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High-efficiency detoxification of fumonisin B<sub>1</sub>, B<sub>2</sub> and B<sub>3</sub> by laccase Lac-W with ABTS. [PDF]
Xu K +8 more
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Gold Nanoparticles Coated With Hydrophobin-ProteinA Fusion Protein: Development of a Versatile Immunosensing Platform. [PDF]
Cicatiello P +5 more
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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
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
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
openaire +2 more sources
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
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
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
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
Laccase activity and putative laccase genes in marine-derived basidiomycetes
Fungal Biology, 2010Studies 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
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Laccases from Aureobasidium pullulans
Enzyme and Microbial Technology, 2013Laccases are polyphenol oxidases (EC 1.10.3.2) that have numerous industrial and bioremediation applications. Laccases are well known as lignin-degrading enzymes, but these enzymes can play numerous other roles in fungi. In this study, 41 strains of the fungus Aureobasidium pullulans were examined for laccase production. Enzymes from A.
Joseph O, Rich +4 more
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