2006/11/01 by R. Soliva-Fortuny, Robert Soliva‐Fortuny, S. Bendicho-Porta +2 · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Engineering · Mathematics · Medicine · #Analytical Chemistry (journal) #Biochemistry #Biological system #Biology #Chemistry #Chromatography #Electric field #Electrohydrodynamics and Fluid Dynamics #Enzyme #Intensity (physics) #Kinetics #Lipase #Materials science #Mathematics #Microbial Inactivation Methods #Optics #Physics #Plasma Applications and Diagnostics #Pseudomonas fluorescens #Residual #Statistics #Weibull distribution
paper · pdf · doi:10.3168/jds.s0022-0302(06)72455-9
openalex publication_date 2006/11/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
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.