ABSTRACTHeat inactivation of pectinesterase in juice pulp was nonlinear suggesting the presence of fractions of pectinesterase with differing heat stabilities. The residual activity rapidly decreased to 4 upon heating for 19 sec at 80°C and decreased very little upon subsequent heating for up to 180 sec at 80°C. The D values (time to inactivate 90 of the enzyme) at 90°C of the heat sensitive and heat stable fractions were estimated to be 0.225 and 32 sec, respectively. The Z values (change in temperature to achieve a 10‐fold change in time of inactivation) were estimated to be 10.8°C and 6.5°C for the sensitive and stable fractions, respec
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