Activation and Characterization of Trypsin-Treated LipaseZiqin Liu and Huihua Huang*
Department of Food Science and Technology, South China University of Technology, Wushan Road 381,Guangzhou 510641, China
- *Corresponding Author:
- Huihua Huang
Department of Food Science and Technology
South China University of Technology, Wushan Road 381
Guangzhou 510641, China
E-mail: [email protected]
Received date: October 11, 2011; Accepted date: November 19, 2011; Published date: December 02, 2011
Citation:Liu Z, Huang H(2012) Activation and Characterization of Trypsin-Treated Lipase. J Food Process Technol 3:133. doi:10.4172/2157-7110.1000133
Copyright: © 2012 Liu Z, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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.