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Protective effects of catalase indicate hydrogen peroxide involvement in hyaluronan degradation initiated by cu(ii) ions plus ascorbate in situ
Published in A. K. Haghi, Lionello Pogliani, Devrim Balköse, Omari V. Mukbaniani, Andrew G. Mercader, Applied Chemistry and Chemical Engineering, 2017
Katarina Valachova, Dominika Topolska, Raniero Mendichi, Jozef Rychly, Ladislav Soltes
Soltés et al.35, 39 and Rychlÿ et al.30 studied hyaluronan degradation induced by Cu(II) ions and hydrogen peroxide. The molecules of hydrogen peroxide are in vivo eliminated by peroxidases, especially by glutathione peroxidase, compounds containing thioredoxin, and catalase. Reaction products of hydrogen peroxide, including lipid hydroperoxides, are also biologically active.5, 6, 16, 20 Catalase is a common enzyme found in nearly all living organisms exposed to oxygen. It consists of four identical subunits, each containing a single heme for hydrogen peroxide decomposition to water molecules and molecular oxygen. The enzyme catalase is present in cytoplasma and peroxizomes.44, 67
Recent Advances in Artificial Cells With Emphasis on Biotechnological and Medical Approaches Based on Microencapsulation
Published in Max Donbrow, Microcapsules and Nanoparticles in Medicine and Pharmacy, 2020
In earlier studies we used a mouse model which, like humans, can have defects in the enzyme catalase. Catalase is an enzyme important in removing peroxides from the body. Artificial cells containing catalase injected into these mice effectively replaced the enzyme deficiency.31 Furthermore, bovine catalase in artificial cells did not produce immunological reaction on repeated injection into mice.32
Fiber and Filament Dyeing
Published in Tom Cassidy, Parikshit Goswami, Textile and Clothing Design Technology, 2017
The reaction rate is extremely fast and, under optimum conditions, 1 mole of catalase is able to decompose 500 million moles of hydrogen peroxide in 1 min. The catalase is free to decompose more hydrogen peroxide as long as both desired pH (6.5–7.5) and temperature (70°C–80°C) are maintained. The need to neutralize before adding the dye is beneficial because catalase is most active in the pH range of 6–8.
Partial characterization of Bacillus pumilus catalase partitioned in poly(ethylene glycol)/sodium sulfate aqueous two-phase systems
Published in Preparative Biochemistry and Biotechnology, 2019
Yonca Yuzugullu Karakus, Semih Isik
In this study, we reported a rapid and effective extraction of catalase from B. pumilus using the liquid-liquid partitioning with PEG/Na2SO4 system. The optimized system was composed of 15% (w/w) PEG4000, 10% (w/w) Na2SO4 and 3% (w/w) NaCl prepared at pH 5.0. Under those conditions, catalase was purified with 4.6 purification fold and 123% activity recovery by ATPS. Optimum temperature and pH values of the partitioned enzyme were measured as 37 °C and pH 7.0, respectively. Catalase enzyme revealed activity recovery at a range of 30–55 °C and pH 7.0–9.0. Km and Vmax of enzyme were estimated as 11 mM and 1667 µmole ml−1 min−1, respectively. AgNO3 was defined as strong inhibitor whereas 2.5% (v/v) DMSO was good solvent for the catalase enzyme. According to the data given above, it can be said that B. pumilus is a promising catalase source. After essential optimization studies conducted, ATPS can be used for purification of catalases. Taking into account of the biochemical characteristics of the purified enzyme, it has a potential for use in industrial applications.
Unveiling the significance of foliar-applied silicon, selenium and phosphorus for the management and remediation of arsenic in two different rice genotypes
Published in International Journal of Phytoremediation, 2023
Muhammad Mahroz Hussain, Nabeel Khan Niazi, Irshad Bibi, Fawad Ali, Fahad Al-Misned, Khalid Hussain, Muhammad Shahid, Abdul Rehman, Hailong Wang
Catalase (CAT) is an important enzyme that decomposes hydrogen peroxide to oxygen and water under oxidative stress. The results of this study revealed that plants growing under As-stress having no application of foliar treatments showed visible toxicity symptoms and increase in CAT activity (Figure 4c). Minimum CAT activity in both varieties, 30.52 and 32.42 µmol mg−1 protein in KSK-133 and Super Basmati, respectively, was observed with Si1.5 foliar application. Genotypic difference showed reduction in CAT activity by 40% and 42% in KSK-133 and Super Basmati, respectively. The average CAT activity was found to be 39.98 µmol mg−1 protein in KSK-133 genotype that was 1.5-fold higher than the Super Basmati.
Functionalised liquid crystal microfibers for hydrogen peroxide and catalase detection using whispering gallery mode
Published in Liquid Crystals, 2020
Rui Duan, Yanzeng Li, Yonggui Yuan, Lu Liu, Hanyang Li
Among these techniques, hydrogen peroxide usually combines with oxidase–peroxidase systems to serve as a reaction medium for screening these enzymes [11,12]. Catalase is a marker enzyme of peroxisomes, with hydrogen peroxide as the sole substrate, and accounts for approximately 40% of all peroxisomes [13]. The biological function of catalase is to promote the decomposition of excess hydrogen peroxide in the cell, thereby protecting the functional role of the antioxidant enzyme system. Therefore, the existence of catalase is of great significance for the metabolic activities of cells [13–15]. Due to the importance of catalase in cell life activities, it is important to design and improve the method for detecting catalase activity.