AI Article Synopsis
- Blends of 5% sodium alginate and 3% gelatin, cross-linked with glutaraldehyde and treated with calcium chloride, create strong and regular beads suitable for enzyme immobilization.
- Lipases from porcine pancreas and other sources were efficiently immobilized in these beads, retaining stability and activity over multiple uses in different media.
- The beads were modified with succinic anhydride to enhance their functionality, leading to a 7.4-fold purification of crude porcine pancreatic lipase through a simple pH-based protein binding and release process.
Article Abstract
Blends of natural polysaccharide sodium alginate (5%) with gelatin (3%) cross-linked with glutaraldehyde provide beads with excellent compressive strength (8 x 10(4) Pa) and regular structure on treatment with calcium chloride. Lipases from porcine pancreas, Pseudomonas cepacia, and Candida rugosa were immobilized in such a blend with excellent efficiency. The immobilized enzymes were stable and were reused several times without significant loss of enzyme activity both in aqueous and reverse micellar media. The beads were functionalized with succinic anhydride to obtain beads with extra carboxylic acid groups. These functionalized beads were then successfully used for 7.4-fold purification of crude porcine pancreatic lipase in a simple operation of protein binding at pH 5 and release at pH 8.5.
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| http://dx.doi.org/10.1021/bp010172f | DOI Listing |
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