1. ComparativeStudy on Lipases Immobilized onto Bentoniteand Modified Bentonites and Their Catalytic Properties.
- Author
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Dong, Huaping, Li, Yimin, Li, Jianfa, Sheng, Guodong, and Chen, Hua
- Subjects
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LIPASES , *BENTONITE , *CATALYTIC activity , *MOLECULAR structure , *HYDROPHOBIC compounds , *SURFACE active agents , *ADSORPTION (Chemistry) , *COMPARATIVE studies - Abstract
Thehydrophobic property and structure of Na-bentonite (Na-bent)were tuned by intercalation with cationic surfactants for lipase adsorption.The adsorption isotherms of lipase on Na-bent and modified bentonitesdemonstrated Langmuir-type shape, and Na-bent showed higher adsorptionefficiency than modified bentonites. The observed overlap of lipasemolecules on the support and the interactions between these moleculesunder high protein loading caused the reduction in the activity ofimmobilized lipase. The immobilized lipases on modified bentonites(Bent-DTAB-lipase, Bent-CTAB-lipase, and Bent-OTAB-lipase) exhibitedhigher catalytic activity than that on Na-bent, due to the hydrophobicallyinterfacial activation of modified bentonites toward lipase. The highestcatalytic activity and stability were observed on Bent-CTAB-lipase,resulting from the tunable hydrophilic/hydrophobic balance of thesupport’s surface, while the excessive hydrophobic propertyshowed negative influence on lipase’s catalytic performance.The immobilized lipases onto modified bentonites with hydrophobicproperty showed higher thermal stability and reusability than Na-bent-lipase. [ABSTRACT FROM AUTHOR]
- Published
- 2013
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