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, 30oC and pH7.0 for 30min. The trypsin-treated lipase showed a lower Km value (79mg mL-1 olive oil substrate) than the native lipase (100mg mL-1), indicating an improved affinity for olive oil substrate. The optimum pH value of the trypsin-treated lipase maintained basically unchanged while the optimum temperature (45oC) showed lower than the native lipase (50oC). The half-inactivation time for the trypsin-treated lipase at 45oC, 50oC and 60oC was calculated as 131min, 35.5min and 4min respectively, while for the native lipase at 50oC and 60oC was calculated as 128min and 13min respectively, indicating that the thermal stability of lipase is lowered after trypsin treatment.
Highlights
Enzymes play more and more important roles in modern food industry and attract much attention for their potential industrial applications [1]
Trypsinogen does not exhibit catalytic activity before a six-peptide is removed from the molecule via protease hydrolysis [3] and the activity of asparaginase can be increased four to five folds after its 10 or more amino acid residues are removed from its carboxyl terminal through trypsin hydrolysis [4,5]
The aim of this paper is to find out the effect of trypsin hydrolysis on the activity of lipase
Summary
Enzymes play more and more important roles in modern food industry and attract much attention for their potential industrial applications [1]. As a protein, enzyme is usually limited to its activity, stability and reaction conditions in catalytic reaction. Appropriate modification to increase the activity and stability of enzyme is essential for applications, such as genetic engineering, immobilization and/or process alterations, chemical modification of enzyme molecules [2]. As an effective modification method, limited hydrolysis can usually result in some beneficial change for an enzyme in chain and conformation and can alter the characteristics and functions of the enzyme. Limited hydrolysis of enzyme via the role of protease belongs to the method of enzyme modification, through which the activity and other properties of enzyme, such as the affinity toward substrates, the optimum reaction condition and heat-reliability, may get beneficially changed due to the modification of molecular structure. The change of the trypsin-treated lipase, including the enzymatic properties and thermal stability are characterized
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