Optimization of lipase immobilization on nylon -6-grafted with PGMA polymer
Lipase from wheat germ was immobilized by covalent binding on a nylon -6- grafted with PGMA. This polymer was successfully activated with diethyl amine to intact with lipase enzyme molecule. Response surface methodology (RSM) was applied to model and optimize immobilization conditions for maximum...
| Main Authors: | , , |
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| Other Authors: | |
| Format: | Conference or Workshop Item |
| Language: | English |
| Published: |
Kulliyyah of Engineering, International Islamic University Malaysia
2016
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/47871/ http://irep.iium.edu.my/47871/ http://irep.iium.edu.my/47871/1/47871_Optimization_of_Lipase_Immobilization.pdf |
| Summary: | Lipase from wheat germ was immobilized by covalent binding on a nylon -6- grafted with PGMA. This
polymer was successfully activated with diethyl amine to intact with lipase enzyme molecule. Response
surface methodology (RSM) was applied to model and optimize immobilization conditions for maximum
activity and understanding the interaction of the factors affecting the activity of the immobilized enzyme. The
face centered central composite design (FCCCD) was applied to measure the effect of reaction pH (6-8),
reaction time (2-10 h) and enzyme concentration (1-2 mg) on enzyme activity. The result showed that pH,
time and enzyme concentration had significant effects on the activity of lipase enzyme. Based on the analysis,
the optimum immobilization conditions obtained were at pH 7, immobilization time 5 hours and enzyme
concentration 0.90 mg/ml.
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