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Effect of Heat Treatment on Buffalo (Bubalus bubalis) Lactoperoxidase Activity in Raw Milk

Author(s): H. Tayefi-Nasrabadi | R. Asadpour

Journal: Journal of Biological Sciences
ISSN 1727-3048

Volume: 8;
Issue: 8;
Start page: 1310;
Date: 2008;
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Keywords: Buffalo milk | lactoperoxidase | thermal denaturation

Inactivation kinetics of buffalo milk lactoperoxidase toward thermal processes was studied at isothermal condition over a range of 67 to 71°C. The analysis of inactivation rate constant data for the process of thermal denaturation of lactoperoxidase showed good agreement with a first-order reaction. Based on the thermal death time model, which describes first-order heat inactivation kinetics in the area of food processing and preservation, D-values and z-value (2.45°C) were obtained. Thermodynamic parameters were also calculated. The high values obtained for activation energy (920.43 kJ mol-1) and change in enthalpy of activation (~917 kJ mol-1) indicate that lactoperoxidase is one of the most heat stable enzymes in buffalo milk which high amount of energy is needed to initiate its denaturation. The mean buffalo lactoperoxidase activity in raw milk also was found 16.84 U mL-1.
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