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- W2009336874 abstract "Lactoperoxidase (LPO) belongs to the innate defence factors in human milk, saliva and tears. LPO is readily bound by bacterial cells and the bound enzyme preserves its antimicrobial activity. The properties of immobilized and soluble LPO were compared. LPO was covalently coupled to both CNBr-activated Sepharose 4B (aga-S4B) and Concanavalin A-Sepharose 4B (Con A-S4B). Immobilized LPOs were much more stable than soluble LPO both during storage at 4 °C and during heat inactivation at 60 °C. In guaiacol oxidation, Km values were two times higher for ConA-S4B than for aga-S4B and soluble LPO. In iodide oxidation, Km values for aga-S4B were 2.5 times lower than for ConA-S4B and soluble LPO. No difference was found in pH optimum between immobilized and soluble LPOs. Immobilized LPOs were less sensitive to cyanide inhibition than free LPO. Thus, solid LPO is more resistant to external factors than soluble LPO. The binding of LPO may be a favourable reaction considering its stability also in vivo." @default.
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- W2009336874 title "Immobilized lactoperoxidase as a biologically active and stable form of an antimicrobial enzyme" @default.
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- W2009336874 doi "https://doi.org/10.1016/0003-9969(81)90052-2" @default.
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