Background: Bacterial lipoxygenase (EC 1.13.11.12, LOX) is an important enzyme used as a brightener and strengthening agent during breadmaking. In this study, thermal inactivation of a recombinant LOX of Pseudomonas aeruginosa BBE was characterized by kinetic and thermodynamic analysis in the absence and presence of additives.
Results: As the heating temperature increased from 25 to 55 °C, the thermal inactivation rate (k) values for LOX without the additives ranged from 0.0407 to 0.2627 min(-1), while the half-life (t1/2) values were between 17.08 and 3.25 min. The activation energy (ΔE) values were increased with rise in heating temperatures from 13.26 to 108.9 kJ mol(-1) . Separate tests at 45 °C in the presence of additives (polyols, sugars and ions) at specific concentrations showed that xylitol (1 mol L(-1)) was the most effective stabilizer for recombinant LOX and increased the t1/2 value by 297%.
Conclusion: Recombinant LOX was sensitive to heat treatment, and addition of polyols, sugars and ions could enhance its thermal stability. Our findings may provide useful information for stabilizing emerging bacterial LOXs.
Keywords: additive; bacterial lipoxygenase; kinetic; thermal inactivation; thermodynamics.
© 2013 Society of Chemical Industry.