Abstract
Effect of trypsin hydrolysis on lipase in activation, characteristics and change in thermal stability were studied. Lipase was found to be increased in activity from 584U mL -1 to 759U mL -1 via trypsin treatment at the concentration of 1.5mg mL -1 , 30°C and p H 7.0 for 30min. The trypsin-treated lipase showed a lower K m value (79mg mL -1 olive oil substrate) than the native lipase (100mg mL -1 ), indicating an improved affinity for olive oil substrate. The optimum p H value of the trypsin-treated lipase maintained basically unchanged while the optimum temperature (45°C) showed lower than the native lipase (50°C). The half-inactivation time for the trypsin-treated lipase at 45°C, 50°C and 60°C was calculated as 131min, 35.5min and 4min respectively, while for the native lipase at 50°C and 60°C was calculated as 128min and 13min respectively, indicating that the thermal stability of lipase is lowered after trypsin treatment.
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