• 제목/요약/키워드: h-stable

검색결과 3,935건 처리시간 0.026초

클로렐라에서 바이너리 벡터를 이용한 hSCF와 hINFγ 단백질의 안정적인 발현과 효율적인 분비 (Stable Expression and Efficient Secretion of hSCF and hINFγ Protein using Binary Vectors in Chlorella vulgaris)

  • 정유정;민희경;이원영;김성천
    • 한국해양바이오학회지
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    • 제16권1호
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    • pp.45-54
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    • 2024
  • Microalgae have great potential in the biomedical and pharmaceutical industries as a new type of bioreactor that can produce proteins for specific purposes, including recombinant proteins, pharmaceuticals, and industrial enzymes. Despite the production advantages and importance of microalgae-based expression systems, studies on secretion efficiency are limited. In this study, for stable expression and efficient secretion of the heterologous protein (human SCF and human INFγ) in Chlorella vulgaris, we constructed SP:hSCF:His and SP:hINFγ:His plant binary vectors using the signal peptide (SP) of Chlamydomonas reinhardtii, and we obtained stable transformants through the effective agrobacterium-mediated transformation of these vectors. Transformants with accurately inserted hSCF and hINFγ demonstrated stably increased mRNA and protein expression using RT-PCR and western blotting under the same culture conditions. Following the analysis of the proteins secreted into the culture medium using ELISA, it was confirmed that hINFγ was effectively produced in the transformed C. vulgaris culture medium. The overall findings indicate that the combination of heterologous protein and SP may be crucial for ensuring the expression and secretion of recombinant proteins in Chlorella culture systems.

난황 항체의 안정성에 관한 연구 (Studies on the Stability of Hen′s Egg Yolk Immunoglobulins)

  • 이경애
    • 한국식품조리과학회지
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    • 제12권1호
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    • pp.54-59
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    • 1996
  • Immunoglobulins (IgY) were isolated from egg yolk of hens immunized with bovine serum albumin(BSA). The stability of anti-BSA IgY against heat and pH was investigated. Antibody activity was measured by enzyme linked immunosorbent assay. IgY was relatively heat-stable and most of the antibody activity remained after heating up 65$^{\circ}C$ for 30 minutes. IgY was stable at pH 5-11. However, inactivation of IgY was observed below pH 4, or above pH 12. Inactivation of IgY proceeded rapidly at low pHs(pH 2-3). Most of the antigen binding activity was lost at low pHs probably because of some conformational changes.

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울금의 색소 추출과 안정성에 관한 연구 (A Study on the Stabitity and Dyeing Condition in the Curcuma Longa L.)

  • 소황옥
    • 복식
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    • 제39권
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    • pp.79-89
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    • 1998
  • This study was carried out the effect of stability and color extract for it's condition in the curcuma L.. dyeing. The stability is to investigate the absorbance of the curcumin, one of the major yellow pigments and the stability regarding the effect of light, oxygen temperature and pH. The dyeing condition is compared the effect of mordanting condition and the best way to extract pigment and analysed through the color-fastness rating, color-difference value test. The main results obtained are summarized as follows ; 1.The best and proper solvent to extrect curcumin pigment was a ethanol and a distilled water. 2. The light effect indicated that the absorbances of solution in absence of ligh was more stable. 3. The oxygen(O2) effect to curcumin show-ed that the condition in the absence of O2 was more stable than that in presence of O2 4. The temperature showed that the absorbnace was best stable in4$^{\circ}C$ and less changed at $25^{\circ}C$ 5. The curcumin-etanol solution was stable in pH 2~4. 6. Generally color-fastness rating to silk, wool and cotton indicated that crocking C.F. and perspiration C.F. were more than 3rd grade and dry cleaning C.F. was more than 4th grade. But light color-fastness and washing color-fastness were very poor. 7. To make good color fastness, the mordan-ting treated group and the pre-mordant conditions were more effective than others 8. When compared with color-difference value test indicated that the silk was looks like more reddish and bluish color and than the wool and cotton were greenish and bluish. As a mordant, A(C2H4OH(COOH3) and D(K2Cr2O7)were more effective to make green-ish color in the silk and the reddish color was abtained by B(Al.K(SO4)2.12H2O) and C(FeSO4.7H2O).

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HOOCl-H2O Cluster의 구조와 결합에너지에 대한 ab initio 연구 (Ab Initio Study of the Structure and Binding Energy of HOOCl-H2O Cluster)

  • 김영미;성은모
    • 대한화학회지
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    • 제52권3호
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    • pp.322-327
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    • 2008
  • HOOCl-H2O cluster에 대하여 안정한 구조와 결합에너지를 MP2/6-311G(d,p), MP2/6-311G(2d,2p)의 방법으로 계산하였고 vibrational frequency계산을 하여 HOOCl의 vibrational frequency와 비교하였다. Skew HOOCl-H2O cluster가 가장 안정한 cluster로 나타났고 결합에너지는 46~48 kJ/mol 정도이며 trans HOOCl-H2O cluster의 경우도 이보다 불안정하나 비교적 큰 결합에너지를 갖는 것으로 나타났다.

Culture Conditions and Characterizations of a New Phytase-Producing Fungal Isolate, Aspergillus sp. L117

  • Lee, Dae-Hee;Choi, Sun-Uk;Hwang, Yong-Il
    • Mycobiology
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    • 제33권4호
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    • pp.223-229
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    • 2005
  • A novel fungal strain Aspergillus sp. L117 that produced acid-stable and thermostable phytase was isolated on basis of the clearing zone on PSM plate and the ability of Na-phytate hydrolysis. The phytase of isolate showed a 3-fold higher activity than that of A. ficuun NRRL3135. The Aspergillus sp. L117 produced maximal level of phytase at initial pH of 5.0 and $30^{\circ}C$. The optimal pH and temperature for phytase activity were 5.5 and $50^{\circ}C$, respectively. The phytase showed totally stable activity after 20 min of exposure between 30 and $90^{\circ}C$, and even at $100^{\circ}C$. The highest level of residual phytase activity was obtained at pH 5.5, and still retained the stability at the broadest pH ranges (2.0 to 7.0) of all the aforementioned phytases. Storage stability of phytase was preserved over 96% of initial activities for 60 days at 4, -20, and $-70^{\circ}C$ and to retain even 70% of the initial activity at room temperature.

꽃사과(Malus prunifolia Wild. Borkh. "Red Fruit")에서 에탄올 추출한 안토시안 색소의 안정성 (Stabilities of Anthocyanin Pigmenta obtained from Crab Apple (Malus prunifolia Wild. Borkh. "Red Fruit") by Ethanol Extraction)

  • 김용환
    • 한국식품영양학회지
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    • 제12권1호
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    • pp.85-90
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    • 1999
  • The characcteristics of anthocyanin pigments from crab apple (Malus prunifolia Wild. Borkh. "red fruit") by ethanol extract were investigated at various condition of light temperature sugar, organic acid me-tal ion and pH. The pigments were stable(over the 60%) on the light irradiation throughout 20 days sto-rage period at room temperature and in the pesenc of Al-foil red blue green and yellow cover were rage period at room temperature and in the pesence of Al-foil red blue green and yellow cover were very stable. The pigments also showed high thermal stbility(over the 67% at 115$^{\circ}C$ 10min) at pH2.5 respectively. The pigments with added organic acid greatly increased thickness of red color. The pig-ments with added metal ions at pH 2.5 such as Na+ K+, Mg2+ Ca2+ and Mn2+ were stable throughout 20 days storage period at $25^{\circ}C$. But Cu2+ addition showed the rapidly degradation of the pigments and Al3+ addition induced the color conversion from red to redish violet. The thickness of the red color of anthocyanin pigments increased increased as the pH decreased. These results indicated that crab apple antho-cyanin pigments might be potental source of natural food colorant. colorant.

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beta-Glucosidase를 생산하는 균주의 분리 및 조효소의 특성

  • 박석규;문일식;성낙계;최옥자
    • 한국미생물·생명공학회지
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    • 제21권5호
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    • pp.440-445
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    • 1993
  • The fungi SFN 416 strain which produced a stable beta-glucosidase was isolated from nature and identified to Aspergillus niger. Optimal conditions of enzyme reaction were temperature 36C, pH-5.0, reaction time-40 minutes. The enzyme was stable below 60C and in the range of pH 4.5-6.5. The enzyme was greatly inhibitied by Ag+ and slightly activated by Ca2+ (0.5mM) and Cu2+ (5 mM).

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Bacillus sp. GS가 생산하는 Xylanase의 정제 및 특성 (Purification and Characterization of Xylanase from Bacillus sp. GS)

  • 안준배;박헌국;이계호
    • 한국식품영양학회지
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    • 제7권1호
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    • pp.16-22
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    • 1994
  • Xylanase from Bacillus sp. GS was purified through acetone precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel filtration. The optimum reaction temperature of purified xylanase was 50t . Its optimum pH was between pH 6.0 and pH 6.5. This enzyme was stable below 5$0^{\circ}C$ for several hours and stable at between pH 5.5 and pH 8.0. The enzyme activity of xylanase was remarkably increased by Co++ and Cu++ ions. According to the study of hydrolysis mode of this enzyme, it was turned out to be ends type xylanase that can produce xylooligosaccharides, known as bifidogenic factor, from xylan.

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