• 제목/요약/키워드: laccase

검색결과 303건 처리시간 0.021초

Assembly of Laccase over Platinum Oxide Surface and Application as an Amperometric Biosensor

  • Quan, De;Kim, You-sung;Yoon, Kyung-Byung;Shin, Woon-sup
    • Bulletin of the Korean Chemical Society
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    • 제23권3호
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    • pp.385-390
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    • 2002
  • Laccase could be successfully assembled on an amine-derivatized platinum electrode by glutaraldehyde coupling. The enzyme layer formed on the surface does not communicate electron directly with the electrode, but the enzymatic activity of the surf ace could be followed by electrochemical detection of enzymatically oxidized products. The well-known laccase substrates, ABTS (2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)) and PPD (p-phenylenediamine) were used. ABTS can be detected down to 0.5 ${\mu}M$ with linear response up to 15 ${\mu}M$ and current sensitivity of 75 nA/ ${\mu}M.$ PPD showed better response with detection limit of 0.05 ${\mu}M$, linear response up to 20 ${\mu}M$, and current sensitivity of 340 nA/ ${\mu}M$ with the same electrode. The sensor responses fit well to the Michaelis-Menten equation and apparent $K_M$ values are 0.16 mM for ABTS and 0.055 mM for PPD, which show the enzymatic reaction is the rate-determining step. The laccase electrode we developed is very stable and more than 80% of initial activity was still maintained after 2 months of uses.

Demethoxylation of Milled Wood Lignin and Lignin Related Compounds by Laccase from White-rot Fungus, Cerrena unicolor

  • Leonowicz, A.;Rogalski, J.;Malarczyk, E.;Grzywnowicz, K.;Ginalska, G.;Lobarzewski, J.;Ohga, S.;Pashenova, N.;Lee, S.S.;Cho, Nam-Seok
    • Journal of the Korean Wood Science and Technology
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    • 제28권4호
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    • pp.29-40
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    • 2000
  • Highly purified Cerrena unicolor laccase (benzenediol:oxygen oxidoreductase, EC 1.10.3.2) caused the demethoxylation of milled wood lignin and several lignin related substances. The constitutive form of the enzyme produced extracellularly by C. unicolor fermenter culture was isolated and purified by ion-exchange chromatography on the DEAE-Toyopearl column and by affinity chromatography on a ConA-Sepharose and Syringyl-AH-Sepharose 4B columns. The enzyme was further immobilized on functionalized porous glass (CPG) and keratin coated CPG. The demethylating activity was monitored both by estimation of released methanol and by detection of the level of methoxyl groups (also in some water miscible solvents) after incubation of lignin materials with laccase preparations (free and immobilized). The effects of the incubation time and temperature on the demethoxylating activity of immobilized laccase preparations were also studied.

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Degradation of Lignosulfonate by Fungal Laccase with Low Molecular Mediators

  • Cho, Nam-Seok;Shin, Woon-Sup;Jeong, Seon-Wha;Leonowicz, A.
    • Bulletin of the Korean Chemical Society
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    • 제25권10호
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    • pp.1551-1554
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    • 2004
  • In the presence of laccase, low molecular weight (M.W.) fractions from lignosulfonate (M.W. 97 kD) were produced. By Sephadex column chromatography, four lower M.W. fractions of 9 kD, 1.8 kD, 1 kD and 0.85 kD were identified. The addition of acetovanillone (AV) or acetosyringone (AS) enhanced to the degradation of lignosulfonate with fungal laccase. During this process, there were found new generation of lower M.W. fractions, e.g. approximately 20 kD, 1.8 kD, 1 kD and 0.85 kD for AV, and 20 kD, 3 kD, 1 kD and 0.85 kD for AS, respectively. The quantities of lower M.W. products (especially the fractions of M.W. 1 kD and 0.85 kD) were larger than those in the controls. Also, its degradation became more active in the presence of AS than AV. The presence of AS or AV seems to prevent the re-polymerization of degraded lignosulfonate by the laccase.

액체배양한 Coprinus congregatus에서 세포막 연관 Iaccase의 생성 조절 (Regulation of membrane-associated laccase synthesis in liquid culture of Coprinus congregatus)

  • 최영옥;하은수;김순자;최형태;윤권상
    • 한국균학회지
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    • 제22권1호
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    • pp.46-49
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    • 1994
  • C. congregatus를 산성 액체배지(pH4.2)에 배앙할 경우 세포막연관 laccase가 배양 초기에 대량 합성분비되었으며 분비된 효소의 작용에 의하여 melanin색소가 중성배지에 비하여 빨리 생성되었고 배양 24시간 후에 배지의 산도는 pH5.2로 증가되었다. 이 효소의 합성은 transcription inhibitor인 5-fluorouracil에 의하여 크게 억제되었다.

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Biotechnological Approaches on Pulp and Papermaking Technology - Effect of New Mediator with Fungal Laccase on Degradation of Non-Phenolic Lignin Model Compound -

  • 조남석
    • 한국펄프종이공학회:학술대회논문집
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    • 한국펄프종이공학회 2010년도 춘계학술발표회 논문집
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    • pp.79-92
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    • 2010
  • In the presence of laccase, generation of monomeric aromatic acids from nonphenolic lignin model dimer veratrylglycerol-$\beta$-vanillate ether (VVE) was observed. The addition of acetovanillone (AV) or acetosyringone (AS) intensified this process, i.e. transformation was more extensive than in the experiments omitting mediators. Among the products isovanillic (IA) and vanillic (VA) acids were identified.

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버섯균류에서 산충격에 의한 Laccase의 유도 (Induction of laccases under acidic stresses in several mushroom-forming fungi.)

  • 김근숙;금잔디;최형태
    • 미생물학회지
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    • 제38권1호
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    • pp.54-56
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    • 2002
  • Induction of laccase isozymes under acidic stresses were determined in Trametes versicolor, Pleurotus ostreatus and Ganoderma lucidum isolated in Korea, and in Lentinus squarrosulrs isolated in Thai. When cultures of these fungi were transferred to acidic liquid media (pH 3.0-4.0), the activities of secreted extralcellular laccases were increased 60% and 400% in T. versicolor and G. lucidum respectively. However, there was no such induction in L. squarrosulus or P. ostreatus. In L. squarrosulus, different laccase isozymes in the electrophoretic mobilities were induced under acidic conditions.

Mediator-Assisted Biobleaching of Kraft Pulp by Laccase from Botrytis cinerea

  • Kim, Myungkil
    • Journal of the Korean Wood Science and Technology
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    • 제32권3호
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    • pp.52-58
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    • 2004
  • The use of N-hydroxyphthalimide (NHPI) as a mediator for laccase has proven to be comparable to N-hydroxybenzotriazole (HBT) for the delignification of kraft pulp, and the transformation of a number of industrial dyes. The advantages of NHPI derivatives are the biodegradation of these compounds compared to HBT, which has been shown to be recalcitrant in the environment, and the more reasonable cost of synthetic process.

Identification of Single Nucleotide Polymorphism Markers in the Laccase Gene of Shiitake Mushrooms (Lentinula edodes)

  • Kim, Ki-Hwan;Ka, Kang-Hyeon;Kang, Ji Hyoun;Kim, Sangil;Lee, Jung Won;Jeon, Bong-Kyun;Yun, Jung-Kuk;Park, Sang Rul;Lee, Hyuk Je
    • Mycobiology
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    • 제43권1호
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    • pp.75-80
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    • 2015
  • We identified single nucleotide polymorphism (SNP) markers in the laccase gene to establish a line-diagnostic system for shiitake mushrooms. A total of 89 fungal isolates representing four lines, including Korean registered, Korean wild type, Chinese, and Japanese lines, were analyzed. The results suggest that SNP markers in the laccase gene can be useful for line typing in shiitake mushrooms.

Pleurotus ostreatus의 laccase 작용특성 (Characterization of laccase from pleurotus ostreatus)

  • 김규중;신광수;맹진수;강사욱;하영칠;홍순우
    • 미생물학회지
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    • 제25권2호
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    • pp.148-156
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    • 1987
  • Extracellular laccase (E.C. 1.10.3.2) from the culture filtrate of Pleurotus ostreatus was purified by ammonium sulfate precipctation, protamine sulfate precipitation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel permeation chromatography. The molecular weight of the enzyme was estimated by SDS-polyacrylamide gel electrophoresis to be 58,000 and the isoelectric point was 3.75. The optimum temperature for the enzyme was about $45^{\circ}C$ and the optimum pH was 6.5. The enzyme was found to be stable at temperature below $35^{\circ}C$ and rapidly inactivated at higher temperatures. Km values for ferulic acid, vanillic acid, dihydroxyphenylalanine (DOPA) were 48.6.$\mu$M, 0.52mM, and 2.73mM, respectively, which indicates that the enzyme has much higher affinity towards ferulic acid. The reaction products of the enzyme were separated by TLC and HPLC.

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Laccase를 이용한 Triclosan의 처리 (Oxidative Transformation of Triclosan by Laccase)

  • 김영진
    • 한국환경보건학회지
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    • 제31권1호
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    • pp.61-65
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    • 2005
  • The oxidative transformation of triclosan with laccase from Trametes versicolor was conducted in a closed, temperature controlled system containing phosphate buffer for pH control. The optimum pH for triclosan transformation showed about 5. Despite the observation that elevated temperatures tended to inactivate the enzyme, increased transformation of triclosan was observed up to $50^{\circ}C$. Of the mediators studied, ABTS was most successful at enhancing triclosan transformation. About 80% of the toxicity of the initial mixture was reduced after the enzymatic treatment. In the presence of 1.0 mM of anions such as sulfite, sulfide, and cyanide, triclosan transformation was greatly inhibited. Chloride and fluoride ions exhibited inhibition of triclosan transformation at 25 mM. Ferric ion substantially inhibited triclosan transformation at 1.0 mM.