Modeling high-intensity pulsed electric field inactivation of a lipase from Pseudomonas fluorescens.
The inactivation kinetics of a lipase from Pseudomonas fluorescens (EC 3.1.1.3.) were studied in a simulated skim milk ultrafiltrate treated with high-intensity pulsed electric fields. Samples were subjected to electric field intensities ranging from 16.4 to 27.4 kV/cm for up to 314.5 micros, thus achieving a maximum inactivation of 62.1%. The suitability of describing experimental data using mechanistic first-order kinetics and an empirical model based on the Weibull distribution function is discussed. In addition, different mathematical expressions relating the residual activity values to field strength and treatment time are supplied. A first-order fractional conversion model predicted residual activity with good accuracy (A(f) = 1.018). A mechanistic insight of the model kinetics was that experimental values were the consequence of different structural organizations of the enzyme, with uneven resistance to the pulsed electric field treatments. The Weibull model was also useful in predicting the energy density necessary to achieve lipase inactivation.
Soliva-Fortuny
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Departament de Tecnologia d'Aliments, TPV-CeRTA, Universitat de Lleida, Alcalde Rovira Roure 191, 25198, Lleida, Spain.
Bendicho-Porta
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Martín-Belloso
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O
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D004560:Electricity; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000737:chemistry / Q000378:metabolism*; D008892:Milk / Q000737:chemistry / Q000201:enzymology / Q000382:microbiology*; D008954:Models, Biological; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D014462:Ultrafiltration
D001426:Bacterial Proteins; D008071:Lipoprotein Lipase