Lignin peroxidase functionalities and prospective applications
نویسندگان
چکیده
منابع مشابه
Lignin peroxidase functionalities and prospective applications
Ligninolytic extracellular enzymes, including lignin peroxidase, are topical owing to their high redox potential and prospective industrial applications. The prospective applications of lignin peroxidase span through sectors such as biorefinery, textile, energy, bioremediation, cosmetology, and dermatology industries. The litany of potentials attributed to lignin peroxidase is occasioned by its...
متن کاملLignin peroxidase structure and function.
Lignin peroxidase (LiP) plays a central role in the biodegradation of the plant cell wall constituent lignin. LiP is able to oxidize aromatic compounds with redox potentials higher than 1.4 V (NHE) by single electron abstraction, but the exact redox mechanism is still poorly understood. The finding in our laboratory that the Cbeta-atom of Trp171 carries a unique modification led us to initiate ...
متن کاملLignin Peroxidase Compound III
Lignin peroxidase compound III (LiPIII) was prepared via three procedures: (a) ferrous LiP + O2 (LiPIIIa), (b) ferric LiP + 0; (LiPIIIb), and (c) LiP compound II + excess HzOz followed by treatment with catalase (LiPIIIc). LiPIIIa, h, and c each have a Soret maximum at -414 nm and visible hands at 543 and 578 nm. LiPIIIa, b, and c each slowly reverted to native ferric Lip, releasing stoichiomet...
متن کاملLignin Peroxidase Of
Ligninase is a generic name for a group of isozymes that catalyze the oxidative depolymerization of lignin. Although undoubtedly produced by other lignin-degrading fungi, these isozymes to data have been isolated only from the basidiomycete Phanerochaete chrysosporium Burds. 1,2 These ligninases are extracellular and are produced during secondary metabolism, brought about by nutrient starvation...
متن کاملDirect interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium.
Binding properties of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium against a synthetic lignin (dehydrogenated polymerizate, DHP) were studied with a resonant mirror biosensor. Among several ligninolytic enzymes, only LiP specifically binds to DHP. Kinetic analysis revealed that the binding was reversible, and that the dissociation equilibrium constant was 330 micro...
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ژورنال
عنوان ژورنال: MicrobiologyOpen
سال: 2016
ISSN: 2045-8827
DOI: 10.1002/mbo3.394