The inactivation of pancreatic lipase by heat

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Abstract
A purified lipase was prepared by adsorptions on Al(OH)3. The heat-inactivation process on this purified lipase was unimolecular. The lipase had an optimum stability at pH 6.0. The critical increment was about 46,000 calories for the heat-inactivation process in 50% glycerol at the pH values: 5.1, 6.0, and 8.01. Unpurified extracts were most stable in the region of pH 6.0. At pH 6.0 in 50% glycerol the critical increment for the process in unpurified extracts was 57,500 calories (for 80% glycerol, the value was 102,000).

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