Abstract
Ricinoleic acid estolide was produced by using free and immobilized Candida rugosa lipase at moderate temperature in a bioreactor. This work describes the immobilization of C. rugosa lipase on 10 different supports by covalent binding and physical adsorption, and how of the most suitable immobilized derivative was selected. The comparison was mainly based on the enzyme content and on the activity results. An anion exchange resin was judged to be the most appropriate support and the corresponding immobilization process was investigated and optimized. Although repeated batch reactions using the same derivative are not entirely advisable, the reaction proceeds at a noticeably slower rate and the degree of condensation reached is lower when the same amount of protein as in the derivative is added to the bioreactor in native form.
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