2012
DOI: 10.1016/j.foodchem.2011.07.001
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Kinetic and thermodynamic study of thermal inactivation of the antimicrobial peptide P34 in milk

Abstract: a b s t r a c tThe knowledge on thermal inactivation of biopreservatives in a food matrix is essential to allow their proper utilisation in food industry, enabling the reduction of heating times and optimisation of heating temperatures. In this work, thermal inactivation of the antimicrobial peptide P34 in skimmed and fat milk was kinetically investigated within the temperature range of 90-120°C. The inactivation kinetic follows a first-order reaction with k-values between 0.071 and 0.007 min À1 in skimmed mil… Show more

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Cited by 36 publications
(19 citation statements)
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“…where, where A/A° is the residual enzyme activity at time t (min), and k (min −1 ) is the inactivation rate constant at a determined temperature . Half‐life (t 1/2 ) of inactivation is calculated using equation : truenormalt1/2=ln4pt(2)4pt/4ptk …”
Section: Methodsmentioning
confidence: 99%
“…where, where A/A° is the residual enzyme activity at time t (min), and k (min −1 ) is the inactivation rate constant at a determined temperature . Half‐life (t 1/2 ) of inactivation is calculated using equation : truenormalt1/2=ln4pt(2)4pt/4ptk …”
Section: Methodsmentioning
confidence: 99%
“…As the α parameter was considered a kinetic constant dependent on the temperature according to the Arrhenius equation, the activation energy (E a ) for the extraction processes, which may be described as the energy barrier that bioactive compounds need to cross in order to be removed from the orange byproduct matrix, was estimated. The E a figure may depend on different factors in the extraction process, such as the food matrix, the target biocompounds, the sample pretreatment, and the solvent used, among others [36]. The estimated E a for CE extractions of TPC, TFC and AA were of 62,900, 48,100, and 66,300 J/mol, respectively.…”
Section: Cementioning
confidence: 99%
“…where, where A/A8 is the residual enzyme activity at time t (min), and k (min À1 ) is the inactivation rate constant at a determined temperature. [75] Half-life (t 1/2 ) of inactivation is calculated using equation (2):…”
Section: Thermostability Study For Free Lipase and Lipase Immobilizedmentioning
confidence: 99%