Abstract
A continuous pulsed electric field (PEF) system integrated with six co-field flow PEF treatment chambers was used to study the inactivation of pepsin. The inactivation of pepsin activity was a function of applied electric field strength, electrical conductivity, and pH. The inactivation of pepsin by PEF followed a first-order model. The first-order inactivation kinetic constant of pepsin was 0.012 (1/mus) in 7.5 mM HCl (pH 2.0) at 34.2 kV/cm. Aggregation of pepsin was observed during PEF treatment; however, the inactivation took place before the formation of aggregates. Circular dichroism analysis showed that inactivation of pepsin by PEF was correlated to the loss of beta-sheet structure in a pepsin molecule. The relative residual activity of PEF-treated pepsin was correlated to the relative molar ellipticity at 215 nm. Both PEF- and heat-induced inactivation of pepsin were correlated with the alteration of the secondary structure (beta-sheet dominant structure) of pepsin.
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