Results 161 to 170 of about 11,695 (199)

Specific immobilization of laccase onp-benzoquinone-activated supports

Biology of Metals, 1990
A specific immobilization of laccase (EC 1.10.3.2) onto a ready-to-usep-benzoquinone-activated agarose support is described. The single-step procedure leads to a laccase protein coupling of I8% and an enzyme activity immobilization yield of 27%, while the retained specific activity of the immobilized enzyme was 150% of the specific activity of the free
Mateescu MA, AGOSTINELLI, Enzo, Weltrowska G, Weltrowski M, MONDOVI', Bruno   +4 more
openaire   +2 more sources

Assay for Laccase activity by microcalorimetry: Laccase was extracted from China lacquer of Rhus vernicifera

Journal of Biochemical and Biophysical Methods, 2000
The reactions between Laccase (extracted from China lacquer of Rhus vernicifera) and various substrates (3,4-Dihydroxybenzaldehyde, Guaiacol, Pyrogallol, Gallic acid) have been studied using LKB-2107 batch microcalorimetry system. Based on calorimetry, a new method has been proposed. Laccase activity and the Michaelis constant K(m) have been determined
T, Wang, W, Li, H W, Wan, P J, Zhou, S S, Qu   +4 more
openaire   +2 more sources

Laccase activity in soils: Considerations for the measurement of enzyme activity

Chemosphere, 2012
Laccases (benzenediol: oxygen oxidoreductases, EC 1.10.3.2) are copper-containing enzymes that catalyze the oxidative conversion of a variety of chemicals, such as mono-, oligo-, and polyphenols and aromatic amines. Laccases have been proposed to participate in the transformation of organic matter and xenobiotics as well as microbial interactions ...
Ivana, Eichlerová, Jaroslav, Šnajdr, Petr, Baldrian   +2 more
openaire   +2 more sources

Laccase-catalyzed synthesis of optically active polyaniline

Synthetic Metals, 2007
One step, simple and environmentally friendly enzymatic synthesis of optically active polyaniline in the bulk solution and on the surface of glass slides (in situ deposition) was developed. Fungal laccase from Trametes hirsuta was used as the catalyst of the oxidative polymerisation of aniline.
I.S. Vasil’eva, O.V. Morozova, G.P. Shumakovich, S.V. Shleev, I.Yu. Sakharov, A.I. Yaropolov   +5 more
openaire   +1 more source

Activation of laccase by penicillin and derivatives

Process Biochemistry, 2006
Abstract Capable of oxidizing a wide range of reducing substances, laccase has a great potential for various biocatalytic applications. Extensive research effort is being made for improving laccase's activity, specificity, and stability. We observed that pre-incubating with penicillin led to a significant activation of a Rhizoctonia solani laccase,
Darron Ransbarger, Feng Xu
openaire   +1 more source

Laccase Activity in Trichoderma virens

2011
Fungal laccases are involved in multiple functions, such as lignin degradation, pigments (melanin) synthesis and degradation, detoxification and pathogenesis. Furthermore, they are useful biocatalysts for several biotechnological applications.The laccase gene function was previously analysed in Trichoderma virens, an effective biocontrol agent: six ...
Mannella L., Guglielminetti L., Vannacci G., VERGARA, Mariarosaria   +3 more
openaire   +2 more sources

Optimization of a Small Laccase by Active‐Site Redesign

ChemBioChem, 2013
Small but faster: A small laccase from Streptomyces coelicolor (SLAC) has been engineered by structure-based design and site-directed mutagenesis to improve the activity on commercially relevant substrates. The variants generated showed up to 40-fold increased efficiency on 2,6-dimethoxyphenol and the ability to use mediators with considerably higher ...
Miguel D, Toscano, Leonardo, De Maria, Sune, Lobedanz, Lars H, Ostergaard   +3 more
openaire   +2 more sources

Enhanced laccase activity of biocatalytic hybrid copper hydroxide nanocages

Enzyme and Microbial Technology, 2019
Nanobiocatalysis is the combination of the unique properties of nano-sized materials and the efficiency and sophistication of catalytic properties of enzymes. In this work, Cu(OH)2 nanocages with an mean size of 170 nm were synthesized and used as a support for the covalent conjugation with fungal ligninolytic enzymes; versatile peroxidase and laccase.
Omar Silva-Torres, Luis Bojorquez-Vazquez, Andrey Simakov, Rafael Vazquez-Duhalt   +3 more
openaire   +2 more sources

Activity and stability of laccase in conjugation with chitosan

International Journal of Biological Macromolecules, 2005
Laccase is one of a few enzymes that can directly reduce oxygen into water under ambient conditions, while oxidizing a variety of aromatic compounds. Its conjugation with chitosan generates a pH-sensitive functional biomaterial that changes its solubility in response to pH variation.
Gary, Delanoy, Qing, Li, Jian, Yu
openaire   +2 more sources

Dihydrobenzofuran Neolignanamides: Laccase-Mediated Biomimetic Synthesis and Antiproliferative Activity

Journal of Natural Products, 2016
The biomimetic synthesis of a small library of dihydrobenzofuran neolignanamides (the natural trans-grossamide (4) and the related compounds 21-28) has been carried out through an eco-friendly oxidative coupling reaction mediated by Trametes versicolor laccase.
N. Cardullo, L. Pulvirenti, C. Spatafora, N. Musso, BARRESI, VINCENZA, CONDORELLI, Daniele Filippo, TRINGALI, Corrado   +6 more
openaire   +3 more sources