When immersed in milk, breakfast cereal easily take up moisture, lose their brittle texture and become soggy. Earlier comparative analysis of the moisture sorption by breakfast cereal immersed in water and milk indicated that milk solids might play an important role on the sorption kinetics. In this work, the moisture uptake by ready-to-eat corn breakfast cereal immersed in milk solutions, reconstituted from whole and skimmed milk powder, was measured under isothermal conditions at 5, 30 and 55°C. Dilutions between 0.25 and 1.5 were tested, with the factor of dilution 1 corresponding to the standard recommended by the milk powder manufacturer. The Weibull probabilistic model adequately fitted the experimental data by appropriate choice of its variable parameters. The dependence of the model parameters on temperature and total solids concentration was assessed for both skimmed and whole milk. Fat was found to play a major role on the process mechanism, which was attributed to the deposition of a fat layer at the solid matrix surface, hindering water and solids uptake. Yet, for short times, moisture uptake proceeded at a similar rate both in skimmed and whole milk.

Thermal deactivation kinetics of horseradish peroxidase (HRP) were studied from 45 to 90 degrees C in phosphate buffer and 5-25% (v,w/v) 1-butyl-3-methylimidazolium tetrafluoroborate [BMIM][BF4] and 1-butyl-3-methylimidazolium chloride [BMIM][Cl]. HRP activity at 25 degrees C was not affected by the presence of ionic liquids up to 20% (v,w/v). Increasing the ionic liquids concentration up to 25% (v,w/v) changed the biphasic character of deactivation kinetics to an apparent single first-order step. The presence of 5-10% (v/v) [BMIM][BF4] significantly improved HRP thermal stability with lower activation energies for the deactivation second phase (83-87 kJ mol(-1)). After deactivation, enhanced activity regain of the enzyme, up to 70-80% of the initial activity, was found in 25% (v/v) [BMIM][BF4] and 10% (w/v) [BMIM][Cl] and correlated to prevalence of the deactivation first phase.

No abstract

The effects of different alkyl chain lengths of ionic liquids 1-ethyl-, 1-butyl- and 1-hexyl-3-methylimidazolium chloride, on the catalytic activity, thermal stability and deactivation kinetics of horseradish peroxidase were studied in the temperature range of 45-85 °C. The presence of 1-ethyl- and 1-butyl-ionic liquids up to 25% (w/v) did not affect significantly the enzyme activity at 25 °C, whereas the addition of 1-hexyl-solvent resulted in lower activity of enzyme. Typical biphasic deactivation profiles were obtained and adequately fitted by a bi-exponential equation. When increasing ionic liquids concentration up to 25% (w/v), the second phase of deactivation became more prominent, till leading to apparent first-order kinetics. Occurrence of activity regain, following thermal deactivation was found, reaching up 60-80% of the initial activity, especially in 1-hexyl-3-methylimidazolium chloride. Activity regain was particularly noticeable in the first phase of deactivation. Temperature sensitivity of the Soret band maxima indicated that the enzyme prepared in buffer or 1-hexyl-3-methylimidazolium chloride had similar conformational changes in the haem region, but no correlations were found with activity decrease.

Enzymatic browning due to the action of polyphenoloxidase (PPO) is highly undesirable and efficient methodologies to avoid/reduce it are of great interest for food industry. The effect of a pressure pretreatment (100 MPa, 15 min, room temperature) on the activity of PPO extracts obtained from three apple cultivars (Bravo de Esmolfe [BE], Reineta [RN], and Golden delicious [GD]), and subsequent thermal inactivation kinetics was evaluated, as a way to more efficiently achieve thermal inactivation of PPO. The effect of pH on PPO activity was also assessed to define the value at which carry out the thermal inactivation of PPO. The enzymatic activity decreased in the order BE, RN, and GD. Two log‐linear ranges ([62.5–72.5] °C and [72.5–80.0] °C) of D‐value with temperature were found. The pressure pretreatment caused enhanced stability within the range of 62.5–67.5 °C, caused no changes at 70.0–72.5 °C, and decreased the stability at 75.0–80.0 °C (e.g., at 75 °C the D‐values for BE, GD, and RN ranged, respectively, from 25.6/27.3, 14.5/18.6, and 8.8/10.4, after/before the pressure pretreatment) and increased thermal sensitivity (decreased the z‐value), particularly in the lower temperature range studied (up to 72.5 °C). Practical applications Knowledge of PPO activity level and its thermal resistance for different cultivars is of interest to develop efficient and optimized enzymatic browning control by thermal treatments. Sequential combination of low intensity pressure treatments followed by thermal treatments can be an interesting approach to enhance enzyme inactivation. In this work was found that after a low intensity pressure pretreatment (100 MPa, 15 min), apple PPO temperature stability could be reduced, since a lower stability (lower D‐values) and increased sensitivity toward temperature (lower z‐value) was systematically found for PPO thermally inactivated at T > 72.5 °C. These findings are of interest for a more efficient PPO inactivation for enhanced browning control.