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담자균으로부터 생산되는 균체 Laccases 및 이 효소의 유도특성
안드레 레오노비치 외 한국버섯학회 2004 한국버섯학회지 Vol.2 No.3
Laccases are multicopper-containing enzymes which catalyze the oxidation of phenolic and nonphenolic compounds with the concomitant reduction of molecular oxygen. They often occur as isoenzymes, either constitutive or inducible, that oligomerize to multilateral complexes, what allow for penetration to the woody cell wall structure. White rot basidiomycete fungi may produce a number of laccase isoenzymes, some constitutively and others after induction. Fungal laccase is commonly induced by many ions, such as Cu^(2+), Cd^(2+) Ca^(2+), Li^(+), Mn^(2+), Ag^(+), Hg^(2+), Mn and Fe^(3+), phenolic compounds, some organic compounds, such as ethanol, isopropanol, cAMP, caffeine, p-anisidine, viscosinamide and paraquat, and nitrogens and even heat shock. A combination of Cu and pHB (p-hydroxybenzoic acid) made it possible to extend the inducible laccase activities over 30-fold. But the most effective inducer of laccase in the basidiomycete and other higher fungi is 2,5-xylidine, over 160-fold stimulation of laccase activity. The laccases are frequently encoded by gene families, as e.g. in Pycnoporus cinnabarinus, from which the lcc3-1 or the allelic form lac1 and lac3-2 have been cloned and sequenced. In the case of inducible forms the post-inductional laccase formation depends upon the synthesis of mRNA and the induction is due to the synthesis of a new protein. Laccase는 여러개의 Cu를 포함하는 효소로서 분자상 산소를 환원시키면서 패놀성 및 비페놀성화합물의 산화를 촉매하는 작용을 한다. 이들 효소들은 미생물 고유의 혹은 유도상의 동위효소의 형태로 목질화된 세포벽을 침투하게 된다. 백색부후균은 많은 종류의 고유의 혹은 유도상의 동위효소를 생산한다. 이들 균체 laccase효소들은 통상 Cu^(2+), Cd^(2+) Ca^(2+), Li^(+), Mn^(2+), Ag^(+), Hg^(2+), Mn 및 Fe^(3+)이온과 같은 금속이온들, 페놀성 화합물, ethanol, isopropanol, cAMP, caffeine, p-anisidine, viscosinamide 및 paraquat 등과 같은 유기화합물, 질소 및 열충격 등에 의하여 유도될 수 있다. Cu 및 pHB (p-hydroxybenzoic acid)의 조합으로 laccase 활성을 30배이상 유도시킬 수 있었다. 여러 가지 inducer 가운데, 2,5-xylidine이 담자균 및 기타 다른 고등균류로부터 160배이상의 가장 효과적인 laccase의 유도효과를 나타냈다. 한편 laccase효소는 Pycnoporus cinnabarinus의 gene family로부터 자주 code로 표시되었는데, lcc3-1 혹은 lac1 및 lac3-2의 페어 gene으로 클론 및 시퀀싱되었다. 유도형 laccase의 경우 mRNA의 합성에 의존하여 laccase가 생성되며, 이러한 유도효과는 결국 새로운 단백질의 합성으로부터 기인된다.
Fungal laccases from basidiomycetes and their inducibility
Andrzej Leonowicz,A. Wilkolazka,J. Rogalski,Dong-Hoon Kim,Nam-Seok Cho 한국버섯학회 2004 한국버섯학회지 Vol.2 No.3
Laccases are multicopper-containing enzymes which catalyze the oxidation of phenolic and nonphenolic compounds with the concomitant reduction of molecular oxygen. They often occur as isoenzymes, either constitutive or inducible, that oligomerize to multilateral complexes, what allow for penetration to the woody cell wall structure. White rot basidiomycete fungi may produce a number of laccase isoenzymes, some constitutively and others after induction. Fungal laccase is commonly induced by many ions, such as Cu2+, Cd2+ Ca2+, Li+, Mn2+, Ag+, Hg2+, Mn and Fe3+, phenolic compounds, some organic compounds, such as ethanol, isopropanol, cAMP, caffeine, p-anisidine, viscosinamide and paraquat, and nitrogens and even heat shock. A combination of Cu and pHB (p-hydroxybenzoic acid) made it possible to extend the inducible laccase activities over 30-fold. But the most effective inducer of laccase in the basidiomycete and other higher fungi is 2,5-xylidine, over 160-fold stimulation of laccase activity. The laccases are frequently encoded by gene families, as e.g. in Pycnoporus cinnabarinus, from which the lcc3-1 or the allelic form lac1 and lac3-2 have been cloned and sequenced. In the case of inducible forms the post-inductional laccase formation depends upon the synthesis of mRNA and the induction is due to the synthesis of a new protein.
조남석,안드레레오노비취,리리아나지안프레다,죠오지로갈스키,마그다야색,욜란타루테렉,마리아바실레브스카,엘리지베타말라책,안드레다비도비취,모니카핑크브츠,그리지나기날스카,마그다스타스책 한국목재공학회 1997 목재공학 Vol.25 No.3
목재부후균으로부터 락케이스 효소의 생산 및 유도를 위하여 여러 가지 유도약품(inducer)을 사용하였다. 이들 가운데 ferulic acid, pentachlorophenol 및 2,5-xylidine이 매우 높은 락케이스 활성을 나타나게 하였으며 거의 동일한 유도효과를 보여주었다. 이들 약품 이외에도 sinapic acid syringic acid 및 coffeic acid 등도 높은 락케이스 활성을 주었는데, 산의 형태가 알데히드류보다도 높은 유도효과를 나타냈다. 그리고 실험한 48개 균주가운데 38개 균주가 락케이스를 생산하였으며, 이 가운데 32균주가 ferulic acid에 의해 강한 효소유도 활성을 보였다. 이러한 결과는 지금까지 락케이스 효소의 검출이 어려웠던 Abortiporus biennis 및 Gleophyllum odoratum에서도 높은 락케이스 효소의 유도를 가능하게 하였다. 아울러 가장 높은 효소활성을 나타낸 균주로서는 Cerrena unicolor 였으며, 그 락케이스 효소활성이 무처리 및 inducer 첨가시 각각 40,000 및 60,000 nkat/l 정도 였다.
Effect of Superoxide Dismutase and Low Molecular Mediators on Lignin Degradation
Cho, Nam Seok,Leonowicz, Andrzej,Matuszewska, Anna,Luterek, Jolanta,Ziegenhagen, Dirk,Wasilewska, Maria Wojtas,Hofrichter, Martin,Rogalski, Jerzy 한국목재공학회 1999 목재공학 Vol.27 No.4
As the biodegradation of wood constituents has been understood as a multi-basidiomycetes and enrymatic processes, this review will focus on the roles of low molecular compounds and radicals working in harmony with fungal enzymes. Wood rotting basidiomycete fungi penetrate wood, and lead to more easily metabolize carbohydrates of the wood complex. The white-rot fungi, having versatile enzymes, are able to attack directly the $quot;lignin barrier$quot;. They also use a multi-enzyme system including so-called $quot;feedback$quot; type enzymes allowing for simultaneous degradation of lignin and carbohydrates. The multi-enzymes including laccase support the proposed route by explaining how the high molecular weight enzymes can function in the wood complex. These enrymes may function separately or cooperate each other. In addition, veratryl alcohol oxidase, cellobiose dehydrogenase, arylalcohol dehydrogenase, and particularly low molecular mediators and radicals have an important role in wood biodegradation. However, the possibility of other mechanism as well as other enzymes, as operating as feedback systems in the process of wood degradation, could not be excluded.
An Immobilization of Extracellular Laccase to Humus - Iron Complex
Cho, Nam Seok,Leonowicz, Andrzej,Ginalska, Grazyna,Lobarzewski, Jerzy,Piccolo, Alessandro 한국목재공학회 2001 목재공학 Vol.29 No.3
There are some evidence that active enzymatic proteins, e.g. fungal laccase, exist in the naturally occured soil humus. This study was performed to investigate the covalent binding of fungal lactase to the humic acid-iron complex, and to measure lactase activity of immobilized ones. Seven methods were adopted to form the covalent binding of fungal lactase with soil humic acids complexed with iron. Using these seven methods it was possible to change the dimension of spacer arm between lactase and support, and also to regulate the mode of covalent binding of this enzyme. The spacer arm was regulated from 2C to 11C. There was not observed any straight relationship between the spacer arm longitude and the lactase activity after immobilization, but the binding mode more effective than the former. Three out of the seven methods gave the high activity of immobilized lactase, and which active products of lactase immobilization was stable up to 10 days after the process. It is indicated that natural soil condition might be prevented the lactase activation by the toxic influence of some phenolic humic compounds. It was shown, for the first time, the possibilities to obtain the high activity of fungal lactase by binding to humic acids, and especially in complex with iron.