Lignin-degrading enzyme system
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Lignin-degrading enzyme system

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Published by U.S. Dept. of Agriculture, Forest Service, Forest Products Laboratory in Madison, Wis .
Written in English


  • Cellulose,
  • Enzymes -- Analysis,
  • Lignin

Book details:

Edition Notes

StatementT. Kent Kirk
ContributionsForest Products Laboratory (U.S.)
The Physical Object
Paginationp. 139-150 :
Number of Pages150
ID Numbers
Open LibraryOL17952653M

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Lignin-degrading enzymes. Pollegioni L(1), Tonin F, Rosini E. Author information: (1)Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy; The Protein Factory, Centro Interuniversitario di Biotecnologie Proteiche, Politecnico di Milano, ICRM CNR Milano, Università degli Studi dell'Insubria Cited by:   Lignin degrading auxiliary enzymes are unable to degrade lignin on their own functions which need additional enzyme involvement for complete degradation (Janusz et al., ). Lignin degrading auxiliary enzymes enables the process of lignin degradation through the sequential action of several proteins that may include oxidative H 2 O 2 (Janusz Author: Adarsh Kumar, Ram Chandra. Lignin is a heterogeneous, phenolic and polydisperse biopolymer which resists degradation due to its aromatic and highly branched structure. Lignin is the most abundant renewable source of aromatic molecules on earth. The valorization of lignin could therefore provide a sustainable alternative to petroleum refineries for the production of valuable aromatic : Stefan Schoenherr, Mehrdad Ebrahimi, Peter Czermak. TY - CHAP. T1 - Lignin-degrading enzyme activities. AU - Chen, Yi Ru. AU - Sarkanen, Simo. AU - Wang, Yun Yan. PY - /8/ Y1 - /8/ N2 - Over the past three decades, the activities of four kinds of enzyme have been purported to furnish the mechanistic foundations for macromolecular lignin depolymerization in decaying plant cell by:

Lignin-degrading fungi and bacteria can produce primarily four major extracellular heme peroxidases, including lignin peroxidase (LiP, EC ), manganese-dependent peroxidase. Due to its aromatic nature and highly branched polymer network, lignin is rather inert towards degradation (Abdel-Hamid et al., ).Yet, to complete global carbon cycling, nature has evolved catabolic pathways since the time that plants started to produce lignin (Nelsen et al., ).White-rot fungi have developed a rich collection of extracellular oxidative enzymes to attack and degrade by: Lignin is the second most abundant natural substance in nature after cellulose and, annually, approximately 5 × 10 6 metric tons of lignin is produced industrially. Indeed, lignin is the most abundant renewable source of aromatic polymers on earth: its degradation is mandatory for carbon by: Lignin is found to be degraded by enzyme lignin peroxidases produced by some fungi like Phanerochaete chrysosporium. The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer involves Veratryl alcohol (Valc); which is a secondary metabolite of white rot fungi that acts as a cofactor for the enzyme. Structural studiesBRENDA: BRENDA entry.

Lignin-modifying enzymes (LMEs) are various types of enzymes produced by fungi and bacteria that catalyze the breakdown of lignin, a biopolymer commonly found in the cell walls of terms ligninases and lignases are older names for the same class, but the name "lignin-modifying enzymes" is now preferred, given that these enzymes are not hydrolytic but rather oxidative (electron. The isolation of lignin-degrading microbial strains may lead to the discovery of novel biocatalysts—peroxidases, laccases, and β-etherases—potentially useful for lignin valorization. The inherent heterogeneity of lignin, together with the sometimes difficult accessibility to representative amounts of it, may become a hurdle for using lignin as a carbon source for screening by: Open Library is an initiative of the Internet Archive, a (c)(3) non-profit, building a digital library of Internet sites and other cultural artifacts in digital projects include the Wayback Machine, and Despite the naturally evolved recalcitrance of lignin, select microbes have discovered enzymatic approaches to its depolymerization. The most active microbes with respect to lignin degradation identified to date are fungi, such as those belonging to the white-rot or brown-rot families that decompose wood [10, 11, 12].Lignin peroxidase (LiP) was the first lignolytic enzyme to be isolated from Cited by: