• 제목/요약/키워드: enzyme inducer

검색결과 97건 처리시간 0.028초

.betha.-1, 3-glucanase 생성균의 분리 및 효소 생성 조건 (Isolation of .betha.-1, 3-glucanase producing strain and cultural conditions of its enzyme production)

  • 정기택;방광웅;송형익;김재근;유대식
    • 미생물학회지
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    • 제24권3호
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    • pp.295-301
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    • 1986
  • The bacteria, which were capable of producing ${\beta}-1$, 3-glucanase inducibly by utilizing cell wall of Aspergillus fumigatus as a sole carbon source, were isolated from soil in the campus of Kyungpook National University. Among them, the strain which produced the enzyme excellently was selected and identified to be Pseudomonas stutzeri KF 13 by morphological, cultural and physiological examination. The optimal conditions for the enzyme production from Pseudomonas stutzeri KF 13 were investigated. the enzyme production was reached maximum state shen the broth cultured for 72hr at $30^{\circ}C$. And the enzyme showed the highest activity in the medium containing 3.5% cell wall as an inducer, 15% yeast autolysate as a nitrogen source and 0.05% $MnSO_4$ at pH 7.5.

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Flammulina velutipes에 의한 Laccase의 생산과 효소적 특성 (Production and Enzymatic Properties of Laccase from Flammulina velutipes)

  • 이재성;서달선
    • 한국균학회지
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    • 제13권2호
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    • pp.111-114
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    • 1985
  • The production of lac case by the funguson various media was studied. The characteristics of the enzyme were also studied regarding to the optimum pH, stability, Km value, and inactivation. The maximum activity of laccase reached the 40 days of incubation and the barley straw extract appeared to be a strong inducer for laccase. The enzyme showed stability at wide range of pH with optimum pH of 6.6. Temperature stability of the enzyme was high. Laccase was not inactivated by the organic solvents used for the precipitation. The enzyme, how­ever, was completely inactivated by trichloroacetic acid and sodium azide.

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변이주 Bacillus sp. A4442에 의한 갈락토스 전이활성이 높은 ${\beta}-Galactosidase$의 생산 (Production of ${\beta}-Galactosidase$ with High Transgalactosylation Activity by Bacillus sp. A4442 Mutant)

  • 최경호;양성준;김민홍;한금수;양지원;정진;인만진
    • Applied Biological Chemistry
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    • 제38권6호
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    • pp.507-511
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    • 1995
  • 토양으로부터 분리된 Bacillus sp.A1 균주는 가수분해활성보다는 전이활성이 훨씬 높은 ${\beta}-galactosidase$를 생산하기 때문에 산업적 응용 가능성이 있으나, glucose에 의한 catabolite repression을 보일 뿐만 아니라 lactose를 inducer로 요구한다는 결정적인 단점이 있어 갈락토올리고당의 제조에 직접 사용하기에는 적합하지 않았다. 따라서 galactose 전이효소의 생산성 제고를 꾀하기 위하여 N-methyl-N'-nitro-N-nitrosoguanidine를 이용한 3단계 변이를 시도하여 A4442변이주를 선발하였다. 이 변이주의 효소생산 능력은 괄목할 만큼 향상하였으며(약 20배 내외) catabolite repression과 lactose 요구성이 상당히 해제되었음을 확인하였다. 아울러 갈락토스가 새로운 inducer로 작용하는 것도 관찰하였다. 변이주를 이용한 발효시에 당의 농도와 배양액의 pH는 상호연관되어 효소의 생산에 영향을 끼쳤다. pH stat 기법을 이용하여 배양중 당의 농도를 0.5% 이하로 조절할 때 pH는 $6.5{\sim}7.5$ 범위내로 유지되었으며 효소활성은 $44\;unit/m{\ell}-broth$로 높게 나타났다.

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볶은 들깨박으로부터 암예방효소계 활성성분의 분획 (Fractionation of Anticarcinogenic Enzyme Inducer(s) from Roasted Perilla)

  • 홍은영;강희정;서명자;남영중;권정숙;김정상
    • 한국식품영양과학회지
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    • 제26권2호
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    • pp.193-197
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    • 1997
  • 볶은 들깨박에 존재하는 항암효소계 유도물질을 분리하기 위해 용매분획과 preparative TLC를 실시하여 이들에 대한 암예방지표효소인 quinone reductase와 AHH 유도활성을 조사하였다. 볶은 들깨박의 메탄올 추출물을 용매분획하여 QR을 측정한 결과 chloroform층에서 가장 높은 활성이 나타났다. 들깨박 메탄올 추출물을 TLC로 분리한 분획가운데 QR과 AHH유도활성은 F1$(R_{f}=0.8)$에서 가장 높았으며, 항산화능은 F1$(R_{f}=0.8)$과 F2$(R_{f}=0.7)$에서 가장 강한 것으로 나타나 QR유도성분과 항산화성분이 동일성분일 가능성이 높은 것으로 사료 된다.

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Enzymatic Degradation of Poly(${\gamma}$-glutamic acid) Hydrogel Prepared by ${\gamma}$-Ray Irradiation

  • Hara, Toshio;Choi, Seong-Hyun;Choi, Woo-Young
    • Journal of Microbiology and Biotechnology
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    • 제11권2호
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    • pp.342-345
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    • 2001
  • A bacterial strain PH-4, which produces an enzyme catalyzing the degradation of crosslinked poly(${\gamma}$-glutamic acid) hydrogels, was isolated and identified as a Flavobacterium sp. The enzyme was obtained by the sonication of the bacterial cells preincubated in a Bouillon medium with shaking, without adding of poly(${\gamma}$-glutamic acid) as an inducer. The products of the hydrogel degraded by the crude enzyme agreed closely with the depolymerized materials in SDS-polyacrylamide gel electrophoresis using methylene blue staining, and with a glutamic acid monomer on thin-layer chromatography, thereby suggesting that strain PH-4 produced a kind of exohydrolase.

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Serratia 배양에 의한 Serrapeptase 생성의 유도와 억제에 관한 연구

  • 노용택
    • 한국미생물·생명공학회지
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    • 제25권4호
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    • pp.408-413
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    • 1997
  • It was studied in order to improve the yield of serrapeptase production in fermentation that organic nitrogen sources play important roles not only as inducer, repressor and activator, but also nitrogen sources. From the investigation of the effect of Na-caseinate on the induction of serrapeptase production, it was elucidated that real inducer was leucine and strong repressor was cysteine, which were produced through hydrolysis of proteins. Serrapeptase production was strongly induced by Na-caseinate in culture time 12 hrs, but was weakly induced before and after that time. Therefore fed batch culture where partial amount of Na-caseinate is added in 12 hrs, is better than batch culture where total amount of Na-caseinate is added at the beginning. Cysteine, methionine, MgSO$_{4}$, and so on, sulfur-containing materials, repressed the serrapeptase production. In the addition of mineral salts, chlorinated salts is better than sulfated salts because of sulfur repression. The synergic effect of soybean meal with Na-caseinate on the serrapeptase production resulted from Mn$^{2+}$ contained in soybean meal, of which the optimal concentration is 4 mM in enzyme production.

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친화크로마토그래프법을 이용한 Cerrena unicolor laccase의 정제특성 (Purification of extracellular Cerrena unicolor laccase by means of affinity chromatography)

  • A. Leonowicz;L. Gianfreda;J. Rogalski;M. Jaszek;M.W. Wasilewska;E. Malarczyk;A. Dawidowicz;M. Fink-Boots;G. Ginalska;Cho, Nam-Seok
    • 펄프종이기술
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    • 제29권4호
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    • pp.7-17
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    • 1997
  • 균체가 생산하는 laccase 효소가 다방면으로 이용되면서, 이 효소를 균체로부터 대량으로 생산하고 분리.정제하여야 할 필요성이 대두되고 있다. 아울러 이 효소의 활성을 유도하기 위한 inducer 로서 2,5-xylidine 이 주로 사용되고 있는바, 이 xylidine 의 유독성이 인정되면서 사람에게 독성을 주지 않는 환경친화적 inducer의 검색이 필요하게 되었다. 본 연구에서는 백색부후균 Cerrena unicolor가 분비하는 laccase 효소의 유도를 위한 inducer로서 ferulic acid를 사용하였으며, 균체로부터 생산 및 분리된 laccase 효소의 정제특성을 구명코자 하였다. 본효소(constitutive enzyme)로서 I 및 II를, ferulic acid를 inducer로 사용한 경우 inducing 효소 III을 분리.정제하였다. 본 효소 I 및 II의 Michaelis 정수는 각각 737 M, 716 M 이었고, inducing효소 III은 167 M 로서, 기질에 대한 높은 친화성을 보여주고 있다. 분자량도 각각 65 kD, 63 kD 였으며, inducing효소 III은 59 kD 였다. 두효소 모두 15-19%의 당 및 단백질분자당 4M의 동(Cu)을 함유하고 있었다. 정제효율은 효소 I 및 II가 10.1%, 9.4% 였으며, III은 3.2% 였다. 모든 효소의 최적 pH 는 5.5였으며, 최적온도는 비교적 높은 $40^{\circ}C$였다.

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Production of 3-Ketosteroid-delta-1-Dehydrogenase by a Two-stage Continuous Culture

  • Ryu, D.Y.;Lee, B.K.;Thoma, R.W.
    • 한국미생물·생명공학회지
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    • 제2권1호
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    • pp.29-35
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    • 1974
  • We have studied the applicability of the principles and inherent advantages of the two-stage dontinuous uclture technique to an enzyme process for the purpose of improving and optimizing the productivity of 3-ketosteroid-delta-1-dehydrogenase. By using a two-stage continuous culture system, the growth st ageand enzyme produdtion stage are separated. In each stage an optimal set of toperaing conditions was determined, and this was tested for feasibility for the period of 10 days. During this period, at least 70% of the maximum enzyme productivity could be maintained. The important design parameters studied are: (1) optimal specific growth rate in the first stage which corresponds to the maximal cell productivity, (2) the optimal dilution rate in the second stage which in turn determines the size of second stage fermentor and the mean residence time of cells in the second stage, (3) cell concentration in both stages, add (4) the specific enzyme productivity and enzyme productivity of the second stage. In addition, by using two-stage continuous culture system we have been able to reduce or eliminate the effect of catabolite repression due to high medium concentration and the adverse effect of the solvent used to dissolve the inducer. We have found the balance between the opposing effects of induction and repression in the second stage judging from the observation that the enzyme productivity goes through a maximum.

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세균의 항생물질 내성에 관한 연구 Macrolide계 항생물질에 대한 유도 내성 Bacillus속 세균 (Studies on the Resistance to Antibiotics in Bacteria Induced Resistance to Macrolide Antibiotics in Bacillus sp.)

  • 최응칠;김병각;심미자;정경수;김혜령;이종길
    • 약학회지
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    • 제26권3호
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    • pp.169-174
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    • 1982
  • Several strains of bacteria having resistance to macrolide antibiotics were isolated. EMR-1, one of them, exhibited the induced resistance to macrolide antibiotics and this microorganism was identified as a bacterium belong to Bacillus species. The subinhibitory concentration of erythromycin or oleandomycin induced strong resistance to both erythromycin and oleandomycin themselves and to other macrolide antibiotics such as leucomycin, spiramycin and josamycin. The effective concentration of inducer, erythromycin was $0.0016-0.2\mu$g/ml. The inactivating enzyme of these antibiotics was not produced by EMR-1.

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Icaritin Preparation from Icariin by a Special Epimedium Flavonoid-Glycosidase from Aspergillus sp.y848 Strain

  • Wang, Zhenghao;Liu, Chunying;Yu, Hongshan;Wu, Bo;Huai, Baoyu;Zhuang, Ziyu;Sun, Changkai;Xu, Longquan;Jin, Fengxie
    • Journal of Microbiology and Biotechnology
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    • 제32권4호
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    • pp.437-446
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    • 2022
  • In this study, to obtain icaritin with high pharmacological activities from icariin, which has a content ratio of over 58% in the total flavonoids of Epimedium herb, a special Epimedium flavonoid-glycosidase was produced, purified and characterized from Aspergillus sp.y848 strain. The optimal enzyme production was gained in a medium containing 5% (w/v) wheat bran extract and 0.7% (w/v) Epimedium leaf powder as the enzyme inducer, and strain culture at 30℃ for 6-7 days. The molecular weight of the enzyme was approximately 73.2 kDa; the optimal pH and temperature were 5.0 and 40℃. The enzyme Km and Vmax values for icariin were 15.63 mM and 55.56 mM/h. Moreover, the enzyme hydrolyzed the 7-O-glucosides of icariin into icariside II, and finally hydrolyzed 3-Orhamnoside of icariside II into icaritin. The enzyme also hydrolyzed 7-O-glucosides of epimedin B to sagittatoside B, and then further hydrolyzed terminal 3-O-xyloside of sagittatoside B to icarisiede II, before finally hydrolyzing 3-O-rhamnoside of icarisiede II into icaritin. The enzyme only hydrolyzed 7-O-glucoside of epimedin A or epimedin C into sagittatoside A or sagittatoside C. It is possible to prepare icaritin from the high-content icariin in Epimedium herb using this enzyme. When 2.5% icariin was reacted at 40℃ for 18-20 h by the low-cost crude enzyme, 5.04 g icaritin with 98% purity was obtained from 10 g icariin. Also, the icaritin molar yield was 92.5%. Our results showed icaritin was successfully produced via cost-effective and relatively simple methods from icariin by crude enzyme. Our results should be very useful for the development of medicines from Epimedium herb.