Enzyme Catalyzed Synthesis of Fatty Monoethanolamides from Palm Kernel Oil Fractions
Fatty monoethanolamldes were synthesized In organic solvent from palm kernel olein (PKL) and palm kernel steann (PKS) using a lipase from Candida rugosa The transamldatlon reactions of PKL and PKS were enhanced In the presence of lipase Fatty monoethanolamldes were characterized by melting point...
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| Format: | Thesis |
| Language: | English English |
| Published: |
1998
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| Subjects: | |
| Online Access: | http://psasir.upm.edu.my/id/eprint/9438/1/FSAS_1998_29_A.pdf |
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| Summary: | Fatty monoethanolamldes were synthesized In organic solvent from
palm kernel olein (PKL) and palm kernel steann (PKS) using a lipase from
Candida rugosa The transamldatlon reactions of PKL and PKS were
enhanced In the presence of lipase Fatty monoethanolamldes were
characterized by melting point, spectroscopic (Infrared red and nuclear
magnetic resonance) and gas chromatography
The optimal Yield was achieved at reaction time 72 hours for both systems
With PKL and PKS as the substrates For PKL as the substrates, the optimal
reaction temperature was 40°C, whereas With PKS as the substrate no
optimum temperature was found (In the range of temperature studied) where
the relative Yield Increased With the Increasing temperature It suggested that
the temperature effect on the transamidation of PKS was more significant
compared to the transamidation for PKL In both systems the precipitation of high meltin g point fatty monoethanolamides hindered the progress of reactions.
Lipase functioned better in hydrophobic sol vents compared to hydrophilic
solvents. The best solvent for the reactions was isooctane. The increasing
amount of monoethanolamine used also resulted in the increase solubility of
the reactants and products, hence, increase the yield. For PKL, increasing the
mole ratio of PKL : monoethanolamine to 1:15 increased the relative yield to
4.45-fol d than the relative yield of that PKL : monoethanolamin e at mole ratio
1:1. However for PKS , its relative yield was only 2.5-fold more than the relative
yield of that PKS : monoethanolamine at mole ratio 1:1. The optimal ratio of
enzyme/PKL (or PKS) was 0.035. An excess of enzyme caused mass transfer
limitation. In the water activity studies, the preequilibrium and the direct salt
hydrate addition methods were used. Both observations were not in agreement
and did not show the actual effects of water activity in transamidation reactions.
The enzymes tend to aggregate and did not fully express its function. Th e
addition of support hardly improved the conditions. Overall, PKL always showed
the higher relative yield compared to PKS . At the optimum conditions, the yield
of PKL monoethanolamide was 77.64% and the yield of PKS
monoethanolamide was 39.32%. Kinetic studies also sh owed a cl ear
preference to PKL which its Km value 10-fold lower than that of PKS at room
temperature. |
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