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Optimization of thermal processes relies on adequate degradation kinetic models to warrant food safety and quality. The knowledge on thermal inactivation kinetics of antimicrobial peptides is necessary to allow for their adequate use as natural biopreservatives in the food industry. In this work, thermal inactivation of the previously characterized bacteriocin-like inhibitory substance (BLIS) P34 was kinetically investigated within the temperature range of 90-120 degrees C. Listeria monocytogenes ATCC 7644 was used as the indicator microorganism for antimicrobial activity. Applicability of various inactivation models available in the literature was critically evaluated. The first-order model provided the best description of the kinetics of inactivation over the selected temperatures, with k values between 0.059 and 0.010 min(-1). D and k values decreased and increased, respectively, with increasing temperature, indicating a faster inactivation at higher temperatures. Results suggest that BLIS P34 is thermostable, with a z value of 37.74 degrees C and E(a) of 72 kJ mol(-1).

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