Spectroscopic study of lipase from Candida rugosa immobilized onto calcined layered double hydroxides
Lipase from Candida rugosa (CRL) was adsorbed onto three calcined layered double hydroxide (CLDH); Mg/Al-NO3 (CMAN), Ni/Al-NO3- (CNAN) and Zn/Al-NO3- (CZAN). Scanning Electron Microscopy-Energy Dispersive X-ray Spectroscopy (SEM-EDX) and protein staining-light microscopy analyses were applied to pr...
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| Main Authors: | , , , , , |
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| Format: | Conference or Workshop Item |
| Language: | English |
| Published: |
2007
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| Online Access: | http://psasir.upm.edu.my/id/eprint/8738/1/ID%208738.pdf http://psasir.upm.edu.my/id/eprint/8738/ |
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| Institution: | Universiti Putra Malaysia |
| Language: | English |
| Summary: | Lipase from Candida rugosa (CRL) was adsorbed onto three calcined layered double hydroxide (CLDH); Mg/Al-NO3 (CMAN), Ni/Al-NO3- (CNAN) and Zn/Al-NO3- (CZAN). Scanning Electron Microscopy-Energy Dispersive X-ray Spectroscopy (SEM-EDX) and protein staining-light microscopy analyses were applied to provide direct spectroscopic and microscopic evidence for the adsorption of CRL onto CLDH. SEM-EDX spectra show CRL presence in CMAN-CRL, CNAN-CRL and CZAN-CRL prepared. Blue spots on the surface of CMAN-CRL, CNAN-CRL and CZAN-CRL stained with Coomasie Blue R confirm protein adsorption onto supports. The catalytic activity of all three CLDH-CRL was also evaluated in synthesis of methyl caprylate and results showed that CMAN-CRL and CNAN-CRL exhibited 70 % conversion while CZAN-CRL exhibited 80 % conversion compared to free lipase that exhibited only 6 % conversion only. |
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