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• Jijakli, M.H.; Lepoivre, P. State of the Art and Challenges of Post-harvest Disease Management in Apples. In Disease Management in Fruits and Vegetables; Mukerij, K.G., Ed.; Springer Netherlands: Cham, The Netherlands, 2004; Volume 1, pp. 59-94
• Snini, S.P.; Tannous, J.; Heuillard, P.; Bailly, S.; Lippi, Y.; Zehraoui, E.; Barreau, C.; Oswald, I.P.; Puel, O. Patulin is a cultivar-dependent aggressiveness factor favouring the colonization of apples by Penicillium expansum. Mol. Plant Pathol. 2016, 17, 920-930
• Sanzani, S.M.; Reverberi, M.; Punelli, M.; Ippolito, A.; Fanelli, C. Study on the role of patulin on pathogenicity and virulence of Penicillium expansum. Int. J. Food Microbiol. 2012, 153, 323-331
• ANSES. étude Nationale de Surveillance des Expositions Alimentaires aux Substances Chimiques-2e étude de L'alimentation Totale 2006-2010 (EAT 2). Tome 1: Contaminants Inorganiques, Minéraux, Polluants Organiques Persistants, Mycotoxines et Phyto-Estrogènes; ANSES: Buenos Aires, Argentina, 2011
• Tenovuo, J.; Makinen, K.K.; Sievers, G. Antibacterial effect of lactoperoxidase and myeloperoxidase against Bacillus cereus. Antimicrob. Agents Chemother. 1985, 27, 96-101
• Bjorck, L.; Claesson, O. Correlation between concentration of hypothiocyanate and antibacterial effect of the lactoperoxidase system against Escherichia coli. J. Dairy Sci. 1980, 63, 919-922
• Oram, J.D.; Reiter, B. The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. The effect of the inhibitory system on susceptible and resistant strains of group N streptococci. Biochem. J. 1966, 100, 373-381
• Bafort, F.; Parisi, O.; Perraudin, J.-P.; Jijakli, M.H. Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review. Enzyme Res. 2014, 2014, 517164
• Aune, T.M.; Thomas, E.L. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Eur. J. Biochem. 1977, 80, 209-214
• Thomas, E.L.; Aune, T.M. Peroxidase-catalyzed oxidation of protein sulfhydryls mediated by iodine. Biochemistry 1977, 16, 3581-3586
• Bafort, F.; Parisi, O.; Perraudin, J.-P.; Jijakli, M.H. The Lactoperoxidase System: A Natural Biochemical Biocontrol Agent for Pre-and Postharvest Applications. J. Phytopathol. 2017, 165, 22-34
• Pruitt, K.M.; Tenovuo, J.O. The lactoperoxidase system: Chemistry and biological significance. Immunol. Ser. 1985, 27, 96-101
• Ahariz, M.; Courtois, P. Candida albicans susceptibility to lactoperoxidase-generated hypoiodite. Clin. Cosmet. Investig. Dent. 2010, 2, 69-78
• Fonteh, F.A.; Grandison, A.S.; Lewis, M.J. Variations of lactoperoxidase activity and thiocyanate content in cows' and goats' milk throughout lactation. J. Dairy Res. 2002, 69, 401-409
• Kussendrager, K.D.; van Hooijdonk, A.C. Lactoperoxidase: Physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 2000, 84 (Suppl. 1), S19-S25
• Boots, J.W.; Floris, R. Lactoperoxidase: From catalytic mechanism to practical applications. Int. Dairy J. 2006, 16, 1272-1276
• van Hooijdonk, A.C.; Kussendrager, K.D.; Steijns, J.M. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defence. Br. J. Nutr. 2000, 84 (Suppl. 1), S127-S134
• Lenander-Lumikari, M.; Tenovuo, J.; Mikola, H. Effects of a lactoperoxidase system-containing toothpaste on levels of hypothiocyanite and bacteria in saliva. Caries Res. 1993, 27, 285-291
• Kirstila, V.; Lenander-Lumikari, M.; Soderling, E.; Tenovuo, J. Effects of oral hygiene products containing lactoperoxidase, lysozyme, and lactoferrin on the composition of whole saliva and on subjective oral symptoms in patients with xerostomia. Acta Odontol. Scand. 1996, 54, 391-397
• Gil-Montoya, J.A.; Guardia-Lopez, I.; Gonzalez-Moles, M.A. Evaluation of the clinical efficacy of a mouthwash and oral gel containing the antimicrobial proteins lactoperoxidase, lysozyme and lactoferrin in elderly patients with dry mouth-A pilot study. Gerodontology 2008, 25, 3-9
• Ihalin, R.; Loimaranta, V.; Lenander-Lumikari, M.; Tenovuo, J. The effects of different (pseudo)halide substrates on peroxidase-mediated killing of Actinobacillus actinomycetemcomitans. J. Periodontal Res. 1998, 33, 421-427
• Bafort, F.; Barthelemy, J.-P.; Parisi, O.; Perraudin, J.-P.; Jijakli, H. Development of a colorimetric method for the dosage of OI-anions and I2 in aqueous media. Commun. Agric. Appl. Biol. Sci. 2014, 79, 155-160
• WHO; UNICEF; ICCIDD. Assessment of Iodine Deficiency Disorders and Monitoring Their Elimination. A Guide for Programme Managers; WHO Press: Geneva, Switzerland, 2007
• Nagy, P.; Alguindigue, S.S.; Ashby, M.T. Lactoperoxidase-catalyzed oxidation of thiocyanate by hydrogen peroxide: A reinvestigation of hypothiocyanite by nuclear magnetic resonance and optical spectroscopy. Biochemistry 2006, 45, 12610-12616
• Bafort, F.; Damblon, C.; Smargiasso, N.; De Pauw, E.; Perraudin, J.-P.; Jijakli, M.H. Reaction product variability and biological activity of the lactoperoxidase system depending on medium ionic strength and pH, and on substrate relative concentration. Chem. Biodivers. 2018, 15, e170049
• Arlandson, M.; Decker, T.; Roongta, V.A.; Bonilla, L.; Mayo, K.H.; MacPherson, J.C.; Hazen, S.L.; Slungaard, A. Eosinophil peroxidase oxidation of thiocyanate. Characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. J. Biol. Chem. 2001, 276, 215-224
• Bosch, E.H.; van Doorne, H.; de Vries, S. The lactoperoxidase system: The influence of iodide and the chemical and antimicrobial stability over the period of about 18 months. J. Appl. Microbiol. 2000, 89, 215-224
• Schlorke, D.; Flemmig, J.; Birkemeyer, C.; Arnhold, J. Formation of cyanogen iodide by lactoperoxidase. J. Inorg. Biochem. 2016, 154, 35-41
• Sebaa, S.; Faltot, M.; De Breucker, S.; Boucherit-Otmani, Z.; Bafort, F.; Perraudin, J.-P.; Courtois, P. Ex vivo decontamination of yeast-colonized dentures by iodine-thiocyanate complexes. Clin. Cosmet. Investig. Dent. 2018, 10, 149-158
• Aune, T.M.; Thomas, E.L. Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion. Biochemistry 1978, 17, 1005-1010
• Thomas, E.L.; Aune, T.M. Lactoperoxidase, peroxide, thiocyanate antimicrobial system: Correlation of sulfhydryl oxidation with antimicrobial action. Infect. Immun. 1978, 20, 456-463
• Thomas, E.L.; Aune, T.M. Oxidation of Escherichia coli sulfhydryl components by the peroxidase-hydrogen peroxide-iodide antimicrobial system. Antimicrob. Agents Chemother. 1978, 13, 1006-1010
• Prütz, W.A.; Kissner, R.; Nauser, T.; Koppenol, W.H. On the oxidation of cytochrome c by hypohalous acids. Arch. Biochem. Biophys. 2001, 389, 110-122
• Prütz, W.A.; Kissner, R.; Koppenol, W.H.; Rüegger, H. On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids. Arch. Biochem. Biophys. 2000, 380, 181-191
• Ashby, M.T. Chapter 8-Hypothiocyanite. Adv. Inorg. Chem. 2012, 64, 263-303
• Magnusson, R.P.; Taurog, A.; Dorris, M.L. Mechanism of iodide-dependent catalatic activity of thyroid peroxidase and lactoperoxidase. J. Biol. Chem. 1984, 259, 197-205
• Ferrari, R.P.; Ghibaudi, E.M.; Traversa, S.; Laurenti, E.; De Gioia, L.; Salmona, M. Spectroscopic and binding studies on the interaction of inorganic anions with lactoperoxidase. J. Inorg. Biochem. 1997, 68, 17-26
• Long, C.; Skoog, D.A. A Thiocyanate Complex of Iodine(I). Inorg. Chem. 1966, 5, 206-210
• Gottardi, W. Iodine and disinfection: Theoretical study on mode of action, efficiency, stability, and analytical aspects in the aqueous system. Arch. Pharm. 1999, 332, 151-157
• Bichsel, Y.; Von Gunten, U. Oxidation of iodide and hypoiodous acid in the disinfection of natural waters. Environ. Sci. Technol. 1999, 33, 4040-4045
• Bichsel, Y.; Von Gunten, U. Hypoiodous acid: Kinetics of the buffer-catalyzed disproportionation. Water Res. 2000, 34, 3197-3203
• Holm, K.A. Automated determination of microbial peroxidase activity in fermentation samples using hydrogen peroxide as the substrate and 2, 20-azino-bis(3-ethylbenzothiazoline-6-sulfonate) as the electron donor in a flow injection system. Analyst 1995, 120, 2101-2105
• Marcozzi, G.; Di Domenico, C.; Spreti, N. Effects of surfactants on the stabilization of the bovine lactoperoxidase activity. Biotechnol. Prog. 1998, 14, 653-656
• Arnhold, J.; Monzani, E.; Furtmüller, P.G.; Zederbauer, M.; Casella, L.; Obinger, C. Kinetics and thermodynamics of halide and nitrite oxidation by mammalian heme peroxidases. Eur. J. Inorg. Chem. 2006, 19, 3801-3811
• Battistuzzi, G.; Bellei, M.; Vlasits, J.; Banerjee, S.; Furtmüller, P.G.; Sola, M.; Obinger, C. Redox thermodynamics of lactoperoxidase and eosinophil peroxidase. Arch. Biochem. Biophys. 2010, 494, 72-77
• Furtmüller, P.G.; Arnhold, J.; Jantschko, W.; Zederbauer, M.; Jakopitsch, C.; Obinger, C. Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase. J. Inorg. Biochem. 2005, 99, 1220-1229