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Biologically Triggered Injectable Hydrogels as Intelligent Scaffolds
Published in Gilson Khang, Handbook of Intelligent Scaffolds for Tissue Engineering and Regenerative Medicine, 2017
Yoon Ki Joung, Kyung Min Park, Ki Dong Parkc
Peroxidase catalysis is an oxidation of a donor to an oxidized donor through the action of hydrogen peroxide, liberating two water molecules.23 Several studies have focused on an interesting enzyme of peroxidase species. Horseradish peroxidase (HRP) is a single-chain α-type hemoprotein that catalyzes the decomposition of hydrogen peroxide at the expense of aromatic proton donors.24 HRP is a Fe containing porphyrin-type structure that catalyzes the coupling of a number of phenol and aniline derivatives using hydrogen peroxide as the oxidant. Figure 11.1 shows the catalytic cycle of HRP for a phenol substrate.
Nanobiosensors
Published in Vinod Kumar Khanna, Nanosensors, 2021
Horseradish peroxidase (HRP) is one of the heme-containing redox enzymes, with a molecular weight of approximately 42,000 Da. The electron transfer converts Fe(III) in the heme of HRP to Fe(II). This process catalyzes some chemical reactions, such as the reduction of H2O2. Unfortunately, strong adsorption of HRP onto the electrode surface causes denaturation. On the other hand, the electrochemically active centers in HRP are always buried deeply in its extended three-dimensional structure, which makes direct electron transfer between HRP and the electrode surface very difficult.
Multiple effects of sodium dodecyl sulfate on chromogenic catalysis of tetramethylbenzidine with horseradish peroxidase
Published in Journal of Dispersion Science and Technology, 2021
Meng Li, Yifan He, Hong Meng, Yinmao Dong, Yazhuo Shang, Honglai Liu, Zhaohui Qu, Youting Liu
Horseradish peroxidase (HRP) is one of the most commonly used oxidoreductase extracted from roots of horseradish. It consists of catalytic active center heme and proteins encapsulated outside, which are both essential for the activity of HRP.[25] HRP can catalyze various of aromatic amine and phenolic compounds oxidation in the presence of H2O2 to produce chromogenic reaction,[26] which endows HRP with widespread applications in enzyme linked immunosorbent assay (ELISA) and colorimetric sensors.[27–29] Therein, HRP/3,3',5,5'-tetramethylbenzidine (TMB) system is the most commonly used color developing agent in immunoassay detection due to its lower toxicity and higher sensitivity of the system. Joseph et al. studied the catalytic mechanism of TMB catalyzed by HRP in presence of H2O2 in buffer solution in detail.[30] As Chart 1 presented that the oxidation of TMB by HRP/H2O2 system yields two kind of colored products. The one is the intermediate products named diamine/diimine electron transfer complex that is a kind of positively charged blue chromogen. However, the blue chromogen is unstable and gradually transforms into the other colored product in acetate buffer at pH of 5.0, namely yellow diimine end-product.
Immobilization of horseradish peroxidase on lysine-functionalized gum Arabic-coated Fe3O4 nanoparticles for cholesterol determination
Published in Preparative Biochemistry & Biotechnology, 2021
Morteza Varamini, Hajar Zamani, Hale Hamedani, Sepide Namdari, Banafsheh Rastegari
Horseradish peroxidase (HRP) (E.C. 1.11.1.7), which is one of the top rate metalloenzymes that plays role in oxidizing numerous compounds from organic to inorganic origin in the presence of hydrogen peroxide.[1] Horseradish peroxidase has been proven to be useful tool in biotechnology.[2] In fact, this enzyme has several applications in environmental (e.g., wastewater treatment)[2] and biological fields (e.g., biosensors) as well as food industry.[3] Additional merit of HRP is its activity in broad range of pH.[4]