Lipase-Catalysed Synthesis of Fatty Aminoesters from Fatty Acids and Triethanolamine
Fatty aminoesters containing mixtures of mono-, di- and triaminoesters were prepared from the enzyme-catalysed esterification of fatty acids and triethanolamine in organic solvents. Screening of enzymes suitable for the reactions was carried out by conducting the esterification reaction in n-hex...
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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/9429/1/FSAS_1998_20_A.pdf |
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| Summary: | Fatty aminoesters containing mixtures of mono-, di- and triaminoesters
were prepared from the enzyme-catalysed esterification
of fatty acids and triethanolamine in organic solvents. Screening of
enzymes suitable for the reactions was carried out by conducting the
esterification reaction in n-hexane catalysed by 5 types of enzymes.
Lipozyme 1M and Novozym 435 gave positive results indicated by
the additional spots obtained on TLC analysis. FT1R analysis of the
products indicated the presence ester linkage at wavenumber 1740
cm-1. Reduction in transmittance of the hydroxyl group at 3500 cm-1
indicated the disappearance of the hydroxyl group which was originally on the triethanolamine molecule. Effects of some reaction
parameters such as time course, temperature, substrate mole ratio,
substrate concentration, amount of enzyme and thermodynamic
water activity were also investigated based on esterification of oleic
acid and triethanolamine catalysed by Lipozyme 1M and Novozym
435 in n-hexane.
Lipozyme 1M gave maximum conversion of 43.9% in 24
hours while Novozym 435 gave a maximum conversion of 37.34% in
6 hours. Optimum activity was obtained when the lipases catalyse
the reaction at 50oC, at substrate concentration of 1.0 M in n-hexane.
The lipases, however, behaved differently when preequilibrated in
salt hydrates of different thermodynamic water activity. Novozym
435 exhibited high esterification activity when preequilibrated in the
salt hydrates of lowest aw studied. On the other hand, Lipozyme 1M
exhibited optimum esterification activity when preequilibrated in
salts hydrates having aw value of 0.32. The activity of Lipozyme 1M
was drastically reduced when the mole of triethanolamine was
increased while Novozym 435 gave optimum activity when the
substrates were reacted at 1:1 mole ratio. In addition, when the oleic. |
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