Lactoperoxidase properties

Carmen, M., Hernandez, M., van Markwijk, B.W., and Vreeman, H.J. 1990. Isolation and properties of lactoperoxidase from bovine milk. Neth. Milk Dairy J. 44, 213-221. 

Kussendrager, K.D. and van Hooijdonk, A.C. 2000. Lactoperoxidase physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 84, S19—S25. 

Wong, C.W., Watson, D.L., Regester, G.O., and Smithers, G.W. 1998b. Comparison of immunomodulatory properties of purified lactoferrin, lactoperoxidase and (3-casein in sheep. J. Dairy Res. 65, 697-701. 

Polis, B. D. and FI. W. Shmuhler Crystalline Lactoperoxidase I. Isolation by displacement chromatography. II. Physicochemical and enzymatic properties. J. Biol. Chem. 201, 475 (1953). 

The functional properties of milk proteins in foods have recently been expertly treated by Holt and Roginski (2001). These authors described the antihypersensitive, opioid, immunomodulatory, and calcium-binding milk peptides, the antiviral properties of various milk components, and the antimicrobial activity of lactoperoxidase, lactoferrin, lactoferricins, casein peptides, and peptides from a-lactalbumin. 

During the trial, feed samples were taken weekly and analyzed for ehemical-nutritional features. Individual DMI and milk yield were measured daily, and representative milk samples from morning milking were collected every 3-4 d and analyzed for fat, protein, lactose, urea and titratable acidity (FT120, Foss Electric, Denmark) SCC (Fossomatic, Foss Electric) rermeting properties (Formawin, Foss Electric) AR measured either on raw milk either on milk after pasteurization (80 °C x 10 ) (Calamari et al., 2003) some milk enzymes involved in the antimicrobial activity of milk or related to the udder health (GOT, GOT, LDH, lactoperoxidase and xanthine oxidase) (Calamari etal., 2003). Fecal samples were also collected at the end of each period and analyzed for pH and DM. 

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