Results 151 to 160 of about 15,252 (200)
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“Blue” laccases

Biochemistry (Moscow), 2007
This review concerns copper-containing oxidases--laccases. Principal biochemical and electrochemical properties of laccases isolated from different sources are described, as well as their structure and mechanism of catalysis. Possible applications of laccases in different fields of biotechnology are discussed.
O V, Morozova   +4 more
openaire   +2 more sources

How to enjoy laccases

Cellular and Molecular Life Sciences, 2015
An analysis of the scientific literature published in the last 10 years reveals a constant growth of laccase applicative research in several industrial fields followed by the publication of a great number of patents. The Green Chemistry journal devoted the cover of its September 2014 issue to a laccase as greener alternative for chemical oxidation ...
PEZZELLA, Cinzia   +2 more
openaire   +3 more sources

Antioxidants determination with laccase

Talanta, 2007
The spectrophotometric method of antioxidants determination using recombinant laccase Polyporus pinsitus (rPpL) and Myceliophthora thermophila (rMtL) was developed. The method includes simultaneous oxidation of the antioxidant and high reactive laccase substrate producing chromophoric radical cation.
Juozas, Kulys, Irina, Bratkovskaja
openaire   +2 more sources

Thermotolerant and thermostable laccases

Biotechnology Letters, 2009
Laccases are phenol-oxidizing, usually four-copper containing metalloenzymes. For industrial and biotechnological purposes, laccases were among the first fungal oxidoreductases providing larger-scale applications such as removal of polyphenols in wine and beverages, conversion of toxic compounds and textile dyes in waste waters, and in bleaching and ...
Kristiina, Hildén   +2 more
openaire   +2 more sources

Laccases and their occurrence in prokaryotes

Archives of Microbiology, 2003
Laccases are copper-containing proteins that require O(2) to oxidize phenols, polyphenols, aromatic amines, and different non-phenolic substrates by one-electron transfer, resulting in the formation of reactive radicals. Although their specific physiological functions are not completely understood, there are several indications that laccases are ...
openaire   +2 more sources

Laccase activity and putative laccase genes in marine-derived basidiomycetes

Fungal Biology, 2010
Studies of laccases from marine-derived fungi are limited. In the present work, putative laccase genes from three marine-derived basidiomycetes and their laccase activities were evaluated. High amounts of laccase were produced by the fungal strains Marasmiellus sp. CBMAI 1062 (971.2UL⁻¹) and Peniophora sp.
Rafaella C, Bonugli-santos   +2 more
openaire   +2 more sources

Laccases: a never-ending story

Cellular and Molecular Life Sciences, 2009
Laccases (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
openaire   +4 more sources

Laccase and Laccase‐Mediated Systems in the Synthesis of Organic Compounds

Advanced Synthesis & Catalysis, 2014
AbstractLaccase, 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
openaire   +1 more source

Bacterial laccases

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
openaire   +1 more source

Laccase fromPleurotus ostreatus

Biotechnology Letters, 1986
Laccase 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
openaire   +2 more sources

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