Journal of Agricultural and Food Chemistry vol:47 issue:7 pages:2950-2958
Inactivation of commercially available orange pectinesterase (PE) was investigated under isothermal and isothermal-isobaric conditions. In both cases, inactivation data could be accurately described by a fractional conversion model. The influence of enzyme concentration, pH, Ca2+ concentration, and sucrose on the inactivation kinetics was studied. Enzyme stability against heat and pressure increased by increasing enzyme concentration. An increased Ca2+ concentration caused sensitization to temperature and increased the residual fraction active PE after thermal treatment. To the contrary, in the case of pressure treatment, decreasing Ca2+ concentrations increased pressure inactivation. The remaining fraction active PE after pressure treatment was not influenced by the addition of Ca2+ ions. Acidification accelerated thermal as well as pressure-temperature inactivation, whereas in the presence of sucrose an increased temperature and pressure stability of orange PE was observed. Sucrose had no influence on the remaining activity after thermal treatment, but it increased the residual fraction after pressure treatment. The remaining fraction was for all additives studied independent of the pressure and temperature level applied except for the inactivation in an acid medium, when a decrease of the residual fraction was observed with increasing temperature and pressure.