The immobilization of candida rugosa lipase on the chitosan beads
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Date
2018-06
Authors
Muliati Mohd Romli
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Abstract
The immobilized enzyme is an important catalyst which used mainly to increase
the rate of reaction. One of the methods to immobilize the enzyme is by covalent
bonding. In the present research, Candida rugosa (C. rugosa) lipase was successfully
immobilized by the method of covalent bonding onto activated chitosan beads. The
immobilization of lipase on the chitosan beads was confirmed by determining lipase
activity during hydrolysis of a standard substance. The effect of lipase and
glutaraldehyde (GA) concentrations on immobilization yield and activity yield were
investigated. In general, the concentration of GA and lipase gave significant effect on
immobilization yield and activity yield. As the GA concentration increase, the activity
yield was decreased, while as the lipase concentration increase, the immobilization yield
relatively decrease. The highest immobilization yield was 77.335 %, were achieved at 6
% of GA and 0.001 g/mL of C. rugosa lipase. After that, the highest activity was
50.3613 IU, where obtained at 2 % of GA and 0.010 g/mL of C. rugosa lipase.
The optimization of immobilization process parameters was carried out via
Respond Surface Method (RSM). It has been found that the most optimal condition for
immobilization was at 4 % glutaraldehyde concentration and 0.005 g/mL of C. rugosa
lipase which gave 65.14 % of immobilization yield and 32.84 IU of unit activity. The
immobilized lipase was used repeatedly in the hydrolysis reaction. It was found that the
immobilized enzyme was more stable and has the ability to be used multiple times.
Therefore, immobilization of lipase onto activated chitosan support was feasible and it
can be reused for 7 times. However, the activities reduce to 53.67 % after the 7th cycle.