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Published in Yannick Guari, Joulia Larionova, Prussian Blue-Type Nanoparticles and Nanocomposites, 2019
A technically interesting property of Prussian blue is its ability to catalyze the reduction of hydrogen peroxide [57]. This property can be used in glucose biosensors, as shown in 1994 by Russian chemist Arkady A. Karyakin and coworkers. They presented research on electrodes modified with glucose oxidase and Prussian blue as a selective electrocatalyst for hydrogen peroxide reduction [58]. Glucose oxidase produces hydrogen peroxide from glucose. Hydrogen peroxide can be detected electrochemically at Prussian blue with high sensitivity and selectivity. Therefore, they denoted Prussian blue as an “artificial peroxidase” [59]. Later, many oxidase enzymes other than glucose oxidase have been coupled to Prussian blue modified electrodes to expand the possible use of Prussian blue sensors to many other analytes, such as cholesterol, oxalate, galactose, or glutamate to name but a few [60]. Prussian blue is also an excellent material as a sensor for some electroinactive cations such as potassium [61] or ammonium [62] because of its selective intercalation property. The use of Prussian blue as an active material for sensors is still a hot research topic [63].
Biomems
Published in Simona Badilescu, Muthukumaran Packirisamy, BioMEMS, 2016
Simona Badilescu, Muthukumaran Packirisamy
Electrowetting-based digital microfluidics platforms to assay glucose in physiological samples have been developed. A colorimetric enzyme-kinetic method based on Trinder’s reaction is used for the determination of glucose concentration. Glucose is enzymatically oxidized to gluconic acid and hydrogen peroxide in the presence of glucose oxidase. The hydrogen peroxide reacts with 4-amino antipyrine (4-AAP) and N-ethyl-N-sulfopropyl-m-toluidine (TOPS) in the presence of peroxidase (EC 1.11.1.7) to form violet-colored quinoneimine, which has an absorbance peak at 545 nm, as shown in Figure 9.52.
Reusable Microencapsulated Enzymes for the Clinical Laboratory
Published in Franklin Lim, Biomedical Applications of Microencapsulation, 2019
Glucose oxidase-peroxidase — Glucose oxidase catalyzes the production of hydrogen peroxide from glucose and oxygen. Peroxidase then transfers oxygen from the hydrogen peroxide to oxygen acceptor, aminophenozone, which reacts with phenol forming a chromagen. A stock solution containing 25 of liquidified phenol, 5 mℓ of aminophenazone reagent (0.6 mg aminophenazone per milliliter water), 0.2 mℓ of 1 g/dl glucose and 10 mℓ water was prepared. To 500 µℓ of this solution in a cuvette at 37°C, 10 µℓ of capsule suspension or 100 µℓ of supernate was added and the change in absorbance at 510 nm followed for 10 min.
Extremozymes used in textile industry
Published in The Journal of The Textile Institute, 2022
Priyanka Kakkar, Neeraj Wadhwa
Bleaching is important wet processing to remove any natural pigment and provide pure white cotton fibers. Glucose oxidase enzyme is used for the bleaching of cotton fibers and the process is called biobleaching. In the presence of oxygen, glucose oxidase enzyme oxidise the glucose molecule into gluconic acid and hydrogen peroxide. Catalase, laccase is used to remove the left behind hydrogen peroxide called bleach cleanup. Small amount of catalase is sufficient to convert it into hydrogen and oxygen as shown in Figure 2. Catalase only acts on the hydrogen peroxide present on the fabric and the other material remain unharmed. Enzymatic cleaning of peroxide is eco-friendly and use less water by avoiding extensive washing and less energy consumption (Shahid et al., 2016), (Roy Choudhury, 2020). Geobacillus thermo pakistaniensis is used to isolate catalase and laccase (Basheer et al., 2017; Shaeer et al., 2019). Recombinant enzyme of catalase has been produced by encoding the gene CAT responsible for cold adaptive catalytic activity in psychrophile and its hetrogenous expression in E.coli. It is active in wide range of temperature form 20 to 70 °C (Sarmiento et al., 2015). Biopolishing is the process to remove fuzz and pilling from the fabric surface. Cellulase enzyme is used to treat the fabric surface. It makes the fabric texture smoother, better appearance, color brightness, and improves water absorbing property. Controlled enzymatic treatments optimise the surface properties of the fabric but may result in decrease in tensile strength which is commercially acceptable (Roy Choudhury, 2020).
Complexes of glucose oxidase with chitosan and dextran possessing enhanced stability
Published in Preparative Biochemistry & Biotechnology, 2020
Ecem Baykal, Gokay Vardar, Azade Attar, Melda Altikatoglu Yapaoz
Glucose oxidase (GOD) is an enzyme of the class of oxidoreductase which is produced by fermentation from Aspergillus and Penicillium species.[16] GOD is a commercial enzyme that occurs between β-D-glucose and hydrogen peroxide, which ultimately catalyzes the reaction of D-glucono-δ-lactone.[17] GOD is widely used in many areas such as bioelectrochemical applications,[18] cancer therapy,[19] photocatalysis,[20] biosensing,[21] and drug delivery[22] due to its high durability and affordable price rather than various enzymes.