Results 191 to 200 of about 29,422 (235)
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Laccases: a never-ending story
Cellular and Molecular Life Sciences, 2009Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a
GIARDINA, PAOLA +5 more
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Laccase and Laccase‐Mediated Systems in the Synthesis of Organic Compounds
Advanced Synthesis & Catalysis, 2014AbstractLaccase, a blue multicopper oxidase, has recently received considerable attention because of its usefulness in oxidizing phenolic and non‐phenolic compounds, as well as its suitability for organic synthesis, environmental pollutant treatment, and other biotechnological applications. This review covers recent studies on the structural properties,
Mehdi Mogharabi, Mohammad Ali Faramarzi
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World Journal of Microbiology and Biotechnology, 2006
Laccases (benzenediol oxygen oxidoreductases, EC 1.10.3.2) are polyphenol oxidases (PPO) that catalyze the oxidation of various substituted phenolic compounds by using molecular oxygen as the electron acceptor. The ability of laccases to act on a wide range of substrates makes them highly useful biocatalysts for various biotechnological applications ...
P. Sharma, R. Goel, N. Capalash
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Laccases (benzenediol oxygen oxidoreductases, EC 1.10.3.2) are polyphenol oxidases (PPO) that catalyze the oxidation of various substituted phenolic compounds by using molecular oxygen as the electron acceptor. The ability of laccases to act on a wide range of substrates makes them highly useful biocatalysts for various biotechnological applications ...
P. Sharma, R. Goel, N. Capalash
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Laccase — a Useful Enzyme for Modification of Biopolymers
2001Laccases are an interesting group of multi-copper enzymes, which have potential within various applications. They have surprisingly broad substrate specificities and can oxidize simple diphenols, polyphenols, diamines, and aromatic amines. Laccases oxidize their substrates by a one-electron transfer mechanism.
Kruus Kristiina +2 more
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Laccase fromPleurotus ostreatus
Biotechnology Letters, 1986Laccase was purified from culture broth ofPleurotus ostreatus mycelium. The enzyme was a single protein of Mr 59000, pI 2.9 and was active on o-diphenyl substrates. Amino acid composition and N-terminal sequence (15 residues) were determined. Polyclonal anti-laccase antibodies were obtained.
SANNIA, GIOVANNI +4 more
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Applied Biochemistry and Biotechnology, 1994
D. Schomburg, M. Salzmann, D. Stephan
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D. Schomburg, M. Salzmann, D. Stephan
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Laccase immobilization for water purification: A comprehensive review
Chemical Engineering Journal, 2021Wenxiang Zhang
exaly