Characterization of the three-phase partitioned laccase from Trametes versicolor strain with antiproliferative activity against breast cancer cells.

An extracellular laccase from T. versicolor was 20.4-fold purified by three-phase partitioning with high recovery (245 %) and biochemically characterized in detail for the first time.

Investigation of how gate residues in the main channel affect the catalytic activity of Scytalidium thermophilum catalase.

Catalase is an antioxidant enzyme that breaks down hydrogen peroxide (HO) into molecular oxygen and water. In all monofunctional catalases the pathway that HO takes to the catalytic centre is via the `main channel'. However, the structure of this channel differs in large-subunit and small-subunit catalases.

Probing the role of Val228 on the catalytic activity of Scytalidium catalase.

Scytalidium catalase is a homotetramer including heme d in each subunit. Its primary function is the dismutation of HO to water and oxygen, but it is also able to oxidase various small organic compounds including catechol and phenol. The crystal structure of Scytalidium catalase reveals the presence of three linked channels providing access to the exterior like other catalases reported so far.

Characterization of polyphenol oxidase from fennel (Foeniculum vulgare Mill.) seeds as a promising source.

Fennel seeds were recognized as a promising polyphenol oxidase (PPO) source upon investigating some edible green plants (carob, jujube, coriander, fennel, and licorice). The fennel PPO enzyme was purified by three-phase partitioning and biochemically characterized in detail for the first time. The purification fold and activity recovery values were determined as 20-fold and 120%, respectively.

Partial characterization of Bacillus pumilus catalase partitioned in poly(ethylene glycol)/sodium sulfate aqueous two-phase systems.

Aqueous two-phase partitioning system (ATPS) was used to extract and purify catalase from Bacillus pumilus. The system parameters for effective purification of catalase were optimized. The best catalase recovery (123%) with a 4.

Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase.

The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigate this, the crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole (3TR) was determined at 1.