• 1978

We have studied to develop a process for the preparation of protein isolates free of isothiocyanate and oxazolidine-thione when defatted meal was extrracted with a cold alkaline solution at pH11.0. The rapeseed protein isolates were separated at $0^{\circ}C$ using 1% sodium algiante of 500 cps as a precipitation aid, also. The proteins had original colors, namely, a grey curd at pH 6.7, a light cream at pH 5.6 and a yellow cream at pH 5.0, The purity and the color was improved by washing with water and freez-drying with acetone, not at room temperature. A countercurrent procedure was a prerequisite for a continuous large scale production of protein isolates.

• Proceedings of the Korean Nutrition Society Conference
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• 2002.11a
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• pp.118-118
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• 2002

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 1998.06a
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• pp.432.1-433
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• 1998

• Korean Chemical Engineering Research
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• v.43 no.2
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• pp.187-201
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• 2005

Bioprocessing technologies utilizing 'biorecognition' between a solid matrix and a protein is being widely experimented as a means to replacing the conventional, solution-based technology. Frequently the matrices are chromatographic resins with specific functional groups exposed outside. Since the reactions of and interactions with the proteins occur as they are attached to the solid matrix, this 'solid-phase' processing has distinct advantages over the solution-phase technology. Solid-phase refolding of inclusion body proteins uses ion exchange resins to adsorb denaturant-dissolved inclusion body. As the denaturant is slowly removed from the micromoiety around the protein, it is refolded into a native, three-dimensional structure. Once the refolding is complete, the folded protein can be eluted by a conventional elution technique such as the salt-gradient. This concept was successfully extended to 'EBA (expanded bed adsorption)-mediated refolding,' in which the denaturant-dissolved inclusion body in whole cell homogenate is adsorbed to a Streamline resin while cell debris and other impurity proteins are removed by the EBA action. The adsorbed protein follows the same refolding steps. This solid-phase refolding process shows the potential to improve the refolding yield, reduce the number of processing steps and the processing volume and time, and thus improve the overall process economics significantly. In this paper, the experimental results of the solid-phase refolding technology applied to several biopharmaceutical proteins of various types are presented.

• Korean Journal of Food Science and Technology
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• v.32 no.1
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• pp.212-217
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• 2000

This study was determined protein reaction, antioxidative activity, nitrite scavening ability and antimicrobial activity of tannins isolated from astringent persimmon fruits. Tannins extracted from green persimmon fruits reacted highly with BSA(bovine serum albumin). Reactions between tannins and BSA were more active when contents of tannin were higher than that of BSA. Antioxidative abilities of green persimmon tannin were comparable to that of BHT(butylated hydroxytoluene). Green persimmon tannins exhibited remarkable nitrite-scavenging activity. Different antimicrobial activities of persimmon tannins were observed depending on the maturity. The growth of V. parahaemolyticus and E coil were highly inhibited by the addition of persimmon tannins. Tannins from soft persimmon did not have antimicrobial activities against B. subtilis and S. typhimurium.

• Korean Journal of Food Science and Technology
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• v.12 no.4
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• pp.263-271
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• 1980

Detoxified and deallergenized castor bean protein isolate was prepared from defatted castor bean pomace for use in animal feedstuffs and human foods. Succinylation and acetylation of the ${\varepsilon}-amino$ groups of the protein improved markedly the water solubility of the protein at $pH\;7{\sim}8$. The results of the amino acid analysis of the protein isolate revealed that the sulfur-containing amino acids and L-lysine were limiting amino acids and that succinylation and acetylation caused some little loss of the amino acid content. The L-methionine enriched plastein was synthesized from the protein isolate or the acylated protein isolates and DL-methionine ethyl ester by one step process with papain. By this method the extent of incorporation of L-methionine was about 50%. Pepsin hydrolyzed both unmodified and modified protein isolates at the same rate (about 92%). Tryptic hydrolysis, however, was less for the succinylated protein isolates (about 42%) and less for the acetylated protein isolates (about 26%). The protein efficiency ratio of L-methionine enriched protein isolate (about 2.5 weight %) was 90% that of reference casein. The protein efficiency ratio values of succinylated (88%) and acetylated (84%) protein isolate were 55 and 69% of reference casein, respectively.

• Korean Journal of Food Science and Technology
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• v.22 no.3
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• pp.343-349
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• 1990

The solubility of protein and phytate was measured at various pH's in distilled water and at various concentrations of NaCl, $CaCl_2\;and\;Na_2SO_3$ solutions, and then optimum condition for producing low phytate protein isolate from perilla flour was investigated. The protein solubility in water showed minimum at pH 4.0 and increased at pH higher or lower than 4.0, while phytate solubility was highest at pH 5.0 and decreased at pH higher or lower than 5.0. In NaCl solution, protein solubility was lowest between pH 3.0-4.0, while phytate solubility was high between pH 2.0-5.0 and abruptly decreased above PH 6.0. In $Na_2SO_3$ solution, protein solubility was lowest between pH 2.0-3.0 and phytate solubility showed maximum values between pH $5.0{\sim}6.0$, and it's solubility was low in 3% salt concentration at all pH ranges. In $CaCl_2$ solution, protein solubility in 3% salt concentration was relatively low at all pH ranges, and phytate solubility showed highest values between pH $2.0{\sim}3.0$ and abruptly decreased (1.0%) above pH 4.0. In order to make low phytate protein isolate, defatted perilla flour protein was extracted at pH9.0 and precipitated at pH 4.0 in 3% NaCl solution. The yield of low phytate protein isolate was 61.4% of total protein. This protein was found to contain 0.02% phytate by weight.