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Effect of Heat Treatment on Bovine Lactoperoxidase Activity in Skim Milk: Kinetic and Thermodynamic Analysis
Author(s) -
Marín E.,
Sánchez L.,
Pérez M.D.,
Puyol P.,
Calvo M.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb14120.x
Subject(s) - lactoperoxidase , chemistry , enthalpy , denaturation (fissile materials) , activation energy , kinetic energy , reaction rate constant , skimmed milk , thermodynamics , kinetics , chromatography , enzyme , organic chemistry , nuclear chemistry , food science , peroxidase , physics , quantum mechanics
The effect of heat on lactoperoxidase activity in bovine milk was studied over a range of 68 to 76 °C. Values of residual enzymatic activity after different treatments were studied by kinetic analysis, obtaining D‐values and the Z‐value (3.1 °C). Denaturation of lactoperoxidase, measured by loss in activity, can be described as a 1st‐order reaction. Rate constants were calculated, as was the energy of activation, which was 737.69 kJ/mol. Thermodynamic parameters were also calculated. The high value obtained for the variation in enthalpy of activation indicates that a high amount of energy is required to initiate denaturation, probably due to the molecular conformation of lactoperoxidase.