• Proceedings of the Korean Institute of Intelligent Systems Conference
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• 2002.12a
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• pp.473-477
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• 2002

세포내에서 특정 단백질이 합성되어 이용되는 것을 단백질의 발현이라 한다. 이러한 단백질의발현을 조사하는 작업은 세포내 대사과정을 밝혀내는 데 있어서 매우 중요한 역할을 담당하고 있다. 단백질의 발현을 조사하기 위해서는 세포로부터 추출하여 정제한 단백질이 어떤 단백질인지를 확인하는 작업이 필요한데 현재로써는 확인하고자 하는 단백질 효소로 분해하여 분해된 조각들의 질량을 측정하여 기존에 알려진 단백질들을 분해했을 때 이론상 나을 수 있는 조각들의 무게와 비교하여 가장 근접한 단백질을 찾아내는 질량분석기법(mass Spectrometry)이 널리 사용된다. 그러나 이 방법은 확인하고자 하는 단백질의 아미노산 서열이 알려져 있을 경우에만 사용할 수 있다는 한계점을 가지고 있다. 본 논문에서는 이러한 한계를 계산적인 방법으로 극복하고자 동일단백질을 여러가지 효소로 분해하여 나오는 조각들의 질량을 측정하고 이들을 조합하여 원래 단백질의 아미노산 서열을 알아낼 수 있는 알고리즘을 제안한다.

• Proceedings of the Membrane Society of Korea Conference
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• 1993.10a
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• pp.42-43
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• 1993

최근 특별한 기능을 갖는 단백질의 수요가 늘어남에 따라 단백질의 기능성을 개량하려는 연구가 활발히 이루어지고 있다. 이들 중 대표적인 것이 단백질을 단백질 분해효소로 처리한 가수분해물을 환자의 영양강화제와 같은 의약품이나 기능성이 요구되는 식량소재로서의 이용이다. 단백질의 효소적 가수분해에 있어서 회분식 공정은 장치가 간단하고 조작이 단순하며, 고 농도의 기질을 사용할 수 있지만 많은 양의 효소가 필요하며 높은 에너지와 노동력이 요구된다. 그리고 최종생성물의 저해작용으로 인해 수율이 적고 최종생성물의 기능적인 성질을 조절할 수 없는 단점이 있다.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.803-806
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• 1993

The properties of proteolytic enzymes from the fruit of Broussonetia Kazinoki Siebold were investigated. The protease activity of the enzymes from the fruit of Broussonetia Kazinoki Siebold was 1.6 unit. The optimum temperature and pH of the enzymes were $60^{\circ}C$ and 7.0, respectively. The enzymes were stable at pH values from 6 to 8 for 1 hr. at $37^{\circ}C$ of incubation and also retained all activity after incubation for 1 hr. at $60^{\circ}C$. The enzyme preparations showed strong activities toward hemoglobin and collagen.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.57-57
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• 1993

단백질 분해효소는 염증주변에 축적된 파괴조직이나 변성단백질등을 분해하여 염증, 특히 만성염증의 순환을 정상화함으로써 소염제로서 사용되어 왔으며 현재, Chymotrypsin, Trypsin, Promelain, Papain, Serrathiopeptidase, Pronase 등이 소염효소제로써 사용되고 있다. 이들은 주로 미생물 배양액에서 통상적인 방법으로 정제하여 사용하며, 유전자 재조합기술을 사용하여 재조합 균주에서 생산할 경우 그 생산성을 증대시킬수 있을 것이라 기대된다.

• Korean Journal of Microbiology
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• v.28 no.2
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• pp.162-168
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• 1990

The aims of the present study were to evaluate the effects of culture conditions on the biosynthesis of extra-cellular alkaline protease in Streptomyces sp. The formation of aerial mycelia and spores were compared with the protease production in order to know the relations between the alkaline protease and the cell differentiation. As results, it was found that substrate concentration was very critical to regulate the formation of the protease, aerial mycelia, and spores, which were resulted from the changes of culture pH to acid. When the culture pH was adjusted with phosphate buffer from pH 6 to pH 9, the alkaline protease production was increased as the culture pH increased whereas aerial mycelia and spore formation were reversely related to the culture pH. Therefore, it was thought that the culture pH was an important factor to regulate the alkaline protease synthesis.

• Parasites, Hosts and Diseases
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• v.35 no.1
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• pp.39-46
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• 1997

The present study was undertaken to determine whether live T. uaginnlis degrades human secretory IgA, serum If and IgG molecules. Human immunoglobulins were exposed to live trophozoites, parasite Iysate, and excretory-secretory product (ESP) of T ucginnlis. To determine the fragmentation of immunoglobulins, the reaction sample was subjected to SDS-PAGE and EITB, and peroxidase conjugated antihuman IgA and IgG were used as probes. Live trophozoites degraded secretory IgA, serum IgA and IgG, and degradation were pressed forward by the prolongation of the incubation time and by increasing the number of trichomonads respectively. Also the Iysates and ESP of trichomonads degraded IgA and IgG. The cysteine and serine proteinase inhibitors such as I-64, antipain, iodoacetic acid, iodoacetamide, TLCK reduced the ability of cleaving immunoglobulins. The proteinase activity and cytotoxicity of T. uaginnlis to HeLa cells were decreased when live T. vusinalis was treated with metallo-proteinase inhibitor as well as cysteine and serine proteinase inhibitors. These results suggest that proteinase secreted from live T ucginclis may play a part role in host pathogenesis by T. uosinnlis, and the cleaving ability of host immunoglobulins by the proteinase may contribute as a one of immune evasion mechanism for parasite survival in the host.

• The Microorganisms and Industry
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• v.13 no.3
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• pp.50-52
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• 1987

지난 10여년간에 걸쳐 급속히 발전한 유전공학 기술로 인해서 자연계에 존재하는 단백질이면 어느 단백질이나 그 유전자를 clone할 수 있게 되었으며, 그 유전자의 정확한 조작으로 원하는 단백질을 박테리아 등에서 대량 생산할 수 있게 되었을 뿐 아니라 최근 DNA 합성기술의 발달로 거의 무제한으로 유전자를 변형시킬 수 있게 되었다. 따라서 자연계에 존재하지 않는 새로운 단백질을 창제하고자 하는 기술인 단백질공학기술의 개발이 가능해진 것이다. 단백질공학기술은 실제로 무한한 응용성을 갖고 있는 기술로서 단백질의 구조및 기능을 연구하는 기본적인 문제점을 해결하는데 이용될 수 있을뿐 아니라 새로운 세대의 의약품이나 산업용 효소등을 비롯한 보다 경제적이고 생산성 높은 유용단백질의 설계에도 응용될 수 있다.

• Korean Journal of Food Science and Technology
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• v.43 no.6
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• pp.729-734
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• 2011

With the goal of transforming rice protein from an insoluble to a soluble form to increase the industrial utilization of rice wine meal (RWM), RWM was derivatized using commercial proteases and the RWM hydrolysates were characterized. Eight commercial proteases were used individually or in combination for hydrolysis of RWM. The degree of hydrolysis was assessed by determining the soluble protein in supernatant using the Lowry assay, protein in precipitates using a semimicro Kjeldahl procedure, and gravimetrically by the weight difference before and after hydrolysis. Protamex, Alcalase and Protease N proteases were most effective for hydrolysis of RWM. Although these assessment methodologies displayed some variation, they generally showed a similar pattern. When the aforementioned three proteases were simultaneously used to treat RWM, no significant difference was observed between the three assays (p<0.05) indicating an absence of enzymatic synergy.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.13-17
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• 1998

To improve extraction of insoluble proteins and functional properties of abolished proteins by protease. It was found that the optimum pH, optimum temperature, optimum treatment time and optimum unit of enzyme far extraction of protein were pH 9.0, $60^{\circ}C$, 8 hrs, 40 units. The foaming capacity and foaming satbility of sesame meal protein after treatment of enzyme were especially higher than control. The emulsion capacity and emulsion satbility of sesame meal protein were higher than control. Coil absorption as well as water absorption capacities of sesame meal protein were higher than control.

• Journal of Life Science
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• v.20 no.11
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• pp.1656-1661
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• 2010

Alkaline protease for the hydrolysis of egg yolk protein was immobilized on five carriers - Duolite A568, Celite R640, Dowex-1, Dowex 50W and Silica gel R60. Duolite A568 showed a maximum immobilization yield of 24.7%. Optimum pH for the free and immobilized enzyme was pH 8 and 9, respectively. However, no change was observed in optimum temperature ($50^{\circ}C$). Thermal stability was observed in immobilized enzymes compared to free enzymes. The immobilized enzyme retained 86% activity after 10 cycle operations in a repeated batch process. The effect of flow rate on the stability of enzyme activity in continuous packed-bed reactor was investigated. Lowering flow rate increased the stability of the immobilized enzyme. After 96 hr of continuous operation in a packed-bed reactor, the immobilized enzyme retained 83 and 61% activity when casein and egg yolk were used as a raw materials, respectively.