• Title/Summary/Keyword: hGMP

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Study of Herb Manufacturers' Status in Implementing hGMP Operational Systems in South Korea (우수 한약 제조 및 품질 관리 기준 (hGMP) 시행을 위한 한약 제약 업소 현황 조사 연구)

  • Nam, Dong-Woo;Yang, Woong-Mo
    • The Journal of Korean Medicine
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    • v.32 no.4
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    • pp.111-127
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    • 2011
  • Objectives: The aim of this study was to establish a fundamental base for hGMP operational systems implementation. Method: The survey was done with a questionnaire developed through consulting specialists, in order to investigate the present state of manpower, facilities and capitalization of private enterprises, and opinions on what the road map for hGMP implementation must include. Results: The results showed that the business scales of related enterprises were relatively small. Education and health monitoring of employees has been done in fair amounts, but a standard must be established. Essential facilities required for herbal product production were present in most cases. Recognition and understanding of hGMP was low. Various opinions on the implementation of hGMP were gathered. Conclusion: Standardized hGMP education programs, plans to modify existing facilities, public announcements and advertisement of the system, and public assistance funds and tax privileges are needed for the successful implementation of the hGMP operational system.

Brevibacterium ammoniagense 융합균주의 GMP 생성

  • 김동만;임번삼;전문진
    • Proceedings of the Korean Society for Applied Microbiology Conference
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    • 1986.12a
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    • pp.522.1-522
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    • 1986
  • 5'-Xanthylic acid 생성균주인 Brevibacterium ammoniagenes ATCC 21263 R에 XMP에서 GMP로의 전환효소인 GMP synthetase활성을 부여하기 위해 동종간 세포융합을 시도하여 융합균주들을 얻었다. 이들 우량 융합균주들과 융합모균의 GMP synthetase 활성을 측정하여 상호 비교하였으며, pH 변화에 따른 GMP synthetase 활성과 GMP 생성량과의 관계를 검토하였다. 또한 최적 pH에서 균성장에 따른 당소모량과 GMP 생성량을 비교하였다.

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Production of 5균-GMP by Immobilized 5균-GMP Producing Fusant RC102 (5균-GMP 생산 융합균주 RC102의 고정화에 의한 5균-GMP 생산)

  • 이인선;조정일
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.24 no.5
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    • pp.779-784
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    • 1995
  • The effective production of 5'-GMP(5'-Guanylic acid) by immobilized 5'-GMP producing fusant RC102(intergeneric protoplast fusion between Brevibacterium ammoniagenes ATCC21263 and Corynebacterium glutamicum ATCC21171) was investigated. The Fusant RC102 was immobilized by entrapping in -carrageenan, agar, polyacrylamide or Ca-alginate. 3% k-carrageenan was selected as the most suitable matrix. In the production of 5'-GMP using the immobilized whole cells of fusant RC102, the optimum conditions were $32^{\circ}C$, pH 8.0, $30\mu\textrm{g}/L\;of\;Mn^{2+},\;1{\times}10^{-6}%\;of\;Zn^{2+}$. In order to use fermentation medium containing CSL(Corn Steep Liquor) plentiful in $Mn^{2+}$, the optimum conditions of penicillin G, D-cycloserine and POESA(polyoxyethylene stearylamine) for production of 5'-GMP were 0.8unit/ml, 0.8unit/ml, 0.8unit/ml and 5mg/ml, respectively. Cationic surfactant, POESA was effective and superior to the antibiotics, penicillin G or D-cyloserine in 5'-GMP productivity. The condinuous fermentation using immobilized fusant RC102 showed that 5'-GMP productivity was stable for more than 15 days.

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Purification of a major protein with physiological activities from Panax ginseng C. A. Meyer (고려인삼(Panax ginseng C. A. Meyer)에서 생리활성을 보이는 25 kDa 주요단백질 (GMP)의 분리정제)

  • Kwon, Taek-H.;Oh, Sei-R.;Park, H.;Kim, Kyung-H.
    • Applied Biological Chemistry
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    • v.41 no.6
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    • pp.410-413
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    • 1998
  • The major protein (GMP) from the roots of Panax ginseng C. A. Meyer was purified, using gel filtration and ion exchange chromatography followed by reversed-phase and ion exchange FPLC. Staining analysis indicated that the protein has a carbohydrate moiety, which was also shown by band shift experiments using various glycosidases. Electrophoretic and gel permeation studies showed that GMP has an apparent molecular weight of 63 kDa composed of possibly two subunits of 25 kDa containing carbohydrate moiety. GMP showed an anticomplementary activity on the hemolysis of red blood cells, which is a screening tool for inflammation mediator search.

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Production of Nucleotide by Immobilized Cell (고정화 미생물에 의한 뉴크레오타이드 생산)

  • CHO Jung-Il;JUNG Sung-Won
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.24 no.2
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    • pp.111-116
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    • 1991
  • The effective p.eduction of 5'-GMP(5'-Guanylic acid) by enzymatic conversion of 5'-XMP(5'-Xanthyic acid) was investigated. The Iyophilized Brevibacterium ammoniagenes ATCC 19216 which were used as the XHP aminase source, was immobilized by entrapping in K-carrageenan, agar, polyacrylamide or Ca-alginate. $3\%$ K-carrageenan was selected as the most suitable matrix. In the production of 5'-GMP using the free cells of 3. ammoniagenes ATCC 19216, the optimum conditions were $42^{\circ}C$, PH 7.0, 100mg/ml glucose, 120mg/ml cell ,8mg/ml $MgSO_4\cdot7H_2O$, 5mg/ml POESA, 5mg/ml phytic acid. Under the conditions, $94.5\%$ of 5'-GMP was converted within 8 hours. In the production of 5'-GMP using the immobilized whole cells of B. ammoniagenes ATCC 19216, the optimum conditions were $37^{\circ}C$, pH 7.5, 50mg/ml glucose, 1mg/ml $KH_2PO_4$, 10mg/ml phytic acid, 60mg/ml cell, 8mg/ml $MgSO_4\;\cdot\;7H_2O$, 5mg/ml POESA. Under the conditions, $64.7\%$ of 5'-GMP was converted within 40 hours.

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Fermentative Production of 5'-GMP from 5'-XMP by XMP aminase and ATP-generation System of Saccharomyces cerevisiae (효모 Saccharomyces cevevisiae의 ATP 생성계와 XMP aminase에 의한 5'-XMP로부터 5'-GMP 발효생산)

  • Cho, Jung-Il
    • The Korean Journal of Mycology
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    • v.21 no.4
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    • pp.285-292
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    • 1993
  • For the enzymatic conversion of 5'-XMP to 5'-GMP, partially purified XMP aminase from Escherichia coli was coupled with the yeast, Saccharomycrs cerevisiae, capable of ATP regeneration through glycolytic pathway. In order to elevate the level of XMP aminase in E. coli, $guaB^{-}(IMP\;dehydrogenase-less)$ mutant were introduced, and the yeast used as ATP supplier was treated by some method to increase its membrane permeability. The optimum conditions for efficient conversion reaction by energy-coupled system were investigated. As the results, a CH 41, $guaB^-$ mutant of E. coli K-12, showed 2.75 fold increase in the level of XMP aminase, compared with its parent cell. And the lyophylized yeast was the most effective at the ATP supplier. The optimum temperature and pH of conversion reaction were $40{\circ]C$ and pH 7.4, and the highest conversion ratio was shown under the reaction condition of 100 mM glucose, 100 mM inorganic phosphate and 6 mM AMP. When 36 units/ml XMP aminase used under the above conditions, the amount of 60 mg/ml yeast was sufficient to be used. Under the optimum condition, 71% of 1.8 mM(65.6 mg/100 ml) 5'-XMP was converted to 5'-GMP within 8 hr.

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A Study on the Thermal Stresses of the Glass Lens Mold Using in Progressive GMP Process (순차이송 GMP 방식용 유리렌즈 금형의 열응력에 관한 연구)

  • Chang, S.H.;Lee, Y.M.;Shin, G.H.;Yoon, G.S.;Jung, W.C.;Jung, T.S.;Heo, Y.M.
    • Proceedings of the Korean Society for Technology of Plasticity Conference
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    • 2007.10a
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    • pp.289-292
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    • 2007
  • To prevent the damage of glass lens molds and deterioration of glass lenses using in progressive GMP process, a thermal stress and a deformation of the glass lens molds at forming temperature should be considered in the design step. In this study, as a fundamental study to develop a multi cavity mold used in an aspheric glass lens molding, a heat transfer and a thermal stress analysis were carried out for the case of one cavity glass lens mold used in progressive GMP process. Finally, using analysis results, we estimated the thermal stress in a glass lens mold and predicted a modified height of guide ring that determines the forming height of a glass lens.

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Study on the Aspheric Glass Lens Forming Simulation in the Progressive GMP process (순차이송 GMP 공정에서의 비구면 유리렌즈 성형 해석에 관한 연구)

  • Chang, S.H.;Gang, J.J.;Shin, K.H.;Jung, W.C.;Heo, Y.M.;Jung, T.S.
    • Proceedings of the Korean Society for Technology of Plasticity Conference
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    • 2008.05a
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    • pp.539-542
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    • 2008
  • Recently, GMP(Glass Molding Press) process is mainly used to produce aspheric glass lenses. Because glass lens is heated at high temperature above Ty (yielding point) for forming glass, the quality of aspheric glass lens is deteriorated by residual stresses which are generated in a aspheric glass lens after forming. Before this study, as a fundamental study to develop forming conditions for progressive GMP process, compression, strain relaxation and thermal conductivity tests were carried out to obtain the visco-rigid plastic, the visco-elastic and thermal properties of K-PBK40 which is newly developed and applied for precision molding glass material, In this study, using the experimental results we obtained, a glass lens forming simulation in progressive GMP process was carried out and we could forecast the shape of deformed glass lenses and residual stresses contribution in the structure of deformed glass lenses after forming.

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Preparation of Yeast Extract from Waste Brewer's Yeast using Various Enzymes (각종 효소를 이용한 맥주 폐효모로부터 효모추출물 제조)

  • Lee, Ok-Hwan;Rhee, Seong-Kap;Son, Jong-Youn;Kim, Kyung-Im;Kim, Hyun-Duk;Lee, Boo-Yong
    • Korean Journal of Food Science and Technology
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    • v.34 no.5
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    • pp.867-872
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    • 2002
  • This study was performed to investigate the optimum process conditions for manufacturing yeast extract from waste brewer's yeast using various enzymes. Contents of IMP, GMP, free amino acids, and crude protein of yeast extracts were measured by enzymes treatment. Crude protein contents of yeast extracts subjected to cell wall digestion enzyme treatment were 21.1, 33.6, and 28.0% for the control grouup, glucanase (0.5%, 12 h), and tunicase (1%, 18 h), respectively. Crude protein contents of yeast extracts subjected to protease treatment were 22.0, 30.8, and 29.8% for control group, bromelin (1%, 3 h), and protamex (1%, 3 h), respectively. Crude protein content of yeast extract subjected to glucanase and protamex mixed treatment was 34.4%. The total contents of IMP and GMP of yeast extracts subjected to G+P+A (glucanase+phosphodiesterase+adenyldeminase) and G+Pro+P+A (glucanase+protamex+phosphodiesterase+adenyldeaminase) treatments were 1,066 and 1,047 mg/100 g, respectively. The content of free amino acids of yeast extract was the highest (2,302 mg/100 g) in G+Pro+P+A treatment. Optimum concentration and process condition of enzyme treatment to obtain yeast extract with high IMP, GMP, and free amino acid content were in the order of glucanase (0.5%, 12 h), protamex (1%, 3h), phosphodiesterase (0.1%, 3 h) and adenyldeaminase (1%, 1.5 h) treatments.