Abstract
In this work, a novel approach for lipase immobilization was exploited. Lipase from Burkholderia cepacia was encapsulated into κ-carrageenan by co-extrusion method to form a liquid core capsule. The diameter of the encapsulated lipase was found to be in the range of 1.3-1.8 mm with an average membrane thickness of 200 μm and 5% coefficient of variance. The encapsulation efficiency was 42.6% and 97% moisture content respectively. The encapsulated lipase was stable between pH 6 and 9 and temperature until 50 °C. The encapsulated lipase was stable until disintegration of the carrier when stored at 27 °C and retained 72.3% of its original activity after 6 cycles of hydrolysis of p-NPP. The encapsulated lipase was stable in various organic solvents including methanol, ethanol, iso-propanol, n-hexane and n-heptane. Kinetic parameters Km and Vmax were found to be 0.22 mM and 0.06 μmol/min for free lipase and 0.25 mM and 0.05 μmol/min for encapsulated lipase respectively.
Original language | English |
---|---|
Pages (from-to) | 78-83 |
Number of pages | 6 |
Journal | Journal of Molecular Catalysis B: Enzymatic |
Volume | 58 |
Issue number | 1-4 |
DOIs | |
Publication status | Published - Jun 2009 |
Externally published | Yes |
Keywords
- κ-Carrageenan
- Burkholderia cepacia lipase
- Co-extrusion
- Encapsulation
- Immobilization
- Liquid core capsule
- Stability