• 제목/요약/키워드: Artificial enzyme

검색결과 98건 처리시간 0.024초

인공효소의 분자 설계 (The Molecular Design of Artificial Enzyme)

  • 김세권;전유진
    • 생명과학회지
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    • 제4권3호
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    • pp.92-101
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    • 1994
  • With the rapid development of bioorganic chemistry recently, a field of artificial enzymes has a great concern from the industrial point of view. A number of possibilities now exist ofr the construction of artificial enzymes. They must posses two structural entities, a substrate-binding site and a catalytically effective site. It has been found that producing the facility for substrate binding is relatively straightforward but catalytic sites are somewhat more difficult. Therefore, synthetic catalysts do not yet match all the properties of an enzyme, however, the design of catalysts has lead to very powerful effects. This article reviews the existing literature on the modeling of artificial enzymes using cyclodextrin, modified cyclodextrin and crown compounds.

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견 Fibroin의 효소분해에 관한 연구 I. 인공사료조성에 의한 Fibroin 분해율의 차이 (The Studies on Hydrolysis of the silk Fibroin by Proteolytic Enzyme, Bombyx mori 1. Effect of Various Compositions of Artificial Diet for Silkworms on the Fibroin-Hydrolyzing)

  • 이용우;송기언;마석일;남중희
    • 한국잠사곤충학회지
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    • 제17권2호
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    • pp.155-160
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    • 1975
  • 인공사료조성차이가 견층 fibroin의 효소분해에 미치는 영향을 구명코저 시험한 결과는 다음과 같다. 1. 인공사료육잠견의 fibroin효소분해율은 상엽육잠견에 비하여 낮은 수준에 있다. 2. 인공사료의 soybean meal함량과 견층 fibroin효소분해율과는 거의 상관이 없었으나 견층 sericin함유량과는 부의 상관이 인정되었다. 3. 인공사료의 sucrose함량과 견층 sericin함유량과는 부의 상관이 있었으나 견층 fibroin효소분해율과는 상관이 인정되지 않았다. 4. 인공사요 육잠견의 자웅별로 fibroin효소 분해율에서는 유의차가 없었지만 Sericin함유량은 자>웅이었다. 5. 인공사료 조성에 있어서 상엽분말을 8%함유한 구는 10%구와 8%구에 methionine을 첨가한 구에 비하여 fibroin효소분해율이 높았다. 6. 1령부터 3령까지 인공사료와 4 및 5령은 상엽사육잠견의 fibroin효소분해율은 전령 인공사료육잠견에 비하여 높았다.

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Purification of a Steroid $\triangle^1$-dehydrogenase from Arthrobacter simplex

  • BAE. MOO;MI-KYUNG LEE
    • Journal of Microbiology and Biotechnology
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    • 제3권3호
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    • pp.181-187
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    • 1993
  • Steroid $\Delta^1$-dehydrogenase which introduces a double bond into the 1, 2 positions of steroid ring A was purified from Arthrobacter simplex, an excellent biotransformer of hydrocortisone into prednisolone. Hydrocortisone-induced cells were disrupted by vigorous agitation with glass beads, and a solubilized enzyme was obtained after centrifugation at 100, 000$\times$g for 90 minutes. The enzyme was purified 123-fold in three steps of chromatographic procedures with 13% yield. The last step of testosterone-agarose affinity column decisively contributed to the successful purification. The molecular weight of the enzyme was estimated to be 98, 000 by SDS-PAGE and 100, 000 by gel filtration, indicating that this enzyme behaves as a monomer. The enzyme showed demands for artificial electron acceptor, and among the several reagents tested, phenazine methosulfate acted as the most effective electron acceptor. Subcellular distribution of this enzyme was studied by centrifugation experiment. Comparison of the enzyme activities in pelleted membrane and cytosol fractions suggests that the enzyme may be a weakly attached peripheral membrane protein in vivo. But considerable amounts of enzyme was solubilized without any additional treatments for membrane protein.

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Purification and Properties of Quinone Reductase

  • 신해용;심승보;장미;박종옥;김경순
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2000년도 추계학술발표대회 및 bio-venture fair
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    • pp.638-639
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    • 2000
  • Quinone reductase was purified to electrophoretic homogeneity from bovine liver by using ammonium sulfate fractionation, ion-exchange chromatography, and gel filtration chromatography. The enzyme utilized either NADH or NADPH as the electron donor. The optimum pH of the enzyme was pH 8.5, and the activity of the enzyme was greatly inhibited by $Cu^{2+}$ and $Hg^{2+}$ ions, dicumarol and cibacron blue 3GA. The enzyme catalyzed the reduction of several quinones and other artificial electron acceptors. Furthermore, the enzyme catalyzed NAD(P)H-dependent reduction of azobenzene or 4-nitroso-N,N-dimethylaniline. The apparent $K_m$ for 1,4-benzoquinone, azobenzene, and 4-nitroso-N,N-dimethylaniline was 1.64mM, 0.524mM and 0.225mM, respectively. The reduction of azobenzene or 4-nitroso-N,N-dimethylaniline by quinone reductase was strongly inhibited by dicumarol or cibacron blue 3GA, potent inhibitors of quinone reductase.

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Molecular Computing with Artificial Neurons

  • Michael Conrad;Zauner, Klaus-Peter
    • 정보과학회지
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    • 제18권8호
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    • pp.78-89
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    • 2000
  • Today's computers are built up from a minimal set of standard pattern recognition operations. Logic gates, such as NAND, are common examples. Biomolecular materials offer an alternative approach, both in terms of variety and context sensitivity. Enzymes, the basic switching elements in biological cells, are notable for their ability to discriminate specific molecules in a complex background and to do so in a manner that is sensitive to particular milieu features and indifferent to others, The enzyme, in effect, is a powerful context sensitivity pattern processor that in a rough way can be analogized to a neuron whose input-output behavior is controlled by enzymatic dynamics.

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Production of D-Xylonic Acid from Hemicellulose Using Artificial Enzyme Complexes

  • Lee, Charles C.;Kibblewhite, Rena E.;Paavola, Chad D.;Orts, William J.;Wagschal, Kurt
    • Journal of Microbiology and Biotechnology
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    • 제27권1호
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    • pp.77-83
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    • 2017
  • Lignocellulosic biomass represents a potentially large resource to supply the world's fuel and chemical feedstocks. Enzymatic bioconversion of this substrate offers a reliable strategy for accessing this material under mild reaction conditions. Owing to the complex nature of lignocellulose, many different enzymatic activities are required to function in concert to perform efficient transformation. In nature, large multienzyme complexes are known to effectively hydrolyze lignocellulose into constituent monomeric sugars. We created artificial complexes of enzymes, called rosettazymes, in order to hydrolyze glucuronoxylan, a common lignocellulose component, into its cognate sugar ${\small{D}}$-xylose and then further convert the ${\small{D}}$-xylose into ${\small{D}}$-xylonic acid, a Department of Energy top-30 platform chemical. Four different types of enzymes (endoxylanase, ${\alpha}$-glucuronidase, ${\beta}$-xylosidase, and xylose dehydrogenase) were incorporated into the artificial complexes. We demonstrated that tethering our enzymes in a complex resulted in significantly more activity (up to 71%) than the same amount of enzymes free in solution. We also determined that varying the enzyme composition affected the level of complex-related activity enhancement as well as overall yield.

Biodegradation of Hydrocarbon Contamination by Immobilized Bacterial Cells

  • Rahman Raja Noor Zaliha Abd.;Ghazali Farinazleen Mohamad;Salleh Abu Bakar;Basri Mahiran
    • Journal of Microbiology
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    • 제44권3호
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    • pp.354-359
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    • 2006
  • This study examined the capacity of immobilized bacteria to degrade petroleum hydrocarbons. A mixture of hydrocarbon-degrading bacterial strains was immobilized in alginate and incubated in crude oil-contaminated artificial seawater (ASW). Analysis of hydrocarbon residues following a 30-day incubation period demonstrated that the biodegradation capacity of the microorganisms was not compromised by the immobilization. Removal of n-alkanes was similar in immobilized cells and control cells. To test reusability, the immobilized bacteria were incubated for sequential increments of 30 days. No decline in biodegradation capacity of the immobilized consortium of bacterial cells was noted over its repeated use. We conclude that immobilized hydrocarbon-degrading bacteria represent a promising application in the bioremediation of hydrocarbon-contaminated areas.

Changes of Enzyme Activities and Compositions of Abnormal Fruiting Bodies Grown under Artificial Environmental Conditions in Pleurotus ostreatus

  • Jang, Kab-Yeul;Cho, Soo-Muk;June, Chang-Sung;Weon, Hang-Yeon;Park, Jeong-Sik;Choi, Sun-Gyu;Cheong, Jong-Chun;Sung, Jae-Mo
    • Mycobiology
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    • 제33권1호
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    • pp.30-34
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    • 2005
  • This study investigated the biochemical changes of abnormal fruiting bodies grown under artificial environmental conditions in P. ostreatus. Abnormal mushroom growth during cultivation damages the production of good quality mushroom. This study showed that different environmental conditions produced morphological changes in the fruiting bodies of P. ostreatus. The fruiting bodies with morphological changes were collected and examined for differences in biochemical properties, enzyme activities, and carbohydrates composition. The enzyme activities assay showed that glucanase and chitinase activities decreased when the temperature was below or above the optimum cultivation temperature for P. ostreatus. The biochemical compositions of the abnormal mushroom were significantly different from the normal fruiting bodies. It was suggested that the changes in the biochemical composition of abnormal mushroom were caused by the unfavorable environmental conditions during mushroom cultivation.