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Thermodynamics study of immobilized lipase in farnesyl laurate production /Rima Syafida Ismail

Thermodynamics study of immobilized lipase in farnesyl laurate production_Rima Syafida Ismail_K4_2011_875003824_NI
Kajian termodinamik tentang lipase tersekatgerak kormersil telah dilakukan dalam usaha untuk mengkarakterisasi aktiviti dan kestabilan enzim sesuai dengan pengaruh suhu. Di dalam penyelidikan ini, tindakbalas pengesteran dalam pelarut organik bermangkinkan lipase tersekatgerak telah dikaji untuk sintesis farnesil laurat. Didapati Lipozyme RM IM daripada sumber Rhizomucor miehei adalah biokatalis paling efektif dan iso-oktana telah dipertimbangkan sebagai pelarut paling sesuai untuk proses pengesteran ini. Suhu optimum 45C diperoleh pada tindak balas ini. Penurunan kadar tindakbalas melebihi suhu optimum menunjukkan kejadian enzim ternyahaktif boleh diterbalikkan. Kajian termodinamik pada penyahaslian enzim lipase menunjukkan pola urutan pertama kinetik dengan kestabilan yang cukup melalui masa yang ditunjukkan oleh lipase juga. Tenaga pengaktifan dan penyahaktifan adalah 55.62 kJ mol-1 and 84.05 kJ mol-1, masing-masing, mengandaikan lebih banyak tenaga dikehendaki untuk penyahaslian enzim tidak dapat dibalikkan semula berlaku. ___________________________________________________________________________________ Thermodynamics studies on commercial immobilized lipase have been carried out in order to characterize enzyme activity and stability corresponding to temperature effect. In the present work, esterification reaction in organic solvent catalyzed by immobilized lipase was studied for the synthesis of farnesyl laurate. Lipozyme RM IM origin from Rhizomucor miehei was found to be the most effective biocatalyst and iso-octane was considered the most suitable solvent for this esterification process. An optimum temperature of 45⁰C was obtained in this reaction. The decreasing reaction rates beyond the optimum temperature indicated the occurrence of reversible enzyme deactivation. Thermodynamics studies on lipase denaturation exhibited a first-order kinetics pattern with considerable stability through time shown by the lipase as well. The activation and deactivation energies were 55.62 kJ mol-1 and 84.05 kJ mol-1, respectively, implying more energy was required for the irreversible denaturation of the enzyme occur.
Contributor(s):
Rima Syafida Ismail - Author
Primary Item Type:
Final Year Project
Identifiers:
Accession Number : 875003824
Language:
English
Subject Keywords:
lipase ; farnesyl laurate ; iso-octane
First presented to the public:
4/1/2011
Original Publication Date:
8/27/2020
Previously Published By:
Universiti Sains Malaysia
Place Of Publication:
School of Chemical Engineering
Citation:
Extents:
Number of Pages -
License Grantor / Date Granted:
  / ( View License )
Date Deposited
2020-08-27 14:23:17.479
Submitter:
Nor Hayati Ismail

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