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Nghi, Do Huu,Ullrich, Rene,Moritz, Franco,Huong, Le Mai,Giap, Vu Dinh,Chi, Do Huu,Hofrichter, Martin,Liers, Christiane 한국응용생명화학회 2015 Applied Biological Chemistry (Appl Biol Chem) Vol.58 No.3
Three ascomycetous soft-rot fungi belonging to the family Xylariaceae were found to produce high levels of a p-nitrophenyl acetate-hydrolyzing activity during growth on lignocellulosic materials, i.e., wheat straw and beech wood chips. Accordingly, Kretzschmaria deusta, Morchella elata, Xylaria polymorpha were seemingly most noteworthy acetyl esterase producers and, of which, X. polymorpha (strain A35) was chosen for further studies. Induction study indicated that raw carbohydrate sources, such as beech wood, rape straw, birch wood, and wheat straw, were extremely important for acetyl esterase production. Acetyl esterase of X. polymorpha was produced in solid-state culture on wheat straw and purified by different steps of anion-exchange and size-exclusion chromatography. This purified enzyme ($M_W=44kDa$ and pI values of 3.5-3.6) exhibited the capability to solubilise in vitro beech wood to release water-soluble lignin fragments with molecular masses of 1-3 kDa as analyzed by high performance size exclusion chromatography.
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.
Do Huu Nghi,Rene´ Ullrich,Franco Moritz,Le Mai Huong,Vu Dinh Giap,Do Huu Chi,Martin Hofrichter,Christiane Liers 한국응용생명화학회 2015 Applied Biological Chemistry (Appl Biol Chem) Vol.58 No.3
Three ascomycetous soft-rot fungi belonging to the family Xylariaceae were found to produce high levels of a p-nitrophenyl acetate-hydrolyzing activity during growth on lignocellulosic materials, i.e., wheat straw and beech wood chips. Accordingly, Kretzschmaria deusta, Morchella elata, Xylaria polymorpha were seemingly most noteworthy acetyl esterase producers and, of which, X. polymorpha (strain A35) was chosen for further studies. Induction study indicated that raw carbohydrate sources, such as beech wood, rape straw, birch wood, and wheat straw, were extremely important for acetyl esterase production. Acetyl esterase of X. polymorpha was produced in solid-state culture on wheat straw and purified by different steps of anion-exchange and size-exclusion chromatography. This purified enzyme (MW = 44 kDa and pI values of 3.5–3.6) exhibited the capability to solubilise in vitro beech wood to release water-soluble lignin fragments with molecular masses of 1–3 kDa as analyzed by high performance size exclusion chromatography.
( Christiane Liers ),( Rene Ullrich ),( Harald Kellner ),( Do Huu Chi ),( Dang Thu Quynh ),( Nguyen Dinh Luyen ),( Le Mai Huong ),( Martin Hofrichter ),( Do Huu Nghi ) 한국미생물 · 생명공학회 2021 Journal of microbiology and biotechnology Vol.31 No.10
A bifunctional glycoside hydrolase GH78 from the ascomycete Xylaria polymorpha (XpoGH78) possesses catalytic versatility towards both glycosides and esters, which may be advantageous for the efficient degradation of the plant cell-wall complex that contains both diverse sugar residues and esterified structures. The contribution of XpoGH78 to the conversion of lignocellulosic materials without any chemical pretreatment to release the water-soluble aromatic fragments, carbohydrates, and methanol was studied. The disintegrating effect of enzymatic lignocellulose treatment can be significantly improved by using different kinds of hydrolases and phenoloxidases. The considerable changes in low (3 kDa), medium (30 kDa), and high (> 200 kDa) aromatic fragments were observed after the treatment with XpoGH78 alone or with this potent cocktail. Synergistic conversion of rape straw also resulted in a release of 17.3 mg of total carbohydrates (e.g., arabinose, galactose, glucose, mannose, xylose) per gram of substrate after incubating for 72 h. Moreover, the treatment of rape straw with XpoGH78 led to a marginal methanol release of approximately 17 μg/g and improved to 270 μg/g by cooperation with the above accessory enzymes. In the case of beech wood conversion, the combined catalysis by XpoGH78 and laccase caused an effect comparable with that of fungal strain X. polymorpha in woody cultures concerning the liberation of aromatic lignocellulose fragments.
Nghi Do Huu,Kellner Harald,Büttner Enrico,Huong Le Mai,Duy Le Xuan,Giap Vu Dinh,Quynh Dang Thu,Hang Tran Thi Nhu,Verberckmoes An,Diels Ludo,Liers Christiane,Hofrichter Martin 한국응용생명화학회 2021 Applied Biological Chemistry (Appl Biol Chem) Vol.64 No.5
From the biotechnological viewpoint, the enzymatic disintegration of plant lignocellulosic biomass is a promising goal since it would deliver fermentable sugars for the chemical sector. Cellobiose dehydrogenase (CDH) is a vital component of the extracellular lignocellulose-degrading enzyme system of fungi and has a great potential to improve catalyst efficiency for biomass processing. In the present study, a CDH from a newly isolated strain of the agaricomycete Coprinellus aureogranulatus (CauCDH) was successfully purified with a specific activity of 28.9 U mg− 1. This pure enzyme (MW = 109 kDa, pI = 5.4) displayed the high oxidative activity towards β-1–4-linked oligosaccharides. Not least, CauCDH was used for the enzymatic degradation of rice straw without chemical pretreatment. As main metabolites, glucose (up to 165.18 ± 3.19 mg g− 1), xylose (64.21 ± 1.22 mg g− 1), and gluconic acid (5.17 ± 0.13 mg g− 1) could be identified during the synergistic conversion of this raw material with the fungal hydrolases (e.g., esterase, cellulase, and xylanase) and further optimization by using an RSM statistical approach.