laccase/borstkanker

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Enhanced thermostability and anticancer activity in breast cancer cells, of laccase immobilized on Pluronic®-stabilized nanoparticles.

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Laccases are multi-copper oxidase enzymes having widespread applications in various biotechnological fields. However, low stability of free enzymes restricts their industrial use. Development of effective methods to preserve and even increase the enzymatic activity is critical to maximize their use,

Purification and characterization of a laccase from the edible wild mushroom Tricholoma mongolicum.

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A novel laccase from Tricholoma mongolicum was purified by using a procedure which entailed ion exchange chromatography on DEAE-cellulose, CM-cellulose, Q-Sepharose, and FPLC-gel filtration on Superdex 75. The purified enzyme was obtained with a specific activity of 1480 U/mg-protein and a final

A laccase with antiproliferative and HIV-I reverse transcriptase inhibitory activities from the mycorrhizal fungus Agaricus placomyces.

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A novel 68 kDa laccase was purified from the mycorrhizal fungus Agaricus placomyces by utilizing a procedure that comprised three successive steps of ion exchange chromatography and gel filtration as the final step. The monomeric enzyme exhibited the N-terminal amino acid sequence of

A laccase-catalysed one-pot synthesis of aminonaphthoquinones and their anticancer activity.

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Nuclear monoamination of a 1,4-naphthohydroquinone with primary aromatic amines was catalysed by the commercial laccase, Novozym 51003, from Novozymes to afford aminonaphthoquinones. The synthesis was accomplished by reacting a mixture of the primary amine and 1,4-naphthohydroquinone in

A novel laccase with inhibitory activity towards HIV-I reverse transcriptase and antiproliferative effects on tumor cells from the fermentation broth of mushroom Pleurotus cornucopiae.

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A novel laccase with a molecular mass of 67 kDa was isolated from the fermentation broth of Pleurotus cornucopiae through ion exchange chromatography and gel filtration. The optimal pH and temperature for the laccase was pH 4.2 and 30°C, respectively. The laccase activity was remarkably inhibited by

Dextran-Curcumin Nanoparticles as a Methotrexate Delivery Vehicle: A Step Forward in Breast Cancer Combination Therapy.

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With the aim to effectively deliver methotrexate (MTX) to breast cancer cells, we designed a nanocarrier system (DC) derived from the self-assembly of a dextran-curcumin conjugate prepared via enzyme chemistry with immobilized laccase acting as a solid biocatalyst. Nanoparticles consisted of

Synthesis of Dextran-Phenoxodiol and Evaluation of Its Physical Stability and Biological Activity.

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Phenoxodiol, an isoflavene anti-tumor agent, was conjugated on the polysaccharide dextran using immobilized laccase as biocatalyst. The success of the enzymatic conjugation was determined by UV-vis spectrophotometry and its functionalization degree was assessed by ¹H NMR and was found to

Anticancer activities of vitamin K3 analogues.

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In a previous study we reported on the synthesis of 1,4-naphthoquinone-sulfides by thiolation of 1,4-naphthohydroquinones with primary aryl and alkyl thiols using laccase as catalyst. These compounds were synthesized as Vitamin K3 analogues. Vitamin K3 (VK3; 2-methyl-1,4-naphthoquinone; menadione)

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