New highly robust divinyl benzene/acrylate polymer for immobilization of lipase CALB
Candida antartica lipase B (CALB) is the most versatile biocatalyst and is, therefore, widely used in industry. Its advantages range from thermostability, stereoselectivity, and activity in organic solvents to the acceptance of nucleophiles other than water. The actual standard for industrial applic...
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Veröffentlicht in: | European journal of lipid science and technology 2013-04, Vol.115 (4), p.468-472 |
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Zusammenfassung: | Candida antartica lipase B (CALB) is the most versatile biocatalyst and is, therefore, widely used in industry. Its advantages range from thermostability, stereoselectivity, and activity in organic solvents to the acceptance of nucleophiles other than water. The actual standard for industrial applications of CALB is the immobilized enzyme on Lewatit VP OC 1600 and is marketed under the name Novozym® 435. A new acrylic enzyme carrier (ECR1030) for the immobilization by adsorption of CALB and for use in batch or column reactors has been developed. The resin shows an activity of >9000 PLU/gDry, which is similar to Novozym® 435. Protein loading was 24.4 mg/gWet, and immobilizations yields higher than 90% were obtained. Unlike the resin used for the production of Novozym® 435, ECR1030 possesses high mechanical stability and is therefore more suitable for applications that expose the polymers to high mechanical stress, such as multiple reuses in stirred reactors.
Practical applications: Immobilized CALB is the biocatalyst used in the widest amount of industrial applications due to its broad selectivity and stability. It can be used for the manufacture of specialty chemicals such as surfactants, amides, chiral amines, alcohols, biodiesel, and polyesters. Its industrial use is in stirred tanks or packed columns, so high mechanical stability is needed together with high activity and sustainable costs.
ECR1030 is a DVB/acrylate polymer (300–700 µm) with high mechanical stability for use in batch or column reactors. No bead damages were observed even in harsh conditions (see Figure). Lipase CALB was immobilized on ECR1030M with >90% yield and activity of 10,000 PLU/gDry. |
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ISSN: | 1438-7697 1438-9312 |
DOI: | 10.1002/ejlt.201200419 |