Kinetics of digestive enzyme stability in the solid state. II. Quantitative prediction of enzyme inactivation.

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Abstract
The procedure for predicting digestive enzyme stability in the solid state was further investigated by utilizing the Weibull distribution function which needs 2 mathematically meaningful parameters, m and k. These parameters were estimated by graphic calculation. [The enzymes were microbial lipase from Aspergillus, Rhizopus sp. and Candida cylindracea, microbial .alpha.-amylase from A. oryzae; pancreatin from porcine pancreas and diastase from malt.] If the parameter m is independent of temperature, the Arrhenius plots are linear since k1/m is proportional to the inactivation rate constant. The parameter k was estimated by extrapolating to the desired temperature in the Arrhenius plots and the activation energy could be determined from the slope of this line. These parameters, m and k, made it possible to predict the inactivation ratio of enzymes in the solid state. By comparing the predicted value of the inactivation ratio with the observed value under controlled conditions, the proposed method is evidently accurate and useful for studies on enzyme stability in the solid state.

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