Thermal inactivation kinetics (D- and z-values) of the algal protein, R-phycoerythrin (R-PE), were studied under different buffer conditions (pH 4.0, 7.0, and 10.0) and concentrations of sucrose, sodium dodecyl sulfate (SDS), urea, and 2-mercaptoethanol (ME). R-PE solutions were heated in capillary tubes at temperatures between 40 and 90 degrees C depending on buffer conditions. Thermal inactivation parameters for R-PE, calculated on the basis of fluorescence loss, were modified by addition of chemicals. Overall, sucrose and ME had a thermostabilizing effect, while SDS and urea decreased thermal stability of R-PE. The z-values ranged from 5.9 degrees C in 50 mM NaCl, 20 mM glycine buffer, pH 10.0, to 37.8 degrees C in 60% sucrose, 50 mM NaCl, 20 mM phosphate buffer, pH 7.0. The z-values obtained for R-PE closely matched the z-values of some target microorganisms in food processes, suggesting R-PE might be used as a time-temperature integrator to verify thermal processing adequacy.
Fluorescence Hot Temperature