Journal ArticleDOI
Laccases: blue enzymes for green chemistry
TLDR
A brief discussion of laccases, a group of enzymes that work with air and produce water as the only by-product, and their uses span from the textile to the pulp and paper industries, and from food applications to bioremediation processes.About:
This article is published in Trends in Biotechnology.The article was published on 2006-05-01. It has received 1084 citations till now. The article focuses on the topics: Laccase.read more
Citations
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Journal ArticleDOI
Flavonoid oxidation in plants: from biochemical properties to physiological functions.
TL;DR: Flavonoid oxidation contributes to these chemical and biological properties and can lead to the formation of brown pigments in plant tissues as well as plant-derived foods and beverages.
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Enzyme immobilization: an update
TL;DR: This paper is a review of the recent literatures on enzyme immobilization by various techniques, the need for immobilization and different applications in industry, covering the last two decades.
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Laccases and their natural mediators: Biotechnological tools for sustainable eco-friendly processes
Ana Isabel Cañas,Susana Camarero +1 more
TL;DR: This work focuses on phenolic compounds related to lignin polymer that promotes the in vitro transformation of recalcitrant non-phenolic structures by laccase and are seemingly the natural mediators of laccases.
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Tetramethylpiperidine N-Oxyl (TEMPO), Phthalimide N-Oxyl (PINO), and Related N-Oxyl Species: Electrochemical Properties and Their Use in Electrocatalytic Reactions.
TL;DR: This review provides a comprehensive survey of the electrochemical properties and electrocatalytic applications of aminoxyls, imidoxylS, and related reagents, of which the two prototypical and widely used examples are 2,2,6,6-tetramethylpiperidine N-oxyl (TEMPO) and phthalimide N- oxyl (PINO).
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Recent developments and applications of immobilized laccase.
TL;DR: This work discusses the different methodologies of enzyme immobilization that have been reported for laccases, such as adsorption, entrapment, encapsulation, covalent binding and self-immobilization.
References
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Journal ArticleDOI
Multicopper Oxidases and Oxygenases
TL;DR: Copper sites have historically been divided into three classes based on their spectroscopic features, which reflect the geometric and electronic structure of the active site: type 1 or blue copper, type 2 (T2) or normal copper, and type 3 (T3) or coupled binuclear copper centers.
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Laccase: new functions for an old enzyme.
TL;DR: This work has focused on more recent reports on the occurrence of laccase and its functions in physiological development and industrial utility and the reports of molecular weights, pH optima, and substrate specificity are extremely diverse.
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Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation.
TL;DR: Laccase is capable of oxidizing both phenolic and non‐phenolic moieties of lignin but that the latter is dependent on the co‐presence of primary laccase substrates.
Journal ArticleDOI
Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers.
TL;DR: This work presents the first crystal structure of an active laccase containing a full complement of coppers, the complete polypeptide chain together with seven carbohydrate moieties, and a mechanism is presented to explain how laccases could tune their redox potential by as much as 200 mV.