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Radiochemistry for Preclinical Imaging Studies
Published in George C. Kagadis, Nancy L. Ford, Dimitrios N. Karnabatidis, George K. Loudos, Handbook of Small Animal Imaging, 2018
Chloramine-T slowly releases hypochlorite, which oxidizes iodide to form different sources of I+ depending on the reaction conditions (e.g., pH) (Coenen et al. 2006). To avoid excess chloramine-T in the solution, this agent has been immobilized on polymer beads (Pierce Iodination Beads, previously IODO-BEADS) or used as coating on the reaction vessel (Pierce Iodination Reagent, previously IODO-GEN) (Glaser et al. 2003; Adak et al. 2012). However, these in situ oxidation routes can still lead to side products with iodine inserted at different and/or multiple sites, with chlorine being introduced inadvertently into the substrate, and with inadvertent oxidation of susceptible parts of the substrate like methionine residues in a peptide (Coenen et al. 2006). The oxidation related problems are reduced with peracids at a low concentration, which serve as a milder oxidant. Also there is no chlorine present (Coenen et al. 2006). These peracids can be formed in situ from hydrogen peroxide and an organic acid, which transforms iodide probably into hypoiodate, IO−, providing formally I+. This is the preferred synthesis protocol. The oxidation reaction can be catalyzed by a peroxidase such as lactoperoxidase. This concept means that the oxidant concentration is low throughout the synthesis, which greatly reduces the probability of forming side products.
Dairy By-Products as Source of High Added Value Compounds
Published in Francisco J. Barba, Elena Roselló-Soto, Mladen Brnčić, Jose M. Lorenzo, Green Extraction and Valorization of By-Products from Food Processing, 2019
Noemí Echegaray, Juan A. Centeno, Javier Carballo
Lactoperoxidase is a glycoprotein with both bactericidal and bacteriostatic effects (Dajanta et al. 2008; Tayefi-Nasrabadi and Asadpour 2008) that represents 0.5% of the total whey proteins, varying its content with season and diet (Kussendrager and van Hooijdonk 2000). Because of the absence of caseins, whey is the preferential source for isolation and obtaining of this protein (Borzouee et al. 2016).
Downstream processing of lactoperoxidase from milk whey by involving liquid emulsion membrane
Published in Preparative Biochemistry and Biotechnology, 2018
B. S. Priyanka, Navin K. Rastogi
Lactoperoxidase catalyzes the oxidation of substrate thiocyanate (SCN−) in the presence of hydrogen peroxide (H2O2) leading to the production of antibacterial hypothiocyanite (OSCN−) and other related compounds. This oxidation product reduces the bacterial growth by acting on the cell membranes and inactivation of cytoplasmic enzymes.[4,5] This phenomenon renders LPO to be used as an alternate method for enhancing the shelf life of the raw milk during storage and transportation.[6,7] Besides, LPO finds its application as an antimicrobial agent in extending the shelf life of fish fillets under refrigerated storage.[8]
Nanoformulation approach for improved stability and efficiency of lactoperoxidase
Published in Preparative Biochemistry & Biotechnology, 2021
Lactoperoxidase (LPO) is a heme-containing glycosylated protein that separated at first time from cow milk and later was found in numerous exocrine excretions such as tears, airways and saliva. LPO shows a strong effect toward a broad range of pathogenic microbes that make it serves as a non-immunoglobulin protective ingredient. LPO also found to be produced by several glands including hardenian, lacrimal and salivary glands.[1–3] LPO is a candidate of the peroxidases family that converts the pseudohalides and halides in the existence of H2O2 (hydrogen peroxide) to strong oxidants compounds called hypohalous and hypothiocyanous acids, which have significant biocidal activities toward a wide range of pathogenic viruses and microbes, thereby LPO plays crucial roles in the immune system.[4–7] The mature LPO is composed of about 612 amino residues and consists of one chain of polypeptide that contains four to five sites of N-glycosylation and characterized by a carbohydrate level of 10%.[8] The mode of action of LPO against fungi, bacteria and viruses depends on many parameters involving the conformation and pH of tested media, the electron donor type, and the temperature of the experiment, besides LPO can demonstrate either biocidal activity, or inhibition ability to the glycolytic pathways, as well as protection the host cells from the cytopathic effects of viruses. Also, LPO shows an essential role in protecting the intestinal tract cells of neonates and the lactating mammary gland cells against numerous pathogenic microbes.[9–11] The antimicrobial activity of LPO to inhibit the growing of lactic acid streptococci in dairy products was established to be attributed to the presence of SCNˉ and H2O2. Subsequently, the studies revealed that LPO mediates its biocidal effect via a particular inhibitory system called LPO system (LPS) including LPO, SCNˉ and H2O2.[12,13] Furthermore, LPS shows a potential role in the innate immune response due to its activity is not restricted to the antimicrobial activity only, but LPS was found to be an active gradient to degrade the toxins such as aflatoxin.[14]